Full text
PDF![S35](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8aad/358075/95e99a12bc48/cmr00050-0045.png)
![S36](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8aad/358075/311425de57f8/cmr00050-0046.png)
![S37](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8aad/358075/d8c4e14dbacd/cmr00050-0047.png)
![S38](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8aad/358075/99cdab87aa37/cmr00050-0048.png)
![S39](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8aad/358075/ef1adceae635/cmr00050-0049.png)
![S40](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8aad/358075/e76c56ca7310/cmr00050-0050.png)
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Archibald F. S., DeVoe I. W. Iron acquisition by Neisseria meningitidis in vitro. Infect Immun. 1980 Feb;27(2):322–334. doi: 10.1128/iai.27.2.322-334.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Berry A., Jensen R. A., Hendry A. T. Enzymic arrangement and allosteric regulation of the aromatic amino acid pathway in Neisseria gonorrhoeae. Arch Microbiol. 1987;149(2):87–94. doi: 10.1007/BF00425071. [DOI] [PubMed] [Google Scholar]
- Britigan B. E., Cohen M. S., Sparling P. F. Gonococcal infection: a model of molecular pathogenesis. N Engl J Med. 1985 Jun 27;312(26):1683–1694. doi: 10.1056/NEJM198506273122606. [DOI] [PubMed] [Google Scholar]
- Burnakis T. G., Hildebrandt N. B. Pelvic inflammatory disease: a review with emphasis on antimicrobial therapy. Rev Infect Dis. 1986 Jan-Feb;8(1):86–116. doi: 10.1093/clinids/8.1.86. [DOI] [PubMed] [Google Scholar]
- Calver G. A., Kenny C. P., Lavergne G. Iron as a replacement for mucin in the establishment of meningococcal infection in mice. Can J Microbiol. 1976 Jun;22(6):832–838. doi: 10.1139/m76-120. [DOI] [PubMed] [Google Scholar]
- Catlin B. W. Nutritional profiles of Neisseria gonorrhoeae, Neisseria meningitidis, and Neisseria lactamica in chemically defined media and the use of growth requirements for gonococcal typing. J Infect Dis. 1973 Aug;128(2):178–194. doi: 10.1093/infdis/128.2.178. [DOI] [PubMed] [Google Scholar]
- Chen K. C., Buchanan T. M. Hydrolases from Neisseria gonorrhoeae. The study of gonocosin, an aminopeptidase-P, a proline iminopeptidase, and an asparaginase. J Biol Chem. 1980 Feb 25;255(4):1704–1710. [PubMed] [Google Scholar]
- Clark V. L., Campbell L. A., Palermo D. A., Evans T. M., Klimpel K. W. Induction and repression of outer membrane proteins by anaerobic growth of Neisseria gonorrhoeae. Infect Immun. 1987 Jun;55(6):1359–1364. doi: 10.1128/iai.55.6.1359-1364.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Cohen M. S., Britigan B. E., French M., Bean K. Preliminary observations on lactoferrin secretion in human vaginal mucus: variation during the menstrual cycle, evidence of hormonal regulation, and implications for infection with Neisseria gonorrhoeae. Am J Obstet Gynecol. 1987 Nov;157(5):1122–1125. doi: 10.1016/s0002-9378(87)80274-0. [DOI] [PubMed] [Google Scholar]
- Dyer D. W., McKenna W., Woods J. P., Sparling P. F. Isolation by streptonigrin enrichment and characterization of a transferrin-specific iron uptake mutant of Neisseria meningitidis. Microb Pathog. 1987 Nov;3(5):351–363. doi: 10.1016/0882-4010(87)90005-2. [DOI] [PubMed] [Google Scholar]
- Dyer D. W., West E. P., McKenna W., Thompson S. A., Sparling P. F. A pleiotropic iron-uptake mutant of Neisseria meningitidis lacks a 70-kilodalton iron-regulated protein. Infect Immun. 1988 Apr;56(4):977–983. doi: 10.1128/iai.56.4.977-983.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Dyer D. W., West E. P., Sparling P. F. Effects of serum carrier proteins on the growth of pathogenic neisseriae with heme-bound iron. Infect Immun. 1987 Sep;55(9):2171–2175. doi: 10.1128/iai.55.9.2171-2175.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Fohn M. J., Mietzner T. A., Hubbard T. W., Morse S. A., Hook E. W., 3rd Human immunoglobulin G antibody response to the major gonococcal iron-regulated protein. Infect Immun. 1987 Dec;55(12):3065–3069. doi: 10.1128/iai.55.12.3065-3069.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hafiz S., McEntegart M. G., Jephcott A. E. Reversion of Kellogg's colonial types of Neisseria gonorrhoeae in liquid medium. J Med Microbiol. 1977 Aug;10(3):377–380. doi: 10.1099/00222615-10-3-377. [DOI] [PubMed] [Google Scholar]
- Hendry A. T., Dillon J. R. Growth inhibition of Neisseria gonorrhoeae isolates by L-phenylalanine and its analogues in defined media. Can J Microbiol. 1984 Nov;30(11):1319–1325. doi: 10.1139/m84-212. [DOI] [PubMed] [Google Scholar]
- Hendry A. T. Growth responses of Neisseria gonorrhoeae auxotypes to required amino acids and bases in liquid medium. Can J Microbiol. 1983 Oct;29(10):1309–1313. doi: 10.1139/m83-204. [DOI] [PubMed] [Google Scholar]
- Hendry A. T., Stewart I. O. Auxanographic grouping and typing of Neisseria gonorrhoeae. Can J Microbiol. 1979 Apr;25(4):512–521. doi: 10.1139/m79-075. [DOI] [PubMed] [Google Scholar]
- Holbein B. E. Enhancement of Neisseria meningitidis infection in mice by addition of iron bound to transferrin. Infect Immun. 1981 Oct;34(1):120–125. doi: 10.1128/iai.34.1.120-125.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Johnson A. P., Osborn M. F. Failure of iron to promote attachment of gonococci to human spermatozoa under physiological conditions. Br J Vener Dis. 1979 Oct;55(5):329–333. doi: 10.1136/sti.55.5.329. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Keevil C. W., Major N. C., Davies D. B., Robinson A. Physiology and virulence determinants of Neisseria gonorrhoeae grown in glucose-, oxygen- or cystine-limited continuous culture. J Gen Microbiol. 1986 Dec;132(12):3289–3302. doi: 10.1099/00221287-132-12-3289. [DOI] [PubMed] [Google Scholar]
- Keevil C. W., Spillane B. J., Major N. C. Plasmid stability and antibiotic resistance of Neisseria gonorrhoea during glucose-limited continuous culture. J Med Microbiol. 1987 Dec;24(4):351–357. doi: 10.1099/00222615-24-4-351. [DOI] [PubMed] [Google Scholar]
- Kellogg D. S., Crawford J. A., Callaway C. S. Cultivation of Neisseria gonorrhoeae under low-oxygen conditions. J Clin Microbiol. 1983 Jul;18(1):178–184. doi: 10.1128/jcm.18.1.178-184.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Knapp J. S., Clark V. L. Anaerobic growth of Neisseria gonorrhoeae coupled to nitrite reduction. Infect Immun. 1984 Oct;46(1):176–181. doi: 10.1128/iai.46.1.176-181.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
- McKenna W. R., Mickelsen P. A., Sparling P. F., Dyer D. W. Iron uptake from lactoferrin and transferrin by Neisseria gonorrhoeae. Infect Immun. 1988 Apr;56(4):785–791. doi: 10.1128/iai.56.4.785-791.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Mickelsen P. A., Blackman E., Sparling P. F. Ability of Neisseria gonorrhoeae, Neisseria meningitidis, and commensal Neisseria species to obtain iron from lactoferrin. Infect Immun. 1982 Mar;35(3):915–920. doi: 10.1128/iai.35.3.915-920.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Mickelsen P. A., Sparling P. F. Ability of Neisseria gonorrhoeae, Neisseria meningitidis, and commensal Neisseria species to obtain iron from transferrin and iron compounds. Infect Immun. 1981 Aug;33(2):555–564. doi: 10.1128/iai.33.2.555-564.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Mietzner T. A., Bolan G., Schoolnik G. K., Morse S. A. Purification and characterization of the major iron-regulated protein expressed by pathogenic Neisseriae. J Exp Med. 1987 Apr 1;165(4):1041–1057. doi: 10.1084/jem.165.4.1041. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Mietzner T. A., Luginbuhl G. H., Sandstrom E., Morse S. A. Identification of an iron-regulated 37,000-dalton protein in the cell envelope of Neisseria gonorrhoeae. Infect Immun. 1984 Aug;45(2):410–416. doi: 10.1128/iai.45.2.410-416.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Morse S. A., Cacciapuoti A. F., Lysko P. G. Physiology of Neisseria gonorrhoeae. Adv Microb Physiol. 1979;20:251–320. doi: 10.1016/s0065-2911(08)60209-x. [DOI] [PubMed] [Google Scholar]
- Morse S. A., Chen C. Y., LeFaou A., Mietzner T. A. A potential role for the major iron-regulated protein expressed by pathogenic Neisseria species. Rev Infect Dis. 1988 Jul-Aug;10 (Suppl 2):S306–S310. doi: 10.1093/cid/10.supplement_2.s306. [DOI] [PubMed] [Google Scholar]
- Morse S. A., Mietzner T. A., Bolen G., Le Faou A., Schoolnik G. Characterization of the major iron-regulated protein of Neisseria gonorrhoeae and Neisseria meningitidis. Antonie Van Leeuwenhoek. 1987;53(6):465–469. doi: 10.1007/BF00415504. [DOI] [PubMed] [Google Scholar]
- Morse S. A., Mintz C. S., Sarafian S. K., Bartenstein L., Bertram M., Apicella M. A. Effect of dilution rate on lipopolysaccharide and serum resistance of Neisseria gonorrhoeae grown in continuous culture. Infect Immun. 1983 Jul;41(1):74–82. doi: 10.1128/iai.41.1.74-82.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Norrod E. P. A role for sulfite in inducing surface changes in Neisseria gonorrhoeae. Can J Microbiol. 1984 Oct;30(10):1297–1301. doi: 10.1139/m84-207. [DOI] [PubMed] [Google Scholar]
- Odugbemi T. O., Hafiz S. The effects of iron chelators on the colonial morphology of Neisseria gonorrhoeae. J Gen Microbiol. 1978 Jan;104(1):165–167. doi: 10.1099/00221287-104-1-165. [DOI] [PubMed] [Google Scholar]
- Payne S. M., Finkelstein R. A. Pathogenesis and immunology of experimental gonococcal infection: role of iron in virulence. Infect Immun. 1975 Dec;12(6):1313–1318. doi: 10.1128/iai.12.6.1313-1318.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Pillon L., Chan M., Franczyk J., Goldner M. Comparative use of amino acids by three auxotypes of Neisseria gonorrhoeae. Antonie Van Leeuwenhoek. 1988;54(2):139–148. doi: 10.1007/BF00419201. [DOI] [PubMed] [Google Scholar]
- Port J. L., DeVoe I. W., Archibald F. S. Sulphur acquisition by Neisseria meningitidis. Can J Microbiol. 1984 Dec;30(12):1453–1457. doi: 10.1139/m84-232. [DOI] [PubMed] [Google Scholar]
- Powers C. N., Pierson D. L. Stabilization and purification of ornithine transcarbamylase from Neisseria gonorrhoeae. J Bacteriol. 1980 Feb;141(2):544–549. doi: 10.1128/jb.141.2.544-549.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
- 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]
- 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]
- Shafer W. M., Morse S. A. Cleavage of the protein III and major iron-regulated protein of Neisseria gonorrhoeae by lysosomal cathepsin G. J Gen Microbiol. 1987 Jan;133(1):155–162. doi: 10.1099/00221287-133-1-155. [DOI] [PubMed] [Google Scholar]
- Shinners E. N., Catlin B. W. Arginine and pyrimidine biosynthetic defects in Neisseria gonorrhoeae strains isolated from patients. J Bacteriol. 1982 Jul;151(1):295–302. doi: 10.1128/jb.151.1.295-302.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Shinners E. N., Catlin B. W. Arginine biosynthesis in Neisseria gonorrhoeae: enzymes catalyzing the formation of ornithine and citrulline. J Bacteriol. 1978 Oct;136(1):131–135. doi: 10.1128/jb.136.1.131-135.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Short H. B., Clark V. L., Kellogg D. S., Jr, Young F. E. Anaerobic survival of clinical isolates and laboratory strains of Neisseria gonorrhoea: use in transfer and storage. J Clin Microbiol. 1982 May;15(5):915–919. doi: 10.1128/jcm.15.5.915-919.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Simonson C., Brener D., DeVoe I. W. Expression of a high-affinity mechanism for acquisition of transferrin iron by Neisseria meningitidis. Infect Immun. 1982 Apr;36(1):107–113. doi: 10.1128/iai.36.1.107-113.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Simonson C., Trivett T., DeVoe I. W. Energy-independent uptake of iron from citrate by isolated outer membranes of Neisseria meningitidis. Infect Immun. 1981 Feb;31(2):547–553. doi: 10.1128/iai.31.2.547-553.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Tarkka E., Sarvas M. Cloning of an outer membrane protein of Neisseria meningitidis in Escherichia coli. Microb Pathog. 1987 Dec;3(6):445–453. doi: 10.1016/0882-4010(87)90014-3. [DOI] [PubMed] [Google Scholar]
- West S. E., Sparling P. F. Aerobactin utilization by Neisseria gonorrhoeae and cloning of a genomic DNA fragment that complements Escherichia coli fhuB mutations. J Bacteriol. 1987 Aug;169(8):3414–3421. doi: 10.1128/jb.169.8.3414-3421.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
- West S. E., Sparling P. F. Response of Neisseria gonorrhoeae to iron limitation: alterations in expression of membrane proteins without apparent siderophore production. Infect Immun. 1985 Feb;47(2):388–394. doi: 10.1128/iai.47.2.388-394.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Yancey R. J., Finkelstein R. A. Assmilation of iron by pathogenic Neisseria spp. Infect Immun. 1981 May;32(2):592–599. doi: 10.1128/iai.32.2.592-599.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Yancey R. J., Finkelstein R. A. Siderophore production by pathogenic Neisseria spp. Infect Immun. 1981 May;32(2):600–608. doi: 10.1128/iai.32.2.600-608.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Yeowell H. N., White J. R. Iron requirement in the bactericidal mechanism of streptonigrin. Antimicrob Agents Chemother. 1982 Dec;22(6):961–968. doi: 10.1128/aac.22.6.961. [DOI] [PMC free article] [PubMed] [Google Scholar]