Abstract
Although Neisseria meningitidis does not produce siderophores, it is able to obtain iron from human transferrin. We observed saturable specific binding of 125I-labeled human transferrin to meningococci. Human lactoferrin and mouse transferrin did not compete with human transferrin for binding, whereas human apotransferrin and 100% iron-saturated transferrin competed equally well. Meningococci thus have a specific receptor for human transferrin. Scatchard analysis yielded a relatively low Kd of 0.7 microM and an apparent copy number of 2,900 receptors per CFU. Receptor activity was iron-regulated. A meningococcal transformant specifically unable to utilize transferrin as an iron source had decreased transferrin receptor activity. These data are consistent with the hypothesis that receptor-mediated binding of transferrin is a rate-limiting step in meningococcal iron uptake from transferrin.
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Selected References
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- Black J. R., Dyer D. W., Thompson M. K., Sparling P. F. Human immune response to iron-repressible outer membrane proteins of Neisseria meningitidis. Infect Immun. 1986 Dec;54(3):710–713. doi: 10.1128/iai.54.3.710-713.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Brener D., DeVoe I. W., Holbein B. E. Increased virulence of Neisseria meningitidis after in vitro iron-limited growth at low pH. Infect Immun. 1981 Jul;33(1):59–66. doi: 10.1128/iai.33.1.59-66.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Burgett M. W., Fairfield S. J., Monthony J. F. A solid phase fluorescent immunossay for the quantitation of the C4 component of human complement. J Immunol Methods. 1977;16(3):211–219. doi: 10.1016/0022-1759(77)90199-5. [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]
- Frasch C. E., Peppler M. S. Protection against group B Neisseria meningitidis disease: preparation of soluble protein and protein-polysaccharide immunogens. Infect Immun. 1982 Jul;37(1):271–280. doi: 10.1128/iai.37.1.271-280.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
- HUNTER W. M., GREENWOOD F. C. Preparation of iodine-131 labelled human growth hormone of high specific activity. Nature. 1962 May 5;194:495–496. doi: 10.1038/194495a0. [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]
- Holbein B. E. Iron-controlled infection with Neisseria meningitidis in mice. Infect Immun. 1980 Sep;29(3):886–891. doi: 10.1128/iai.29.3.886-891.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
- KELLOGG D. S., Jr, PEACOCK W. L., Jr, DEACON W. E., BROWN L., PIRKLE D. I. NEISSERIA GONORRHOEAE. I. VIRULENCE GENETICALLY LINKED TO CLONAL VARIATION. J Bacteriol. 1963 Jun;85:1274–1279. doi: 10.1128/jb.85.6.1274-1279.1963. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
- Markwell M. A. A new solid-state reagent to iodinate proteins. I. Conditions for the efficient labeling of antiserum. Anal Biochem. 1982 Sep 15;125(2):427–432. doi: 10.1016/0003-2697(82)90025-2. [DOI] [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]
- Neilands J. B. Microbial envelope proteins related to iron. Annu Rev Microbiol. 1982;36:285–309. doi: 10.1146/annurev.mi.36.100182.001441. [DOI] [PubMed] [Google Scholar]
- Neilands J. B. Microbial iron compounds. Annu Rev Biochem. 1981;50:715–731. doi: 10.1146/annurev.bi.50.070181.003435. [DOI] [PubMed] [Google Scholar]
- Peterson K. M., Alderete J. F. Iron uptake and increased intracellular enzyme activity follow host lactoferrin binding by Trichomonas vaginalis receptors. J Exp Med. 1984 Aug 1;160(2):398–410. doi: 10.1084/jem.160.2.398. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Redhead K., Hill T., Chart H. Interaction of lactoferrin and transferrins with the outer membrane of Bordetella pertussis. J Gen Microbiol. 1987 Apr;133(4):891–898. doi: 10.1099/00221287-133-4-891. [DOI] [PubMed] [Google Scholar]
- Russell L. M., Cryz S. J., Jr, Holmes R. K. Genetic and biochemical evidence for a siderophore-dependent iron transport system in Corynebacterium diphtheriae. Infect Immun. 1984 Jul;45(1):143–149. doi: 10.1128/iai.45.1.143-149.1984. [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]
- 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]
- Tryon V. V., Baseman J. B. The acquisition of human lactoferrin by Mycoplasma pneumoniae. Microb Pathog. 1987 Dec;3(6):437–443. doi: 10.1016/0882-4010(87)90013-1. [DOI] [PubMed] [Google Scholar]
- Ventura M. A., Louache F., Rouis M., Erlich D., Goldstein S., Testa U., Thomopoulos P. Specific modulation of surface receptors in J.774 macrophages by anchorage. Exp Cell Res. 1987 Jun;170(2):290–299. doi: 10.1016/0014-4827(87)90307-7. [DOI] [PubMed] [Google Scholar]
- Ward J. H. The structure, function, and regulation of transferrin receptors. Invest Radiol. 1987 Jan;22(1):74–83. doi: 10.1097/00004424-198701000-00017. [DOI] [PubMed] [Google Scholar]
- Weinberg E. D. Iron and infection. Microbiol Rev. 1978 Mar;42(1):45–66. doi: 10.1128/mr.42.1.45-66.1978. [DOI] [PMC free article] [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]