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Human Immune Response to Iron-repressible Outer Membrane Proteins of Neisseria Meningitidis

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Journal Infect Immun
Date 1986 Dec 1
PMID 3096888
Citations 33
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Abstract

Neisseria meningitidis grown under iron-limiting conditions in vitro expresses additional iron-repressible outer membrane proteins (FeRPs). To see which FeRPs were expressed and immunogenic in human infection, we examined purified membranes from four meningococcal disease isolates with Western blotting of patient sera. Convalescent serum from each patient contained immunoglobulin G (IgG) and IgM antibodies against the homologous 70-kilodalton (kDa) FeRP and IgG antibody to the homologous 94-kDa FeRPs. Three other immunoreactive FeRPs were identified in two or more strains. Neither acute-phase sera nor pooled normal human sera contained appreciable levels of these antibodies. Antigenic cross-reactivity among FeRPs was suggested by the observation that the convalescent sera of two patients contained IgG antibodies reactive with the 70- and 94-kDa FeRPs and IgM antibodies reactive with the 70-kDa FeRPs from all four strains. Additionally, rabbit antiserum against the 70-kDa FeRP from one of these disease isolates contained IgG and IgM antibodies that reacted in Western blots with the 70-kDa FeRPs in all four strains. These results demonstrate that meningococcal FeRPs are expressed and immunogenic in vivo and that certain of these proteins are immunologically cross-reactive.

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References
1.
Mickelsen P, Sparling P . Ability of Neisseria gonorrhoeae, Neisseria meningitidis, and commensal Neisseria species to obtain iron from transferrin and iron compounds. Infect Immun. 1981; 33(2):555-64. PMC: 350736. DOI: 10.1128/iai.33.2.555-564.1981. View

2.
Frasch C, Zollinger W, Poolman J . Serotype antigens of Neisseria meningitidis and a proposed scheme for designation of serotypes. Rev Infect Dis. 1985; 7(4):504-10. DOI: 10.1093/clinids/7.4.504. View

3.
Holbein B . Enhancement of Neisseria meningitidis infection in mice by addition of iron bound to transferrin. Infect Immun. 1981; 34(1):120-5. PMC: 350830. DOI: 10.1128/iai.34.1.120-125.1981. View

4.
Wray W, Boulikas T, Wray V, Hancock R . Silver staining of proteins in polyacrylamide gels. Anal Biochem. 1981; 118(1):197-203. DOI: 10.1016/0003-2697(81)90179-2. View

5.
Mickelsen P, Blackman E, Sparling P . Ability of Neisseria gonorrhoeae, Neisseria meningitidis, and commensal Neisseria species to obtain iron from lactoferrin. Infect Immun. 1982; 35(3):915-20. PMC: 351134. DOI: 10.1128/iai.35.3.915-920.1982. View