Skip to main content
PMC home page
Infection and Immunity logoLink to Infection and Immunity
. 1992 Mar;60(3):1047–1054. doi: 10.1128/iai.60.3.1047-1054.1992

Conservation of an Actinomyces viscosus T14V type 1 fimbrial subunit homolog among divergent groups of Actinomyces spp.

M K Yeung 1
PMCID: PMC257592  PMID: 1347285

Abstract

The type 1 fimbrial subunit gene of the human Actinomyces viscosus T14V was used as a DNA probe in Southern analyses to detect related DNA sequences in 16 of 30 strains of Actinomyces spp. under conditions of high stringency. The organisms with homology to the DNA probe included two human and six nonhuman A. viscosus, three human and three nonhuman A. naeslundii, and two A. bovis isolates. Homologous DNA sequences were not detected in strains of A. odontolyticus and A. israelii examined in this study. Northern (RNA) blot analysis revealed expression of a transcript from each of the A. viscosus and A. naeslundii strains and from one A. bovis strain that was comparable in size to that detected from A. viscosus T14V. Cell surface fimbriae were observed on a majority of the strains that expressed the transcript. Various degrees of cross-immunoreactivities between these strains and antibodies specific for type 1 fimbriae of A. viscosus T14V were also observed by colony immunoassay. Thus, the data clearly demonstrate the existence in, and expression by, divergent Actinomyces groups of genomic sequences that are closely related to the type 1 fimbriae of A. viscosus T14V.

Full text

PDF
1053

Images in this article

1050Image
on p.1050
1050Image
on p.1050
1051Image
on p.1051

Selected References

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

  1. Arthur M., Arbeit R. D., Kim C., Beltran P., Crowe H., Steinbach S., Campanelli C., Wilson R. A., Selander R. K., Goldstein R. Restriction fragment length polymorphisms among uropathogenic Escherichia coli isolates: pap-related sequences compared with rrn operons. Infect Immun. 1990 Feb;58(2):471–479. doi: 10.1128/iai.58.2.471-479.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Brennan M. J., Cisar J. O., Vatter A. E., Sandberg A. L. Lectin-dependent attachment of Actinomyces naeslundii to receptors on epithelial cells. Infect Immun. 1984 Nov;46(2):459–464. doi: 10.1128/iai.46.2.459-464.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Cisar J. O., Barsumian E. L., Curl S. H., Vatter A. E., Sandberg A. L., Siraganian R. P. Detection and localization of a lectin on Actinomyces viscosus T14V by monoclonal antibodies. J Immunol. 1981 Oct;127(4):1318–1322. [PubMed] [Google Scholar]
  4. Cisar J. O., Barsumian E. L., Siraganian R. P., Clark W. B., Yeung M. K., Hsu S. D., Curl S. H., Vatter A. E., Sandberg A. L. Immunochemical and functional studies of Actinomyces viscosus T14V type 1 fimbriae with monoclonal and polyclonal antibodies directed against the fimbrial subunit. J Gen Microbiol. 1991 Aug;137(8):1971–1979. doi: 10.1099/00221287-137-8-1971. [DOI] [PubMed] [Google Scholar]
  5. Cisar J. O., David V. A., Curl S. H., Vatter A. E. Exclusive presence of lactose-sensitive fimbriae on a typical strain (WVU45) of Actinomyces naeslundii. Infect Immun. 1984 Nov;46(2):453–458. doi: 10.1128/iai.46.2.453-458.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Cisar J. O., Kolenbrander P. E., McIntire F. C. Specificity of coaggregation reactions between human oral streptococci and strains of Actinomyces viscosus or Actinomyces naeslundii. Infect Immun. 1979 Jun;24(3):742–752. doi: 10.1128/iai.24.3.742-752.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Cisar J. O., Vatter A. E., Clark W. B., Curl S. H., Hurst-Calderone S., Sandberg A. L. Mutants of Actinomyces viscosus T14V lacking type 1, type 2, or both types of fimbriae. Infect Immun. 1988 Nov;56(11):2984–2989. doi: 10.1128/iai.56.11.2984-2989.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Clark W. B., Webb E. L., Wheeler T. T., Fischlschweiger W., Birdsell D. C., Mansheim B. J. Role of surface fimbriae (fibrils) in the adsorption of Actinomyces species to saliva-treated hydroxyapatite surfaces. Infect Immun. 1981 Sep;33(3):908–917. doi: 10.1128/iai.33.3.908-917.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Clark W. B., Wheeler T. T., Cisar J. O. Specific inhibition of adsorption of Actinomyces viscosus T14V to saliva-treated hydroxyapatite by antibody against type 1 fimbriae. Infect Immun. 1984 Feb;43(2):497–501. doi: 10.1128/iai.43.2.497-501.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Clark W. B., Wheeler T. T., Lane M. D., Cisar J. O. Actinomyces adsorption mediated by type-1 fimbriae. J Dent Res. 1986 Sep;65(9):1166–1168. doi: 10.1177/00220345860650091001. [DOI] [PubMed] [Google Scholar]
  11. Donkersloot J. A., Cisar J. O., Wax M. E., Harr R. J., Chassy B. M. Expression of Actinomyces viscosus antigens in Escherichia coli: cloning of a structural gene (fimA) for type 2 fimbriae. J Bacteriol. 1985 Jun;162(3):1075–1078. doi: 10.1128/jb.162.3.1075-1078.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. EFTHYMIOU C., HANSEN P. A. An antigenic analysis of Lactobacillus acidophilus. J Infect Dis. 1962 May-Jun;110:258–267. doi: 10.1093/infdis/110.3.258. [DOI] [PubMed] [Google Scholar]
  13. 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]
  14. Fenno J. C., LeBlanc D. J., Fives-Taylor P. Nucleotide sequence analysis of a type 1 fimbrial gene of Streptococcus sanguis FW213. Infect Immun. 1989 Nov;57(11):3527–3533. doi: 10.1128/iai.57.11.3527-3533.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Fillery E. D., Bowden G. H., Hardie J. M. A comparison of strains of bacteria designated Actinomyces viscosus and Actinomyces naeslundii. Caries Res. 1978;12(6):299–312. doi: 10.1159/000260349. [DOI] [PubMed] [Google Scholar]
  16. Gerencser M. A., Slack J. M. Serological identification of Actinomyces using fluorescent antibody techniques. J Dent Res. 1976 Jan;55:A184–A191. doi: 10.1177/002203457605500110011. [DOI] [PubMed] [Google Scholar]
  17. Gibbons R. J., Hay D. I., Cisar J. O., Clark W. B. Adsorbed salivary proline-rich protein 1 and statherin: receptors for type 1 fimbriae of Actinomyces viscosus T14V-J1 on apatitic surfaces. Infect Immun. 1988 Nov;56(11):2990–2993. doi: 10.1128/iai.56.11.2990-2993.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Hay D. I., Bennick A., Schlesinger D. H., Minaguchi K., Madapallimattam G., Schluckebier S. K. The primary structures of six human salivary acidic proline-rich proteins (PRP-1, PRP-2, PRP-3, PRP-4, PIF-s and PIF-f). Biochem J. 1988 Oct 1;255(1):15–21. doi: 10.1042/bj2550015. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Holmberg K., Nord C. E. Numerical taxonomy and laboratory identification of Actinomyces and Arachnia and some related bacteria. J Gen Microbiol. 1975 Nov;91(1):17–44. doi: 10.1099/00221287-91-1-17. [DOI] [PubMed] [Google Scholar]
  20. Honda E., Yanagawa R. Agglutination of trypsinized sheep erythrocytes by the pili of Corynebacterium renale. Infect Immun. 1974 Dec;10(6):1426–1432. doi: 10.1128/iai.10.6.1426-1432.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Johnson J. L., Moore L. V., Kaneko B., Moore W. E. Actinomyces georgiae sp. nov., Actinomyces gerencseriae sp. nov., designation of two genospecies of Actinomyces naeslundii, and inclusion of A. naeslundii serotypes II and III and Actinomyces viscosus serotype II in A. naeslundii genospecies 2. Int J Syst Bacteriol. 1990 Jul;40(3):273–286. doi: 10.1099/00207713-40-3-273. [DOI] [PubMed] [Google Scholar]
  22. Loesche W. J., Syed S. A. Bacteriology of human experimental gingivitis: effect of plaque and gingivitis score. Infect Immun. 1978 Sep;21(3):830–839. doi: 10.1128/iai.21.3.830-839.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. 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]
  24. Nyvad B., Kilian M. Microbiology of the early colonization of human enamel and root surfaces in vivo. Scand J Dent Res. 1987 Oct;95(5):369–380. doi: 10.1111/j.1600-0722.1987.tb01627.x. [DOI] [PubMed] [Google Scholar]
  25. Paranchych W., Frost L. S. The physiology and biochemistry of pili. Adv Microb Physiol. 1988;29:53–114. doi: 10.1016/s0065-2911(08)60346-x. [DOI] [PubMed] [Google Scholar]
  26. Plos K., Hull S. I., Hull R. A., Levin B. R., Orskov I., Orskov F., Svanborg-Edén C. Distribution of the P-associated-pilus (pap) region among Escherichia coli from natural sources: evidence for horizontal gene transfer. Infect Immun. 1989 May;57(5):1604–1611. doi: 10.1128/iai.57.5.1604-1611.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Purcell B. K., Pruckler J., Clegg S. Nucleotide sequences of the genes encoding type 1 fimbrial subunits of Klebsiella pneumoniae and Salmonella typhimurium. J Bacteriol. 1987 Dec;169(12):5831–5834. doi: 10.1128/jb.169.12.5831-5834.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Sandberg A. L., Mudrick L. L., Cisar J. O., Brennan M. J., Mergenhagen S. E., Vatter A. E. Type 2 fimbrial lectin-mediated phagocytosis of oral Actinomyces spp. by polymorphonuclear leukocytes. Infect Immun. 1986 Nov;54(2):472–476. doi: 10.1128/iai.54.2.472-476.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Socransky S. S., Manganiello A. D., Propas D., Oram V., van Houte J. Bacteriological studies of developing supragingival dental plaque. J Periodontal Res. 1977 Mar;12(2):90–106. doi: 10.1111/j.1600-0765.1977.tb00112.x. [DOI] [PubMed] [Google Scholar]
  30. Theilade E., Theilade J., Mikkelsen L. Microbiological studies on early dento-gingival plaque on teeth and Mylar strips in humans. J Periodontal Res. 1982 Jan;17(1):12–25. doi: 10.1111/j.1600-0765.1982.tb01127.x. [DOI] [PubMed] [Google Scholar]
  31. Vieira J., Messing J. The pUC plasmids, an M13mp7-derived system for insertion mutagenesis and sequencing with synthetic universal primers. Gene. 1982 Oct;19(3):259–268. doi: 10.1016/0378-1119(82)90015-4. [DOI] [PubMed] [Google Scholar]
  32. Yeung M. K., Chassy B. M., Cisar J. O. Cloning and expression of a type 1 fimbrial subunit of Actinomyces viscosus T14V. J Bacteriol. 1987 Apr;169(4):1678–1683. doi: 10.1128/jb.169.4.1678-1683.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  33. Yeung M. K., Cisar J. O. Cloning and nucleotide sequence of a gene for Actinomyces naeslundii WVU45 type 2 fimbriae. J Bacteriol. 1988 Sep;170(9):3803–3809. doi: 10.1128/jb.170.9.3803-3809.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. Yeung M. K., Cisar J. O. Sequence homology between the subunits of two immunologically and functionally distinct types of fimbriae of Actinomyces spp. J Bacteriol. 1990 May;172(5):2462–2468. doi: 10.1128/jb.172.5.2462-2468.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Infection and Immunity are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES