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. 1989 Jun;53(2):210–230. doi: 10.1128/mr.53.2.210-230.1989

Common themes in microbial pathogenicity.

B B Finlay, S Falkow
PMCID: PMC372728  PMID: 2569162

Abstract

A bacterial pathogen is a highly adapted microorganism which has the capacity to cause disease. The mechanisms used by pathogenic bacteria to cause infection and disease usually include an interactive group of virulence determinants, sometimes coregulated, which are suited for the interaction of a particular microorganism with a specific host. Because pathogens must overcome similar host barriers, common themes in microbial pathogenesis have evolved. However, these mechanisms are diverse between species and not necessarily conserved; instead, convergent evolution has developed several different mechanisms to overcome host barriers. The success of a bacterial pathogen can be measured by the degree with which it replicates after entering the host and reaching its specific niche. Successful microbial infection reflects persistence within a host and avoidance or neutralization of the specific and nonspecific defense mechanisms of the host. The degree of success of a pathogen is dependent upon the status of the host. As pathogens pass through a host, they are exposed to new environments. Highly adapted pathogenic organisms have developed biochemical sensors exquisitely designed to measure and respond to such environmental stimuli and accordingly to regulate a cascade of virulence determinants essential for life within the host. The pathogenic state is the product of dynamic selective pressures on microbial populations.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Abraham S. N., Beachey E. H., Simpson W. A. Adherence of streptococcus pyogenes, Escherichia coli, and Pseudomonas aeruginosa to fibronectin-coated and uncoated epithelial cells. Infect Immun. 1983 Sep;41(3):1261–1268. doi: 10.1128/iai.41.3.1261-1268.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Abraham S. N., Sun D., Dale J. B., Beachey E. H. Conservation of the D-mannose-adhesion protein among type 1 fimbriated members of the family Enterobacteriaceae. Nature. 1988 Dec 15;336(6200):682–684. doi: 10.1038/336682a0. [DOI] [PubMed] [Google Scholar]
  3. Aho K., Leirisalo-Repo M., Repo H. Reactive arthritis. Clin Rheum Dis. 1985 Apr;11(1):25–40. [PubMed] [Google Scholar]
  4. Akporiaye E. T., Rowatt J. D., Aragon A. A., Baca O. G. Lysosomal response of a murine macrophage-like cell line persistently infected with Coxiella burnetii. Infect Immun. 1983 Jun;40(3):1155–1162. doi: 10.1128/iai.40.3.1155-1162.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Allweiss B., Dostal J., Carey K. E., Edwards T. F., Freter R. The role of chemotaxis in the ecology of bacterial pathogens of mucosal surfaces. Nature. 1977 Mar 31;266(5601):448–450. doi: 10.1038/266448a0. [DOI] [PubMed] [Google Scholar]
  6. Anderson B. J., Mattick J. S., Cox P. T., Kristo C. L., Egerton J. R. Western blot (immunoblot) analysis of the fimbrial antigens of Bacteroides nodosus. J Bacteriol. 1987 Sep;169(9):4018–4023. doi: 10.1128/jb.169.9.4018-4023.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Bagg A., Neilands J. B. Molecular mechanism of regulation of siderophore-mediated iron assimilation. Microbiol Rev. 1987 Dec;51(4):509–518. doi: 10.1128/mr.51.4.509-518.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Ballantyne G. H., Fitzsimons E. J. Acute hypoferremia following cardiac surgery. Am Surg. 1984 Aug;50(8):450–453. [PubMed] [Google Scholar]
  9. Baltimore R. S., Duncan R. L., Shapiro E. D., Edberg S. C. Epidemiology of pharyngeal colonization of infants with aerobic gram-negative rod bacteria. J Clin Microbiol. 1989 Jan;27(1):91–95. doi: 10.1128/jcm.27.1.91-95.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Baudry B., Kaczorek M., Sansonetti P. J. Nucleotide sequence of the invasion plasmid antigen B and C genes (ipaB and ipaC) of Shigella flexneri. Microb Pathog. 1988 May;4(5):345–357. doi: 10.1016/0882-4010(88)90062-9. [DOI] [PubMed] [Google Scholar]
  11. Baudry B., Maurelli A. T., Clerc P., Sadoff J. C., Sansonetti P. J. Localization of plasmid loci necessary for the entry of Shigella flexneri into HeLa cells, and characterization of one locus encoding four immunogenic polypeptides. J Gen Microbiol. 1987 Dec;133(12):3403–3413. doi: 10.1099/00221287-133-12-3403. [DOI] [PubMed] [Google Scholar]
  12. Bavoil P., Ohlin A., Schachter J. Role of disulfide bonding in outer membrane structure and permeability in Chlamydia trachomatis. Infect Immun. 1984 May;44(2):479–485. doi: 10.1128/iai.44.2.479-485.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Beltran P., Musser J. M., Helmuth R., Farmer J. J., 3rd, Frerichs W. M., Wachsmuth I. K., Ferris K., McWhorter A. C., Wells J. G., Cravioto A. Toward a population genetic analysis of Salmonella: genetic diversity and relationships among strains of serotypes S. choleraesuis, S. derby, S. dublin, S. enteritidis, S. heidelberg, S. infantis, S. newport, and S. typhimurium. Proc Natl Acad Sci U S A. 1988 Oct;85(20):7753–7757. doi: 10.1073/pnas.85.20.7753. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Bergström S., Robbins K., Koomey J. M., Swanson J. Piliation control mechanisms in Neisseria gonorrhoeae. Proc Natl Acad Sci U S A. 1986 Jun;83(11):3890–3894. doi: 10.1073/pnas.83.11.3890. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Betley M. J., Miller V. L., Mekalanos J. J. Genetics of bacterial enterotoxins. Annu Rev Microbiol. 1986;40:577–605. doi: 10.1146/annurev.mi.40.100186.003045. [DOI] [PubMed] [Google Scholar]
  16. Bisno A. L. Alternate complement pathway activation by group A streptococci: role of M-protein. Infect Immun. 1979 Dec;26(3):1172–1176. doi: 10.1128/iai.26.3.1172-1176.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Black C. M., Paliescheskey M., Beaman B. L., Donovan R. M., Goldstein E. Acidification of phagosomes in murine macrophages: blockage by Nocardia asteroides. J Infect Dis. 1986 Dec;154(6):952–958. doi: 10.1093/infdis/154.6.952. [DOI] [PubMed] [Google Scholar]
  18. Blackwell J. M., Ezekowitz R. A., Roberts M. B., Channon J. Y., Sim R. B., Gordon S. Macrophage complement and lectin-like receptors bind Leishmania in the absence of serum. J Exp Med. 1985 Jul 1;162(1):324–331. doi: 10.1084/jem.162.1.324. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Blaser M. J., Smith P. F., Repine J. E., Joiner K. A. Pathogenesis of Campylobacter fetus infections. Failure of encapsulated Campylobacter fetus to bind C3b explains serum and phagocytosis resistance. J Clin Invest. 1988 May;81(5):1434–1444. doi: 10.1172/JCI113474. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Boelaert J. R., van Landuyt H. W., Valcke Y. J., Cantinieaux B., Lornoy W. F., Vanherweghem J. L., Moreillon P., Vandepitte J. M. The role of iron overload in Yersinia enterocolitica and Yersinia pseudotuberculosis bacteremia in hemodialysis patients. J Infect Dis. 1987 Aug;156(2):384–387. doi: 10.1093/infdis/156.2.384. [DOI] [PubMed] [Google Scholar]
  21. Brenner D. J., Mayer L. W., Carlone G. M., Harrison L. H., Bibb W. F., Brandileone M. C., Sottnek F. O., Irino K., Reeves M. W., Swenson J. M. Biochemical, genetic, and epidemiologic characterization of Haemophilus influenzae biogroup aegyptius (Haemophilus aegyptius) strains associated with Brazilian purpuric fever. J Clin Microbiol. 1988 Aug;26(8):1524–1534. doi: 10.1128/jcm.26.8.1524-1534.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Bricker J., Mulks M. H., Plaut A. G., Moxon E. R., Wright A. IgA1 proteases of Haemophilus influenzae: cloning and characterization in Escherichia coli K-12. Proc Natl Acad Sci U S A. 1983 May;80(9):2681–2685. doi: 10.1073/pnas.80.9.2681. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Brown I. N., Glynn A. A., Plant J. Inbred mouse strain resistance to Mycobacterium lepraemurium follows the Ity/Lsh pattern. Immunology. 1982 Sep;47(1):149–156. [PMC free article] [PubMed] [Google Scholar]
  24. Brown R. F., Stocker B. A. Salmonella typhi 205aTy, a strain with two attenuating auxotrophic characters, for use in laboratory teaching. Infect Immun. 1987 Apr;55(4):892–898. doi: 10.1128/iai.55.4.892-898.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Brubaker R. R. Mechanisms of bacterial virulence. Annu Rev Microbiol. 1985;39:21–50. doi: 10.1146/annurev.mi.39.100185.000321. [DOI] [PubMed] [Google Scholar]
  26. Brunius G., Bölin I. Interaction between Yersinia pseudotuberculosis and the HeLa cell surface. J Med Microbiol. 1983 Aug;16(3):245–261. doi: 10.1099/00222615-16-3-245. [DOI] [PubMed] [Google Scholar]
  27. Bukholm G. Effect of cytochalasin B and dihydrocytochalasin B on invasiveness of entero-invasive bacteria in HEp-2 cell cultures. Acta Pathol Microbiol Immunol Scand B. 1984 Jun;92(3):145–149. doi: 10.1111/j.1699-0463.1984.tb02809.x. [DOI] [PubMed] [Google Scholar]
  28. Burton P. R., Kordová N., Paretsky D. Electron microscopic studies of the rickettsia Coxiella burneti: entry, lysosomal response, and fate of rickettsial DNA in L-cells. Can J Microbiol. 1971 Feb;17(2):143–150. doi: 10.1139/m71-025. [DOI] [PubMed] [Google Scholar]
  29. Buysse J. M., Stover C. K., Oaks E. V., Venkatesan M., Kopecko D. J. Molecular cloning of invasion plasmid antigen (ipa) genes from Shigella flexneri: analysis of ipa gene products and genetic mapping. J Bacteriol. 1987 Jun;169(6):2561–2569. doi: 10.1128/jb.169.6.2561-2569.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Campbell A. Evolutionary significance of accessory DNA elements in bacteria. Annu Rev Microbiol. 1981;35:55–83. doi: 10.1146/annurev.mi.35.100181.000415. [DOI] [PubMed] [Google Scholar]
  31. Cantey J. R. Infectious diarrhea. Pathogenesis and risk factors. Am J Med. 1985 Jun 28;78(6B):65–75. doi: 10.1016/0002-9343(85)90367-5. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Carniel E., Mazigh D., Mollaret H. H. Expression of iron-regulated proteins in Yersinia species and their relation to virulence. Infect Immun. 1987 Jan;55(1):277–280. doi: 10.1128/iai.55.1.277-280.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  33. Casin I., Grimont F., Grimont P. A. Deoxyribonucleic acid relatedness between Haemophilus aegyptius and Haemophilus influenzae. Ann Inst Pasteur Microbiol. 1986 Sep-Oct;137B(2):155–163. doi: 10.1016/s0769-2609(86)80104-1. [DOI] [PubMed] [Google Scholar]
  34. Chandra R. K. Nutrition, immunity, and infection: present knowledge and future directions. Lancet. 1983 Mar 26;1(8326 Pt 1):688–691. doi: 10.1016/s0140-6736(83)91980-3. [DOI] [PubMed] [Google Scholar]
  35. Charnetzky W. T., Shuford W. W. Survival and growth of Yersinia pestis within macrophages and an effect of the loss of the 47-megadalton plasmid on growth in macrophages. Infect Immun. 1985 Jan;47(1):234–241. doi: 10.1128/iai.47.1.234-241.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  36. Clegg S., Gerlach G. F. Enterobacterial fimbriae. J Bacteriol. 1987 Mar;169(3):934–938. doi: 10.1128/jb.169.3.934-938.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  37. Clerc P. L., Ryter A., Mounier J., Sansonetti P. J. Plasmid-mediated early killing of eucaryotic cells by Shigella flexneri as studied by infection of J774 macrophages. Infect Immun. 1987 Mar;55(3):521–527. doi: 10.1128/iai.55.3.521-527.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  38. Clerc P., Baudry B., Sansonetti P. J. Molecular mechanisms of entry, intracellular multiplication and killing of host cells by shigellae. Curr Top Microbiol Immunol. 1988;138:3–13. [PubMed] [Google Scholar]
  39. Clerc P., Sansonetti P. J. Entry of Shigella flexneri into HeLa cells: evidence for directed phagocytosis involving actin polymerization and myosin accumulation. Infect Immun. 1987 Nov;55(11):2681–2688. doi: 10.1128/iai.55.11.2681-2688.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  40. Cornelis G., Laroche Y., Balligand G., Sory M. P., Wauters G. Yersinia enterocolitica, a primary model for bacterial invasiveness. Rev Infect Dis. 1987 Jan-Feb;9(1):64–87. doi: 10.1093/clinids/9.1.64. [DOI] [PubMed] [Google Scholar]
  41. Curtiss R., 3rd, Kelly S. M. Salmonella typhimurium deletion mutants lacking adenylate cyclase and cyclic AMP receptor protein are avirulent and immunogenic. Infect Immun. 1987 Dec;55(12):3035–3043. doi: 10.1128/iai.55.12.3035-3043.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  42. Duguid J. P., Darekar M. R., Wheater D. W. Fimbriae and infectivity in Salmonella typhimurium. J Med Microbiol. 1976 Nov;9(4):459–473. doi: 10.1099/00222615-9-4-459. [DOI] [PubMed] [Google Scholar]
  43. Elleman T. C., Hoyne P. A., Emery D. L., Stewart D. J., Clark B. L. Isolation of the gene encoding pilin of Bacteroides nodosus (strain 198), the causal organism of ovine footrot. FEBS Lett. 1984 Jul 23;173(1):103–107. doi: 10.1016/0014-5793(84)81026-1. [DOI] [PubMed] [Google Scholar]
  44. Elleman T. C., Hoyne P. A. Nucleotide sequence of the gene encoding pilin of Bacteroides nodosus, the causal organism of ovine footrot. J Bacteriol. 1984 Dec;160(3):1184–1187. doi: 10.1128/jb.160.3.1184-1187.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  45. Elleman T. C., Hoyne P. A., Stewart D. J., McKern N. M., Peterson J. E. Expression of pili from Bacteroides nodosus in Pseudomonas aeruginosa. J Bacteriol. 1986 Nov;168(2):574–580. doi: 10.1128/jb.168.2.574-580.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  46. Elleman T. C., Peterson J. E. Expression of multiple types of N-methyl Phe pili in Pseudomonas aeruginosa. Mol Microbiol. 1987 Nov;1(3):377–380. doi: 10.1111/j.1365-2958.1987.tb01945.x. [DOI] [PubMed] [Google Scholar]
  47. Elleman T. C. Pilins of Bacteroides nodosus: molecular basis of serotypic variation and relationships to other bacterial pilins. Microbiol Rev. 1988 Jun;52(2):233–247. doi: 10.1128/mr.52.2.233-247.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  48. Espersen F., Clemmensen I. Isolation of a fibronectin-binding protein from Staphylococcus aureus. Infect Immun. 1982 Aug;37(2):526–531. doi: 10.1128/iai.37.2.526-531.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  49. Fantini F. Infection and arthritis. Scand J Rheumatol Suppl. 1987;66:93–106. doi: 10.3109/03009748709102527. [DOI] [PubMed] [Google Scholar]
  50. Farley M. M., Stephens D. S., Mulks M. H., Cooper M. D., Bricker J. V., Mirra S. S., Wright A. Pathogenesis of IgA1 protease-producing and -nonproducing Haemophilus influenzae in human nasopharyngeal organ cultures. J Infect Dis. 1986 Nov;154(5):752–759. doi: 10.1093/infdis/154.5.752. [DOI] [PubMed] [Google Scholar]
  51. Fields P. I., Groisman E. A., Heffron F. A Salmonella locus that controls resistance to microbicidal proteins from phagocytic cells. Science. 1989 Feb 24;243(4894 Pt 1):1059–1062. doi: 10.1126/science.2646710. [DOI] [PubMed] [Google Scholar]
  52. Fields P. I., Swanson R. V., Haidaris C. G., Heffron F. Mutants of Salmonella typhimurium that cannot survive within the macrophage are avirulent. Proc Natl Acad Sci U S A. 1986 Jul;83(14):5189–5193. doi: 10.1073/pnas.83.14.5189. [DOI] [PMC free article] [PubMed] [Google Scholar]
  53. Finlay B. B., Falkow S. Comparison of the invasion strategies used by Salmonella cholerae-suis, Shigella flexneri and Yersinia enterocolitica to enter cultured animal cells: endosome acidification is not required for bacterial invasion or intracellular replication. Biochimie. 1988 Aug;70(8):1089–1099. doi: 10.1016/0300-9084(88)90271-4. [DOI] [PubMed] [Google Scholar]
  54. Finlay B. B., Gumbiner B., Falkow S. Penetration of Salmonella through a polarized Madin-Darby canine kidney epithelial cell monolayer. J Cell Biol. 1988 Jul;107(1):221–230. doi: 10.1083/jcb.107.1.221. [DOI] [PMC free article] [PubMed] [Google Scholar]
  55. Finlay B. B., Heffron F., Falkow S. Epithelial cell surfaces induce Salmonella proteins required for bacterial adherence and invasion. Science. 1989 Feb 17;243(4893):940–943. doi: 10.1126/science.2919285. [DOI] [PubMed] [Google Scholar]
  56. Finlay B. B., Starnbach M. N., Francis C. L., Stocker B. A., Chatfield S., Dougan G., Falkow S. Identification and characterization of TnphoA mutants of Salmonella that are unable to pass through a polarized MDCK epithelial cell monolayer. Mol Microbiol. 1988 Nov;2(6):757–766. doi: 10.1111/j.1365-2958.1988.tb00087.x. [DOI] [PubMed] [Google Scholar]
  57. Fischetti V. A., Jones K. F., Scott J. R. Size variation of the M protein in group A streptococci. J Exp Med. 1985 Jun 1;161(6):1384–1401. doi: 10.1084/jem.161.6.1384. [DOI] [PMC free article] [PubMed] [Google Scholar]
  58. Flock J. I., Fröman G., Jönsson K., Guss B., Signäs C., Nilsson B., Raucci G., Hök M., Wadström T., Lindberg M. Cloning and expression of the gene for a fibronectin-binding protein from Staphylococcus aureus. EMBO J. 1987 Aug;6(8):2351–2357. doi: 10.1002/j.1460-2075.1987.tb02511.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  59. Freter R., Allweiss B., O'Brien P. C., Halstead S. A., Macsai M. S. Role of chemotaxis in the association of motile bacteria with intestinal mucosa: in vitro studies. Infect Immun. 1981 Oct;34(1):241–249. doi: 10.1128/iai.34.1.241-249.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  60. Freter R., O'Brien P. C., Macsai M. S. Role of chemotaxis in the association of motile bacteria with intestinal mucosa: in vivo studies. Infect Immun. 1981 Oct;34(1):234–240. doi: 10.1128/iai.34.1.234-240.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  61. Frost L. S., Carpenter M., Paranchych W. N-methylphenylalanine at the N-terminus of pilin isolated from Pseudomonas aeruginosa K. Nature. 1978 Jan 5;271(5640):87–89. doi: 10.1038/271087a0. [DOI] [PubMed] [Google Scholar]
  62. Fröman G., Switalski L. M., Speziale P., Hök M. Isolation and characterization of a fibronectin receptor from Staphylococcus aureus. J Biol Chem. 1987 May 15;262(14):6564–6571. [PubMed] [Google Scholar]
  63. GERBER D. F., WATKINS H. M. Growth of shigellae in monolayer tissue cultures. J Bacteriol. 1961 Dec;82:815–822. doi: 10.1128/jb.82.6.815-822.1961. [DOI] [PMC free article] [PubMed] [Google Scholar]
  64. Gaillard J. L., Berche P., Mounier J., Richard S., Sansonetti P. In vitro model of penetration and intracellular growth of Listeria monocytogenes in the human enterocyte-like cell line Caco-2. Infect Immun. 1987 Nov;55(11):2822–2829. doi: 10.1128/iai.55.11.2822-2829.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  65. Gardner I. D. The effect of aging on susceptibility to infection. Rev Infect Dis. 1980 Sep-Oct;2(5):801–810. doi: 10.1093/clinids/2.5.801. [DOI] [PubMed] [Google Scholar]
  66. Giannella R. A., Formal S. B., Dammin G. J., Collins H. Pathogenesis of salmonellosis. Studies of fluid secretion, mucosal invasion, and morphologic reaction in the rabbit ileum. J Clin Invest. 1973 Feb;52(2):441–453. doi: 10.1172/JCI107201. [DOI] [PMC free article] [PubMed] [Google Scholar]
  67. Giannella R. A., Washington O., Gemski P., Formal S. B. Invasion of HeLa cells by Salmonella typhimurium: a model for study of invasiveness of Salmonella. J Infect Dis. 1973 Jul;128(1):69–75. doi: 10.1093/infdis/128.1.69. [DOI] [PubMed] [Google Scholar]
  68. Gottesman S. Bacterial regulation: global regulatory networks. Annu Rev Genet. 1984;18:415–441. doi: 10.1146/annurev.ge.18.120184.002215. [DOI] [PubMed] [Google Scholar]
  69. Grossman N., Joiner K. A., Frank M. M., Leive L. C3b binding, but not its breakdown, is affected by the structure of the O-antigen polysaccharide in lipopolysaccharide from Salmonellae. J Immunol. 1986 Mar 15;136(6):2208–2215. [PubMed] [Google Scholar]
  70. Gulig P. A., Curtiss R., 3rd Plasmid-associated virulence of Salmonella typhimurium. Infect Immun. 1987 Dec;55(12):2891–2901. doi: 10.1128/iai.55.12.2891-2901.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  71. Haas R., Meyer T. F. The repertoire of silent pilus genes in Neisseria gonorrhoeae: evidence for gene conversion. Cell. 1986 Jan 17;44(1):107–115. doi: 10.1016/0092-8674(86)90489-7. [DOI] [PubMed] [Google Scholar]
  72. Hackett J., Kotlarski I., Mathan V., Francki K., Rowley D. The colonization of Peyer's patches by a strain of Salmonella typhimurium cured of the cryptic plasmid. J Infect Dis. 1986 Jun;153(6):1119–1125. doi: 10.1093/infdis/153.6.1119. [DOI] [PubMed] [Google Scholar]
  73. Hackstadt T., Williams J. C. Biochemical stratagem for obligate parasitism of eukaryotic cells by Coxiella burnetii. Proc Natl Acad Sci U S A. 1981 May;78(5):3240–3244. doi: 10.1073/pnas.78.5.3240. [DOI] [PMC free article] [PubMed] [Google Scholar]
  74. Hagblom P., Segal E., Billyard E., So M. Intragenic recombination leads to pilus antigenic variation in Neisseria gonorrhoeae. Nature. 1985 May 9;315(6015):156–158. doi: 10.1038/315156a0. [DOI] [PubMed] [Google Scholar]
  75. Hale T. L., Bonventre P. F. Shigella infection of Henle intestinal epithelial cells: role of the bacterium. Infect Immun. 1979 Jun;24(3):879–886. doi: 10.1128/iai.24.3.879-886.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  76. Hale T. L., Formal S. B. Genetics of virulence in Shigella. Microb Pathog. 1986 Dec;1(6):511–518. doi: 10.1016/0882-4010(86)90037-9. [DOI] [PubMed] [Google Scholar]
  77. Hale T. L., Formal S. B. Pathogenesis of Shigella infections. Pathol Immunopathol Res. 1987;6(2):117–127. doi: 10.1159/000157053. [DOI] [PubMed] [Google Scholar]
  78. Hale T. L., Morris R. E., Bonventre P. F. Shigella infection of henle intestinal epithelial cells: role of the host cell. Infect Immun. 1979 Jun;24(3):887–894. doi: 10.1128/iai.24.3.887-894.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  79. Hale T. L., Sansonetti P. J., Schad P. A., Austin S., Formal S. B. Characterization of virulence plasmids and plasmid-associated outer membrane proteins in Shigella flexneri, Shigella sonnei, and Escherichia coli. Infect Immun. 1983 Apr;40(1):340–350. doi: 10.1128/iai.40.1.340-350.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  80. Halula M. C., Stocker B. A. Distribution and properties of the mannose-resistant hemagglutinin produced by Salmonella species. Microb Pathog. 1987 Dec;3(6):455–459. doi: 10.1016/0882-4010(87)90015-5. [DOI] [PubMed] [Google Scholar]
  81. Harrington K. A., Hormaeche C. E. Expression of the innate resistance gene Ity in mouse Kupffer cells infected with Salmonella typhimurium in vitro. Microb Pathog. 1986 Jun;1(3):269–274. doi: 10.1016/0882-4010(86)90051-3. [DOI] [PubMed] [Google Scholar]
  82. Heffernan E. J., Fierer J., Chikami G., Guiney D. Natural history of oral Salmonella dublin infection in BALB/c mice: effect of an 80-kilobase-pair plasmid on virulence. J Infect Dis. 1987 Jun;155(6):1254–1259. doi: 10.1093/infdis/155.6.1254. [DOI] [PubMed] [Google Scholar]
  83. Highsmith A. K., Jarvis W. R. Klebsiella pneumoniae: selected virulence factors that contribute to pathogenicity. Infect Control. 1985 Feb;6(2):75–77. doi: 10.1017/s0195941700062640. [DOI] [PubMed] [Google Scholar]
  84. Hollingshead S. K., Fischetti V. A., Scott J. R. Size variation in group A streptococcal M protein is generated by homologous recombination between intragenic repeats. Mol Gen Genet. 1987 May;207(2-3):196–203. doi: 10.1007/BF00331578. [DOI] [PubMed] [Google Scholar]
  85. Horwitz M. A. Formation of a novel phagosome by the Legionnaires' disease bacterium (Legionella pneumophila) in human monocytes. J Exp Med. 1983 Oct 1;158(4):1319–1331. doi: 10.1084/jem.158.4.1319. [DOI] [PMC free article] [PubMed] [Google Scholar]
  86. Horwitz M. A., Maxfield F. R. Legionella pneumophila inhibits acidification of its phagosome in human monocytes. J Cell Biol. 1984 Dec;99(6):1936–1943. doi: 10.1083/jcb.99.6.1936. [DOI] [PMC free article] [PubMed] [Google Scholar]
  87. Horwitz M. A. The Legionnaires' disease bacterium (Legionella pneumophila) inhibits phagosome-lysosome fusion in human monocytes. J Exp Med. 1983 Dec 1;158(6):2108–2126. doi: 10.1084/jem.158.6.2108. [DOI] [PMC free article] [PubMed] [Google Scholar]
  88. Hoschützky H., Lottspeich F., Jann K. Isolation and characterization of the alpha-galactosyl-1,4-beta-galactosyl-specific adhesin (P adhesin) from fimbriated Escherichia coli. Infect Immun. 1989 Jan;57(1):76–81. doi: 10.1128/iai.57.1.76-81.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  89. Irino K., Grimont F., Casin I., Grimont P. A. rRNA gene restriction patterns of Haemophilus influenzae biogroup aegyptius strains associated with Brazilian purpuric fever. J Clin Microbiol. 1988 Aug;26(8):1535–1538. doi: 10.1128/jcm.26.8.1535-1538.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  90. Isberg R. R., Falkow S. A single genetic locus encoded by Yersinia pseudotuberculosis permits invasion of cultured animal cells by Escherichia coli K-12. Nature. 1985 Sep 19;317(6034):262–264. doi: 10.1038/317262a0. [DOI] [PubMed] [Google Scholar]
  91. Isberg R. R., Voorhis D. L., Falkow S. Identification of invasin: a protein that allows enteric bacteria to penetrate cultured mammalian cells. Cell. 1987 Aug 28;50(5):769–778. doi: 10.1016/0092-8674(87)90335-7. [DOI] [PubMed] [Google Scholar]
  92. Israele V., Darabi A., McCracken G. H., Jr The role of bacterial virulence factors and Tamm-Horsfall protein in the pathogenesis of Escherichia coli urinary tract infection in infants. Am J Dis Child. 1987 Nov;141(11):1230–1234. doi: 10.1001/archpedi.1987.04460110100034. [DOI] [PubMed] [Google Scholar]
  93. Joiner K. A. Complement evasion by bacteria and parasites. Annu Rev Microbiol. 1988;42:201–230. doi: 10.1146/annurev.mi.42.100188.001221. [DOI] [PubMed] [Google Scholar]
  94. Joiner K. A. Studies on the mechanism of bacterial resistance to complement-mediated killing and on the mechanism of action of bactericidal antibody. Curr Top Microbiol Immunol. 1985;121:99–133. doi: 10.1007/978-3-642-45604-6_6. [DOI] [PubMed] [Google Scholar]
  95. Joiner K. A., Warren K. A., Hammer C., Frank M. M. Bactericidal but not nonbactericidal C5b-9 is associated with distinctive outer membrane proteins in Neisseria gonorrhoeae. J Immunol. 1985 Mar;134(3):1920–1925. [PubMed] [Google Scholar]
  96. Jones G. W., Rabert D. K., Svinarich D. M., Whitfield H. J. Association of adhesive, invasive, and virulent phenotypes of Salmonella typhimurium with autonomous 60-megadalton plasmids. Infect Immun. 1982 Nov;38(2):476–486. doi: 10.1128/iai.38.2.476-486.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  97. Jones G. W., Richardson L. A. The attachment to, and invasion of HeLa cells by Salmonella typhimurium: the contribution of mannose-sensitive and mannose-resistant haemagglutinating activities. J Gen Microbiol. 1981 Dec;127(2):361–370. doi: 10.1099/00221287-127-2-361. [DOI] [PubMed] [Google Scholar]
  98. Kan Y. W., Dozy A. M. Evolution of the hemoglobin S and C genes in world populations. Science. 1980 Jul 18;209(4454):388–391. doi: 10.1126/science.7384810. [DOI] [PubMed] [Google Scholar]
  99. Kawahara K., Haraguchi Y., Tsuchimoto M., Terakado N., Danbara H. Evidence of correlation between 50-kilobase plasmid of Salmonella choleraesuis and its virulence. Microb Pathog. 1988 Feb;4(2):155–163. doi: 10.1016/0882-4010(88)90057-5. [DOI] [PubMed] [Google Scholar]
  100. Keat A. Reiter's syndrome and reactive arthritis in perspective. N Engl J Med. 1983 Dec 29;309(26):1606–1615. doi: 10.1056/NEJM198312293092604. [DOI] [PubMed] [Google Scholar]
  101. Kilian M., Mestecky J., Russell M. W. Defense mechanisms involving Fc-dependent functions of immunoglobulin A and their subversion by bacterial immunoglobulin A proteases. Microbiol Rev. 1988 Jun;52(2):296–303. doi: 10.1128/mr.52.2.296-303.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  102. Klemm P. Fimbrial adhesions of Escherichia coli. Rev Infect Dis. 1985 May-Jun;7(3):321–340. doi: 10.1093/clinids/7.3.321. [DOI] [PubMed] [Google Scholar]
  103. Knutton S., Lloyd D. R., Candy D. C., McNeish A. S. Ultrastructural study of adhesion of enterotoxigenic Escherichia coli to erythrocytes and human intestinal epithelial cells. Infect Immun. 1984 May;44(2):519–527. doi: 10.1128/iai.44.2.519-527.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  104. Kohbata S., Yokoyama H., Yabuuchi E. Cytopathogenic effect of Salmonella typhi GIFU 10007 on M cells of murine ileal Peyer's patches in ligated ileal loops: an ultrastructural study. Microbiol Immunol. 1986;30(12):1225–1237. doi: 10.1111/j.1348-0421.1986.tb03055.x. [DOI] [PubMed] [Google Scholar]
  105. Koomey J. M., Gill R. E., Falkow S. Genetic and biochemical analysis of gonococcal IgA1 protease: cloning in Escherichia coli and construction of mutants of gonococci that fail to produce the activity. Proc Natl Acad Sci U S A. 1982 Dec;79(24):7881–7885. doi: 10.1073/pnas.79.24.7881. [DOI] [PMC free article] [PubMed] [Google Scholar]
  106. Kopecko D. J., Baron L. S., Buysse J. Genetic determinants of virulence in Shigella and dysenteric strains of Escherichia coli: their involvement in the pathogenesis of dysentery. Curr Top Microbiol Immunol. 1985;118:71–95. doi: 10.1007/978-3-642-70586-1_5. [DOI] [PubMed] [Google Scholar]
  107. Korhonen T. K., Väisänen-Rhen V., Rhen M., Pere A., Parkkinen J., Finne J. Escherichia coli fimbriae recognizing sialyl galactosides. J Bacteriol. 1984 Aug;159(2):762–766. doi: 10.1128/jb.159.2.762-766.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  108. Korhonen T. K., Väisänen V., Saxén H., Hultberg H., Svenson S. B. P-antigen-recognizing fimbriae from human uropathogenic Escherichia coli strains. Infect Immun. 1982 Jul;37(1):286–291. doi: 10.1128/iai.37.1.286-291.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  109. Kuhn M., Kathariou S., Goebel W. Hemolysin supports survival but not entry of the intracellular bacterium Listeria monocytogenes. Infect Immun. 1988 Jan;56(1):79–82. doi: 10.1128/iai.56.1.79-82.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  110. Kuriyama S. M., Silverblatt F. J. Effect of Tamm-Horsfall urinary glycoprotein on phagocytosis and killing of type I-fimbriated Escherichia coli. Infect Immun. 1986 Jan;51(1):193–198. doi: 10.1128/iai.51.1.193-198.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  111. Kétyi I. Toxins as virulence factors of bacterial enteric pathogens (a review). Acta Microbiol Hung. 1985;32(4):279–304. [PubMed] [Google Scholar]
  112. LANCEFIELD R. C. Current knowledge of type-specific M antigens of group A streptococci. J Immunol. 1962 Sep;89:307–313. [PubMed] [Google Scholar]
  113. Labigne-Roussel A., Falkow S. Distribution and degree of heterogeneity of the afimbrial-adhesin-encoding operon (afa) among uropathogenic Escherichia coli isolates. Infect Immun. 1988 Mar;56(3):640–648. doi: 10.1128/iai.56.3.640-648.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  114. Labigne-Roussel A., Schmidt M. A., Walz W., Falkow S. Genetic organization of the afimbrial adhesin operon and nucleotide sequence from a uropathogenic Escherichia coli gene encoding an afimbrial adhesin. J Bacteriol. 1985 Jun;162(3):1285–1292. doi: 10.1128/jb.162.3.1285-1292.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  115. Law D. Virulence factors of enteropathogenic Escherichia coli. J Med Microbiol. 1988 May;26(1):1–10. doi: 10.1099/00222615-26-1-1. [DOI] [PubMed] [Google Scholar]
  116. Leroux B., Yanofsky M. F., Winans S. C., Ward J. E., Ziegler S. F., Nester E. W. Characterization of the virA locus of Agrobacterium tumefaciens: a transcriptional regulator and host range determinant. EMBO J. 1987 Apr;6(4):849–856. doi: 10.1002/j.1460-2075.1987.tb04830.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  117. Lissner C. R., Weinstein D. L., O'Brien A. D. Mouse chromosome 1 Ity locus regulates microbicidal activity of isolated peritoneal macrophages against a diverse group of intracellular and extracellular bacteria. J Immunol. 1985 Jul;135(1):544–547. [PubMed] [Google Scholar]
  118. Liu S. L., Ezaki T., Miura H., Matsui K., Yabuuchi E. Intact motility as a Salmonella typhi invasion-related factor. Infect Immun. 1988 Aug;56(8):1967–1973. doi: 10.1128/iai.56.8.1967-1973.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  119. Low D., Robinson E. N., Jr, McGee Z. A., Falkow S. The frequency of expression of pyelonephritis-associated pili is under regulatory control. Mol Microbiol. 1987 Nov;1(3):335–346. doi: 10.1111/j.1365-2958.1987.tb01940.x. [DOI] [PubMed] [Google Scholar]
  120. Lubran M. M. Bacterial toxins. Ann Clin Lab Sci. 1988 Jan-Feb;18(1):58–71. [PubMed] [Google Scholar]
  121. Lund B., Marklund B. I., Strömberg N., Lindberg F., Karlsson K. A., Normark S. Uropathogenic Escherichia coli can express serologically identical pili of different receptor binding specificities. Mol Microbiol. 1988 Mar;2(2):255–263. doi: 10.1111/j.1365-2958.1988.tb00027.x. [DOI] [PubMed] [Google Scholar]
  122. Luzzatto L. Genetics of red cells and susceptibility to malaria. Blood. 1979 Nov;54(5):961–976. [PubMed] [Google Scholar]
  123. Makino S., Sasakawa C., Kamata K., Kurata T., Yoshikawa M. A genetic determinant required for continuous reinfection of adjacent cells on large plasmid in S. flexneri 2a. Cell. 1986 Aug 15;46(4):551–555. doi: 10.1016/0092-8674(86)90880-9. [DOI] [PubMed] [Google Scholar]
  124. Marrs C. F., Ruehl W. W., Schoolnik G. K., Falkow S. Pilin-gene phase variation of Moraxella bovis is caused by an inversion of the pilin genes. J Bacteriol. 1988 Jul;170(7):3032–3039. doi: 10.1128/jb.170.7.3032-3039.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  125. Marrs C. F., Schoolnik G., Koomey J. M., Hardy J., Rothbard J., Falkow S. Cloning and sequencing of a Moraxella bovis pilin gene. J Bacteriol. 1985 Jul;163(1):132–139. doi: 10.1128/jb.163.1.132-139.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  126. Mattick J. S., Bills M. M., Anderson B. J., Dalrymple B., Mott M. R., Egerton J. R. Morphogenetic expression of Bacteroides nodosus fimbriae in Pseudomonas aeruginosa. J Bacteriol. 1987 Jan;169(1):33–41. doi: 10.1128/jb.169.1.33-41.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  127. Maurelli A. T., Baudry B., d'Hauteville H., Hale T. L., Sansonetti P. J. Cloning of plasmid DNA sequences involved in invasion of HeLa cells by Shigella flexneri. Infect Immun. 1985 Jul;49(1):164–171. doi: 10.1128/iai.49.1.164-171.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  128. Maurelli A. T., Sansonetti P. J. Genetic determinants of Shigella pathogenicity. Annu Rev Microbiol. 1988;42:127–150. doi: 10.1146/annurev.mi.42.100188.001015. [DOI] [PubMed] [Google Scholar]
  129. Maurelli A. T., Sansonetti P. J. Identification of a chromosomal gene controlling temperature-regulated expression of Shigella virulence. Proc Natl Acad Sci U S A. 1988 Apr;85(8):2820–2824. doi: 10.1073/pnas.85.8.2820. [DOI] [PMC free article] [PubMed] [Google Scholar]
  130. McCune J. M., Namikawa R., Kaneshima H., Shultz L. D., Lieberman M., Weissman I. L. The SCID-hu mouse: murine model for the analysis of human hematolymphoid differentiation and function. Science. 1988 Sep 23;241(4873):1632–1639. doi: 10.1126/science.241.4873.1632. [DOI] [PubMed] [Google Scholar]
  131. McFarland W. C., Stocker B. A. Effect of different purine auxotrophic mutations on mouse-virulence of a Vi-positive strain of Salmonella dublin and of two strains of Salmonella typhimurium. Microb Pathog. 1987 Aug;3(2):129–141. doi: 10.1016/0882-4010(87)90071-4. [DOI] [PubMed] [Google Scholar]
  132. Meier J. T., Simon M. I., Barbour A. G. Antigenic variation is associated with DNA rearrangements in a relapsing fever Borrelia. Cell. 1985 Jun;41(2):403–409. doi: 10.1016/s0092-8674(85)80013-1. [DOI] [PubMed] [Google Scholar]
  133. Mekalanos J. J. Cholera toxin: genetic analysis, regulation, and role in pathogenesis. Curr Top Microbiol Immunol. 1985;118:97–118. doi: 10.1007/978-3-642-70586-1_6. [DOI] [PubMed] [Google Scholar]
  134. Mellman I., Fuchs R., Helenius A. Acidification of the endocytic and exocytic pathways. Annu Rev Biochem. 1986;55:663–700. doi: 10.1146/annurev.bi.55.070186.003311. [DOI] [PubMed] [Google Scholar]
  135. Meyer T. F., Billyard E., Haas R., Storzbach S., So M. Pilus genes of Neisseria gonorrheae: chromosomal organization and DNA sequence. Proc Natl Acad Sci U S A. 1984 Oct;81(19):6110–6114. doi: 10.1073/pnas.81.19.6110. [DOI] [PMC free article] [PubMed] [Google Scholar]
  136. Meyer T. F., Mlawer N., So M. Pilus expression in Neisseria gonorrhoeae involves chromosomal rearrangement. Cell. 1982 Aug;30(1):45–52. doi: 10.1016/0092-8674(82)90010-1. [DOI] [PubMed] [Google Scholar]
  137. Miller J. F., Mekalanos J. J., Falkow S. Coordinate regulation and sensory transduction in the control of bacterial virulence. Science. 1989 Feb 17;243(4893):916–922. doi: 10.1126/science.2537530. [DOI] [PubMed] [Google Scholar]
  138. Miller L., Gray L., Beachey E., Kehoe M. Antigenic variation among group A streptococcal M proteins. Nucleotide sequence of the serotype 5 M protein gene and its relationship with genes encoding types 6 and 24 M proteins. J Biol Chem. 1988 Apr 25;263(12):5668–5673. [PubMed] [Google Scholar]
  139. Miller V. L., Falkow S. Evidence for two genetic loci in Yersinia enterocolitica that can promote invasion of epithelial cells. Infect Immun. 1988 May;56(5):1242–1248. doi: 10.1128/iai.56.5.1242-1248.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  140. Miller V. L., Farmer J. J., 3rd, Hill W. E., Falkow S. The ail locus is found uniquely in Yersinia enterocolitica serotypes commonly associated with disease. Infect Immun. 1989 Jan;57(1):121–131. doi: 10.1128/iai.57.1.121-131.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  141. Miller V. L., Finlay B. B., Falkow S. Factors essential for the penetration of mammalian cells by Yersinia. Curr Top Microbiol Immunol. 1988;138:15–39. [PubMed] [Google Scholar]
  142. Miller V. L., Taylor R. K., Mekalanos J. J. Cholera toxin transcriptional activator toxR is a transmembrane DNA binding protein. Cell. 1987 Jan 30;48(2):271–279. doi: 10.1016/0092-8674(87)90430-2. [DOI] [PubMed] [Google Scholar]
  143. Minion F. C., Abraham S. N., Beachey E. H., Goguen J. D. The genetic determinant of adhesive function in type 1 fimbriae of Escherichia coli is distinct from the gene encoding the fimbrial subunit. J Bacteriol. 1986 Mar;165(3):1033–1036. doi: 10.1128/jb.165.3.1033-1036.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  144. Moch T., Hoschützky H., Hacker J., Kröncke K. D., Jann K. Isolation and characterization of the alpha-sialyl-beta-2,3-galactosyl-specific adhesin from fimbriated Escherichia coli. Proc Natl Acad Sci U S A. 1987 May;84(10):3462–3466. doi: 10.1073/pnas.84.10.3462. [DOI] [PMC free article] [PubMed] [Google Scholar]
  145. Mooi F. R., de Graaf F. K. Molecular biology of fimbriae of enterotoxigenic Escherichia coli. Curr Top Microbiol Immunol. 1985;118:119–138. doi: 10.1007/978-3-642-70586-1_7. [DOI] [PubMed] [Google Scholar]
  146. Moulder J. W. Comparative biology of intracellular parasitism. Microbiol Rev. 1985 Sep;49(3):298–337. doi: 10.1128/mr.49.3.298-337.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  147. Moxon E. R., Kroll J. S. Type b capsular polysaccharide as a virulence factor of Haemophilus influenzae. Vaccine. 1988 Apr;6(2):113–115. doi: 10.1016/s0264-410x(88)80011-2. [DOI] [PubMed] [Google Scholar]
  148. Musser J. M., Kroll J. S., Moxon E. R., Selander R. K. Evolutionary genetics of the encapsulated strains of Haemophilus influenzae. Proc Natl Acad Sci U S A. 1988 Oct;85(20):7758–7762. doi: 10.1073/pnas.85.20.7758. [DOI] [PMC free article] [PubMed] [Google Scholar]
  149. Nixon B. T., Ronson C. W., Ausubel F. M. Two-component regulatory systems responsive to environmental stimuli share strongly conserved domains with the nitrogen assimilation regulatory genes ntrB and ntrC. Proc Natl Acad Sci U S A. 1986 Oct;83(20):7850–7854. doi: 10.1073/pnas.83.20.7850. [DOI] [PMC free article] [PubMed] [Google Scholar]
  150. Norgren M., Normark S., Lark D., O'Hanley P., Schoolnik G., Falkow S., Svanborg-Edén C., Båga M., Uhlin B. E. Mutations in E coli cistrons affecting adhesion to human cells do not abolish Pap pili fiber formation. EMBO J. 1984 May;3(5):1159–1165. doi: 10.1002/j.1460-2075.1984.tb01945.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  151. Normark S., Lark D., Hull R., Norgren M., Båga M., O'Hanley P., Schoolnik G., Falkow S. Genetics of digalactoside-binding adhesin from a uropathogenic Escherichia coli strain. Infect Immun. 1983 Sep;41(3):942–949. doi: 10.1128/iai.41.3.942-949.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  152. Nowicki B., Vuopio-Varkila J., Viljanen P., Korhonen T. K., Mäkelä P. H. Fimbrial phase variation and systemic E. coli infection studied in the mouse peritonitis model. Microb Pathog. 1986 Aug;1(4):335–347. doi: 10.1016/0882-4010(86)90066-5. [DOI] [PubMed] [Google Scholar]
  153. O'Hanley P., Lark D., Normark S., Falkow S., Schoolnik G. K. Mannose-sensitive and Gal-Gal binding Escherichia coli pili from recombinant strains. Chemical, functional, and serological properties. J Exp Med. 1983 Nov 1;158(5):1713–1719. doi: 10.1084/jem.158.5.1713. [DOI] [PMC free article] [PubMed] [Google Scholar]
  154. O'Reilly T. M., Bhatti A. R. Proteases of the pathogenic neisseriae: possible role in infection. Microbios. 1986;45(183):113–129. [PubMed] [Google Scholar]
  155. Ofek I., Sharon N. Lectinophagocytosis: a molecular mechanism of recognition between cell surface sugars and lectins in the phagocytosis of bacteria. Infect Immun. 1988 Mar;56(3):539–547. doi: 10.1128/iai.56.3.539-547.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  156. Ogasawara M., Kono D. H., Yu D. T. Mimicry of human histocompatibility HLA-B27 antigens by Klebsiella pneumoniae. Infect Immun. 1986 Mar;51(3):901–908. doi: 10.1128/iai.51.3.901-908.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  157. Orskov I., Ferencz A., Orskov F. Tamm-Horsfall protein or uromucoid is the normal urinary slime that traps type 1 fimbriated Escherichia coli. Lancet. 1980 Apr 19;1(8173):887–887. doi: 10.1016/s0140-6736(80)91396-3. [DOI] [PubMed] [Google Scholar]
  158. Pasloske B. L., Finlay B. B., Paranchych W. Cloning and sequencing of the Pseudomonas aeruginosa PAK pilin gene. FEBS Lett. 1985 Apr 22;183(2):408–412. doi: 10.1016/0014-5793(85)80821-8. [DOI] [PubMed] [Google Scholar]
  159. Pasloske B. L., Sastry P. A., Finlay B. B., Paranchych W. Two unusual pilin sequences from different isolates of Pseudomonas aeruginosa. J Bacteriol. 1988 Aug;170(8):3738–3741. doi: 10.1128/jb.170.8.3738-3741.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  160. Payne N. R., Horwitz M. A. Phagocytosis of Legionella pneumophila is mediated by human monocyte complement receptors. J Exp Med. 1987 Nov 1;166(5):1377–1389. doi: 10.1084/jem.166.5.1377. [DOI] [PMC free article] [PubMed] [Google Scholar]
  161. Payne N. R., Kim Y. K., Ferrieri P. Effect of differences in antibody and complement requirements on phagocytic uptake and intracellular killing of "c" protein-positive and -negative strains of type II group B streptococci. Infect Immun. 1987 May;55(5):1243–1251. doi: 10.1128/iai.55.5.1243-1251.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  162. Payne S. M., Finkelstein R. A. The critical role of iron in host-bacterial interactions. J Clin Invest. 1978 Jun;61(6):1428–1440. doi: 10.1172/JCI109062. [DOI] [PMC free article] [PubMed] [Google Scholar]
  163. Pedersen K. B., Winblad S., Bitsch V. Studies on the interaction between different O-serotypes of Yersinia enterocolitica and HeLa cells. Acta Pathol Microbiol Scand B. 1979 Apr;87B(2):141–145. doi: 10.1111/j.1699-0463.1979.tb02417.x. [DOI] [PubMed] [Google Scholar]
  164. Peterson K., Baseman J. B., Alderete J. F. Molecular cloning of Treponema pallidum outer envelope fibronectin binding proteins, P1 and P2. Genitourin Med. 1987 Dec;63(6):355–360. doi: 10.1136/sti.63.6.355. [DOI] [PMC free article] [PubMed] [Google Scholar]
  165. Peterson P. K., Schmeling D., Cleary P. P., Wilkinson B. J., Kim Y., Quie P. G. Inhibition of alternative complement pathway opsonization by group A streptococcal M protein. J Infect Dis. 1979 May;139(5):575–585. doi: 10.1093/infdis/139.5.575. [DOI] [PubMed] [Google Scholar]
  166. Phair J. P. Aging and infection: a review. J Chronic Dis. 1979;32(7):535–540. doi: 10.1016/0021-9681(79)90115-2. [DOI] [PubMed] [Google Scholar]
  167. Plant J. E., Blackwell J. M., O'Brien A. D., Bradley D. J., Glynn A. A. Are the Lsh and Ity disease resistance genes at one locus on mouse chromosome 1? Nature. 1982 Jun 10;297(5866):510–511. doi: 10.1038/297510a0. [DOI] [PubMed] [Google Scholar]
  168. Plaut A. G. The IgA1 proteases of pathogenic bacteria. Annu Rev Microbiol. 1983;37:603–622. doi: 10.1146/annurev.mi.37.100183.003131. [DOI] [PubMed] [Google Scholar]
  169. Pohlner J., Halter R., Beyreuther K., Meyer T. F. Gene structure and extracellular secretion of Neisseria gonorrhoeae IgA protease. 1987 Jan 29-Feb 4Nature. 325(6103):458–462. doi: 10.1038/325458a0. [DOI] [PubMed] [Google Scholar]
  170. Pollack C., Straley S. C., Klempner M. S. Probing the phagolysosomal environment of human macrophages with a Ca2+-responsive operon fusion in Yersinia pestis. 1986 Aug 28-Sep 3Nature. 322(6082):834–836. doi: 10.1038/322834a0. [DOI] [PubMed] [Google Scholar]
  171. Portnoy D. A., Jacks P. S., Hinrichs D. J. Role of hemolysin for the intracellular growth of Listeria monocytogenes. J Exp Med. 1988 Apr 1;167(4):1459–1471. doi: 10.1084/jem.167.4.1459. [DOI] [PMC free article] [PubMed] [Google Scholar]
  172. Portnoy D. A., Martinez R. J. Role of a plasmid in the pathogenicity of Yersinia species. Curr Top Microbiol Immunol. 1985;118:29–51. doi: 10.1007/978-3-642-70586-1_3. [DOI] [PubMed] [Google Scholar]
  173. Purtilo D. T., Connor D. H. Fatal infections in protein-calorie malnourished children with thymolymphatic atrophy. Arch Dis Child. 1975 Feb;50(2):149–152. doi: 10.1136/adc.50.2.149. [DOI] [PMC free article] [PubMed] [Google Scholar]
  174. Reid G., Sobel J. D. Bacterial adherence in the pathogenesis of urinary tract infection: a review. Rev Infect Dis. 1987 May-Jun;9(3):470–487. doi: 10.1093/clinids/9.3.470. [DOI] [PubMed] [Google Scholar]
  175. Rhen M., Klemm P., Korhonen T. K. Identification of two new hemagglutinins of Escherichia coli, N-acetyl-D-glucosamine-specific fimbriae and a blood group M-specific agglutinin, by cloning the corresponding genes in Escherichia coli K-12. J Bacteriol. 1986 Dec;168(3):1234–1242. doi: 10.1128/jb.168.3.1234-1242.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  176. Rodriguez-Ortega M., Ofek I., Sharon N. Membrane glycoproteins of human polymorphonuclear leukocytes that act as receptors for mannose-specific Escherichia coli. Infect Immun. 1987 Apr;55(4):968–973. doi: 10.1128/iai.55.4.968-973.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  177. Ronson C. W., Nixon B. T., Ausubel F. M. Conserved domains in bacterial regulatory proteins that respond to environmental stimuli. Cell. 1987 Jun 5;49(5):579–581. doi: 10.1016/0092-8674(87)90530-7. [DOI] [PubMed] [Google Scholar]
  178. Ruoslahti E., Pierschbacher M. D. Arg-Gly-Asp: a versatile cell recognition signal. Cell. 1986 Feb 28;44(4):517–518. doi: 10.1016/0092-8674(86)90259-x. [DOI] [PubMed] [Google Scholar]
  179. Ruoslahti E., Pierschbacher M. D. New perspectives in cell adhesion: RGD and integrins. Science. 1987 Oct 23;238(4826):491–497. doi: 10.1126/science.2821619. [DOI] [PubMed] [Google Scholar]
  180. Russell D. G., Wright S. D. Complement receptor type 3 (CR3) binds to an Arg-Gly-Asp-containing region of the major surface glycoprotein, gp63, of Leishmania promastigotes. J Exp Med. 1988 Jul 1;168(1):279–292. doi: 10.1084/jem.168.1.279. [DOI] [PMC free article] [PubMed] [Google Scholar]
  181. SMITH H. The use of bacteria grown in vivo for studies on the basis of their pathogenicity. Annu Rev Microbiol. 1958;12:77–102. doi: 10.1146/annurev.mi.12.100158.000453. [DOI] [PubMed] [Google Scholar]
  182. Sakai T., Sasakawa C., Makino S., Yoshikawa M. DNA sequence and product analysis of the virF locus responsible for congo red binding and cell invasion in Shigella flexneri 2a. Infect Immun. 1986 Nov;54(2):395–402. doi: 10.1128/iai.54.2.395-402.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  183. Sakai T., Sasakawa C., Yoshikawa M. Expression of four virulence antigens of Shigella flexneri is positively regulated at the transcriptional level by the 30 kiloDalton virF protein. Mol Microbiol. 1988 Sep;2(5):589–597. doi: 10.1111/j.1365-2958.1988.tb00067.x. [DOI] [PubMed] [Google Scholar]
  184. Sansonetti P. J., Kopecko D. J., Formal S. B. Involvement of a plasmid in the invasive ability of Shigella flexneri. Infect Immun. 1982 Mar;35(3):852–860. doi: 10.1128/iai.35.3.852-860.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  185. Sansonetti P. J., Mounier J. Metabolic events mediating early killing of host cells infected by Shigella flexneri. Microb Pathog. 1987 Jul;3(1):53–61. doi: 10.1016/0882-4010(87)90037-4. [DOI] [PubMed] [Google Scholar]
  186. Sansonetti P. J., Ryter A., Clerc P., Maurelli A. T., Mounier J. Multiplication of Shigella flexneri within HeLa cells: lysis of the phagocytic vacuole and plasmid-mediated contact hemolysis. Infect Immun. 1986 Feb;51(2):461–469. doi: 10.1128/iai.51.2.461-469.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  187. Sasakawa C., Kamata K., Sakai T., Makino S., Yamada M., Okada N., Yoshikawa M. Virulence-associated genetic regions comprising 31 kilobases of the 230-kilobase plasmid in Shigella flexneri 2a. J Bacteriol. 1988 Jun;170(6):2480–2484. doi: 10.1128/jb.170.6.2480-2484.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  188. Sasakawa C., Makino S., Kamata K., Yoshikawa M. Isolation, characterization, and mapping of Tn5 insertions into the 140-megadalton invasion plasmid defective in the mouse Sereny test in Shigella flexneri 2a. Infect Immun. 1986 Oct;54(1):32–36. doi: 10.1128/iai.54.1.32-36.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  189. Sastry P. A., Finlay B. B., Pasloske B. L., Paranchych W., Pearlstone J. R., Smillie L. B. Comparative studies of the amino acid and nucleotide sequences of pilin derived from Pseudomonas aeruginosa PAK and PAO. J Bacteriol. 1985 Nov;164(2):571–577. doi: 10.1128/jb.164.2.571-577.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  190. Sato Y., Cowell J. L., Sato H., Burstyn D. G., Manclark C. R. Separation and purification of the hemagglutinins from Bordetella pertussis. Infect Immun. 1983 Jul;41(1):313–320. doi: 10.1128/iai.41.1.313-320.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  191. Saxén H., Reima I., Mäkelä P. H. Alternative complement pathway activation by Salmonella O polysaccharide as a virulence determinant in the mouse. Microb Pathog. 1987 Jan;2(1):15–28. doi: 10.1016/0882-4010(87)90111-2. [DOI] [PubMed] [Google Scholar]
  192. Schryvers A. B., Morris L. J. Identification and characterization of the human lactoferrin-binding protein from Neisseria meningitidis. Infect Immun. 1988 May;56(5):1144–1149. doi: 10.1128/iai.56.5.1144-1149.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  193. Schryvers A. B., Morris L. J. Identification and characterization of the transferrin receptor from Neisseria meningitidis. Mol Microbiol. 1988 Mar;2(2):281–288. doi: 10.1111/j.1365-2958.1988.tb00029.x. [DOI] [PubMed] [Google Scholar]
  194. Schwalbe R. S., Sparling P. F., Cannon J. G. Variation of Neisseria gonorrhoeae protein II among isolates from an outbreak caused by a single gonococcal strain. Infect Immun. 1985 Jul;49(1):250–252. doi: 10.1128/iai.49.1.250-252.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  195. Seifert H. S., So M. Genetic mechanisms of bacterial antigenic variation. Microbiol Rev. 1988 Sep;52(3):327–336. doi: 10.1128/mr.52.3.327-336.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  196. Selander R. K., Caugant D. A., Ochman H., Musser J. M., Gilmour M. N., Whittam T. S. Methods of multilocus enzyme electrophoresis for bacterial population genetics and systematics. Appl Environ Microbiol. 1986 May;51(5):873–884. doi: 10.1128/aem.51.5.873-884.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  197. Selander R. K., Musser J. M., Caugant D. A., Gilmour M. N., Whittam T. S. Population genetics of pathogenic bacteria. Microb Pathog. 1987 Jul;3(1):1–7. doi: 10.1016/0882-4010(87)90032-5. [DOI] [PubMed] [Google Scholar]
  198. Sharon N. Bacterial lectins, cell-cell recognition and infectious disease. FEBS Lett. 1987 Jun 15;217(2):145–157. doi: 10.1016/0014-5793(87)80654-3. [DOI] [PubMed] [Google Scholar]
  199. Skamene E., Gros P., Forget A., Kongshavn P. A., St Charles C., Taylor B. A. Genetic regulation of resistance to intracellular pathogens. Nature. 1982 Jun 10;297(5866):506–509. doi: 10.1038/297506a0. [DOI] [PubMed] [Google Scholar]
  200. Small P. L., Falkow S. Identification of regions on a 230-kilobase plasmid from enteroinvasive Escherichia coli that are required for entry into HEp-2 cells. Infect Immun. 1988 Jan;56(1):225–229. doi: 10.1128/iai.56.1.225-229.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  201. Smith H. Biochemical challenge of microbial pathogenicity. Bacteriol Rev. 1968 Sep;32(3):164–184. doi: 10.1128/br.32.3.164-184.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  202. Smith H. The biochemical challenge of microbial pathogenicity. J Appl Bacteriol. 1984 Dec;57(3):395–404. doi: 10.1111/j.1365-2672.1984.tb01405.x. [DOI] [PubMed] [Google Scholar]
  203. Smith H. The development of studies on the determinants of bacterial pathogenicity. J Comp Pathol. 1988 Apr;98(3):253–273. doi: 10.1016/0021-9975(88)90036-9. [DOI] [PubMed] [Google Scholar]
  204. Somma-Moreira R. E., Caffarena R. M., Somma S., Pérez G., Monteiro M. Analysis of Q fever in Uruguay. Rev Infect Dis. 1987 Mar-Apr;9(2):386–387. doi: 10.1093/clinids/9.2.386. [DOI] [PubMed] [Google Scholar]
  205. Sperber S. J., Schleupner C. J. Salmonellosis during infection with human immunodeficiency virus. Rev Infect Dis. 1987 Sep-Oct;9(5):925–934. doi: 10.1093/clinids/9.5.925. [DOI] [PubMed] [Google Scholar]
  206. Stanislawski L., Simpson W. A., Hasty D., Sharon N., Beachey E. H., Ofek I. Role of fibronectin in attachment of Streptococcus pyogenes and Escherichia coli to human cell lines and isolated oral epithelial cells. Infect Immun. 1985 Apr;48(1):257–259. doi: 10.1128/iai.48.1.257-259.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  207. Stern A., Brown M., Nickel P., Meyer T. F. Opacity genes in Neisseria gonorrhoeae: control of phase and antigenic variation. Cell. 1986 Oct 10;47(1):61–71. doi: 10.1016/0092-8674(86)90366-1. [DOI] [PubMed] [Google Scholar]
  208. Stern A., Nickel P., Meyer T. F., So M. Opacity determinants of Neisseria gonorrhoeae: gene expression and chromosomal linkage to the gonococcal pilus gene. Cell. 1984 Jun;37(2):447–456. doi: 10.1016/0092-8674(84)90375-1. [DOI] [PubMed] [Google Scholar]
  209. Stock J. Mechanisms of receptor function and the molecular biology of information processing in bacteria. Bioessays. 1987 May;6(5):199–203. doi: 10.1002/bies.950060502. [DOI] [PubMed] [Google Scholar]
  210. Stocker B. A. Auxotrophic Salmonella typhi as live vaccine. Vaccine. 1988 Apr;6(2):141–145. doi: 10.1016/s0264-410x(88)80017-3. [DOI] [PubMed] [Google Scholar]
  211. Stoenner H. G., Dodd T., Larsen C. Antigenic variation of Borrelia hermsii. J Exp Med. 1982 Nov 1;156(5):1297–1311. doi: 10.1084/jem.156.5.1297. [DOI] [PMC free article] [PubMed] [Google Scholar]
  212. Straley S. C., Harmon P. A. Growth in mouse peritoneal macrophages of Yersinia pestis lacking established virulence determinants. Infect Immun. 1984 Sep;45(3):649–654. doi: 10.1128/iai.45.3.649-654.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  213. Straley S. C., Harmon P. A. Yersinia pestis grows within phagolysosomes in mouse peritoneal macrophages. Infect Immun. 1984 Sep;45(3):655–659. doi: 10.1128/iai.45.3.655-659.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  214. Stromberg N., Deal C., Nyberg G., Normark S., So M., Karlsson K. A. Identification of carbohydrate structures that are possible receptors for Neisseria gonorrhoeae. Proc Natl Acad Sci U S A. 1988 Jul;85(13):4902–4906. doi: 10.1073/pnas.85.13.4902. [DOI] [PMC free article] [PubMed] [Google Scholar]
  215. Struelens M. J., Patte D., Kabir I., Salam A., Nath S. K., Butler T. Shigella septicemia: prevalence, presentation, risk factors, and outcome. J Infect Dis. 1985 Oct;152(4):784–790. doi: 10.1093/infdis/152.4.784. [DOI] [PubMed] [Google Scholar]
  216. Swanson J., Bergström S., Robbins K., Barrera O., Corwin D., Koomey J. M. Gene conversion involving the pilin structural gene correlates with pilus+ in equilibrium with pilus- changes in Neisseria gonorrhoeae. Cell. 1986 Oct 24;47(2):267–276. doi: 10.1016/0092-8674(86)90449-6. [DOI] [PubMed] [Google Scholar]
  217. Swanson J. Studies on gonococcus infection. XIV. Cell wall protein differences among color/opacity colony variants of Neisseria gonorrhoeae. Infect Immun. 1978 Jul;21(1):292–302. doi: 10.1128/iai.21.1.292-302.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  218. Takeuchi A. Electron microscope studies of experimental Salmonella infection. I. Penetration into the intestinal epithelium by Salmonella typhimurium. Am J Pathol. 1967 Jan;50(1):109–136. [PMC free article] [PubMed] [Google Scholar]
  219. Takeuchi A., Sprinz H., LaBrec E. H., Formal S. B. Experimental bacillary dysentery. An electron microscopic study of the response of the intestinal mucosa to bacterial invasion. Am J Pathol. 1965 Dec;47(6):1011–1044. [PMC free article] [PubMed] [Google Scholar]
  220. Taylor R. K., Miller V. L., Furlong D. B., Mekalanos J. J. Use of phoA gene fusions to identify a pilus colonization factor coordinately regulated with cholera toxin. Proc Natl Acad Sci U S A. 1987 May;84(9):2833–2837. doi: 10.1073/pnas.84.9.2833. [DOI] [PMC free article] [PubMed] [Google Scholar]
  221. Temin H. M. Mechanisms of cell killing/cytopathic effects by nonhuman retroviruses. Rev Infect Dis. 1988 Mar-Apr;10(2):399–405. doi: 10.1093/clinids/10.2.399. [DOI] [PubMed] [Google Scholar]
  222. Terakado N., Sekizaki T., Hashimoto K., Naitoh S. Correlation between the presence of a fifty-megadalton plasmid in Salmonella dublin and virulence for mice. Infect Immun. 1983 Jul;41(1):443–444. doi: 10.1128/iai.41.1.443-444.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  223. Thomas D. D., Baseman J. B., Alderete J. F. Fibronectin mediates Treponema pallidum cytadherence through recognition of fibronectin cell-binding domain. J Exp Med. 1985 Mar 1;161(3):514–525. doi: 10.1084/jem.161.3.514. [DOI] [PMC free article] [PubMed] [Google Scholar]
  224. Thomas D. D., Baseman J. B., Alderete J. F. Fibronectin tetrapeptide is target for syphilis spirochete cytadherence. J Exp Med. 1985 Nov 1;162(5):1715–1719. doi: 10.1084/jem.162.5.1715. [DOI] [PMC free article] [PubMed] [Google Scholar]
  225. Thomas D. D., Baseman J. B., Alderete J. F. Putative Treponema pallidum cytadhesins share a common functional domain. Infect Immun. 1985 Sep;49(3):833–835. doi: 10.1128/iai.49.3.833-835.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  226. Thomas D. D., Navab M., Haake D. A., Fogelman A. M., Miller J. N., Lovett M. A. Treponema pallidum invades intercellular junctions of endothelial cell monolayers. Proc Natl Acad Sci U S A. 1988 May;85(10):3608–3612. doi: 10.1073/pnas.85.10.3608. [DOI] [PMC free article] [PubMed] [Google Scholar]
  227. Timmis K. N., Boulnois G. J., Bitter-Suermann D., Cabello F. C. Surface components of Escherichia coli that mediate resistance to the bactericidal activities of serum and phagocytes. Curr Top Microbiol Immunol. 1985;118:197–218. doi: 10.1007/978-3-642-70586-1_11. [DOI] [PubMed] [Google Scholar]
  228. Uhlin B. E., Båga M., Göransson M., Lindberg F. P., Lund B., Norgren M., Normark S. Genes determining adhesin formation in uropathogenic Escherichia coli. Curr Top Microbiol Immunol. 1985;118:163–178. doi: 10.1007/978-3-642-70586-1_9. [DOI] [PubMed] [Google Scholar]
  229. Uhlman D. L., Jones G. W. Chemotaxis as a factor in interactions between HeLa cells and Salmonella typhimurium. J Gen Microbiol. 1982 Feb;128(2):415–418. doi: 10.1099/00221287-128-2-415. [DOI] [PubMed] [Google Scholar]
  230. Une T. Studies on the pathogenicity of Yersinia enterocolitica. I. Experimental infection in rabbits. Microbiol Immunol. 1977;21(7):341–363. [PubMed] [Google Scholar]
  231. Vesikari T., Sundqvist C., Mäki M. Adherence and toxicity of Yersinia enterocolitica 0:3 and 0:9 containing virulence-associated plasmids for various cultured cells. Acta Pathol Microbiol Immunol Scand B. 1983 Apr;91(2):121–127. doi: 10.1111/j.1699-0463.1983.tb00020.x. [DOI] [PubMed] [Google Scholar]
  232. Virji M., Everson J. S. Comparative virulence of opacity variants of Neisseria gonorrhoeae strain P9. Infect Immun. 1981 Mar;31(3):965–970. doi: 10.1128/iai.31.3.965-970.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  233. Väisänen-Rhen V. Fimbria-like hemagglutinin of Escherichia coli O75 strains. Infect Immun. 1984 Nov;46(2):401–407. doi: 10.1128/iai.46.2.401-407.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  234. Watanabe H., Nakamura A. Identification of Shigella sonnei form I plasmid genes necessary for cell invasion and their conservation among Shigella species and enteroinvasive Escherichia coli. Infect Immun. 1986 Aug;53(2):352–358. doi: 10.1128/iai.53.2.352-358.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  235. Weiss A. A., Hewlett E. L., Myers G. A., Falkow S. Tn5-induced mutations affecting virulence factors of Bordetella pertussis. Infect Immun. 1983 Oct;42(1):33–41. doi: 10.1128/iai.42.1.33-41.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  236. Weiss A. A., Hewlett E. L. Virulence factors of Bordetella pertussis. Annu Rev Microbiol. 1986;40:661–686. doi: 10.1146/annurev.mi.40.100186.003305. [DOI] [PubMed] [Google Scholar]
  237. Whitnack E., Beachey E. H. Inhibition of complement-mediated opsonization and phagocytosis of Streptococcus pyogenes by D fragments of fibrinogen and fibrin bound to cell surface M protein. J Exp Med. 1985 Dec 1;162(6):1983–1997. doi: 10.1084/jem.162.6.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  238. Whitnack E., Dale J. B., Beachey E. H. Common protective antigens of group A streptococcal M proteins masked by fibrinogen. J Exp Med. 1984 Apr 1;159(4):1201–1212. doi: 10.1084/jem.159.4.1201. [DOI] [PMC free article] [PubMed] [Google Scholar]
  239. Winans S. C., Ebert P. R., Stachel S. E., Gordon M. P., Nester E. W. A gene essential for Agrobacterium virulence is homologous to a family of positive regulatory loci. Proc Natl Acad Sci U S A. 1986 Nov;83(21):8278–8282. doi: 10.1073/pnas.83.21.8278. [DOI] [PMC free article] [PubMed] [Google Scholar]
  240. Woods D. E., Bass J. A., Johanson W. G., Jr, Straus D. C. Role of adherence in the pathogenesis of Pseudomonas aeruginosa lung infection in cystic fibrosis patients. Infect Immun. 1980 Dec;30(3):694–699. doi: 10.1128/iai.30.3.694-699.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  241. Woods D. E., Straus D. C., Johanson W. G., Jr, Bass J. A. Role of fibronectin in the prevention of adherence of Pseudomonas aeruginosa to buccal cells. J Infect Dis. 1981 Jun;143(6):784–790. doi: 10.1093/infdis/143.6.784. [DOI] [PubMed] [Google Scholar]
  242. Woods D. E., Straus D. C., Johanson W. G., Jr, Bass J. A. Role of salivary protease activity in adherence of gram-negative bacilli to mammalian buccal epithelial cells in vivo. J Clin Invest. 1981 Dec;68(6):1435–1440. doi: 10.1172/JCI110395. [DOI] [PMC free article] [PubMed] [Google Scholar]
  243. Zinkernagel R. M. Associations between major histocompatibility antigens and susceptibility to disease. Annu Rev Microbiol. 1979;33:201–213. doi: 10.1146/annurev.mi.33.100179.001221. [DOI] [PubMed] [Google Scholar]

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