Immunogenicity and cross-reactivity of the 70-Kda iron-regulated protein of in man and animals Free

Abstract

Summary

The immune response to different serogroups and serotypes of has been examined in acute and convalescent sera from patients with meningococcal diseases. The focus of the study was the . 70-Kda iron-regulated outer-membrane protein (FeRP-70). FeRP-70 was demonstrated on all strains of different serogroups and serotypes examined by sodium dodecylsulphate-polyacrylamide gel electrophoresis or Western blots of outer-membrane proteins (OMPs). Immunoblotting experiments demonstrated the presence of considerable amounts of anti-FeRP-70 IgG antibodies in the acute and convalescent sera of six patients; the antibodies reacted with homologous and heterologous strains. However, sera from two patients who died of severe meningococcal septicaemia had no antibodies against FeRP-70 or any other OMPs demonstrable by immunoblotting. Absorbed rabbit hyperimmune sera reacted with FeRP-70 of their homologous strains, but, unlike human sera, with only a few of the heterologous strains. We believe that FeRP-70 is strongly immunogenic , cross-reactive amongst different strains, and that man and animals differ considerably in their response to similar meningococcal antigens. The functional attribution of human antibody response against this protein requires further exploration.

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1990-08-01
2024-03-29
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References

  1. Devoe IW. The meningococcus and mechanisms of pathogenicity. Microbiol Rev 1982; 46:162–190
    [Google Scholar]
  2. Griffiss JM, Brandt BL, Broud DD, Goroff DK, Baker CJ. Immune response of infants and children to disseminated infections with Neisseria meningitidis. J Infect Dis 1984; 150:71–79
    [Google Scholar]
  3. Mickelsen PA, Blackman E, Sparling PF. Ability of Neisseria gonorrhoeae, Neisseria meningitidis and commensal Neisseria species to obtain iron from transferrin and iron compounds. Infect Immun 1981; 33:555–564
    [Google Scholar]
  4. Simonson C, Brener D, DeVoe IW. Expression of a high-affinity mechanism for acquisition of transferrin iron by Neisseria meningitidis. Infect Immun 1982; 36:107–113
    [Google Scholar]
  5. Schryvers AB, Morris LJ. Identification and characterization of the transferrin receptor from Neisseria meningitidis. Mol Microbiol 1988; 2:281–288
    [Google Scholar]
  6. Schryvers AB, Morris LJ. Identification and characterization of the human lactoferrin-binding protein from Neisseria meningitidis. Infect Immun 1988; 56:1144–1149
    [Google Scholar]
  7. Black JR, Dyer DW, Thompson MK, Sparling PF. Human immune response to iron repressible outer membrane proteins of Neisseria meningitidis. Infect Immun 1986; 54:710–713
    [Google Scholar]
  8. Ala'Aldeen DA, Davies H, Wall RA, Borriello SP. The 70 Kilodalton iron regulated outer membrane protein is not the human transferrin receptor. FEMS Microbiol Lett In press
    [Google Scholar]
  9. Filip C, Fletcher G, Wulff JL, Earhart CF. Solubilization of the cytoplasmic membrane of Escherichia coli by ionic detergent sodium-lauryl sarcosinate. J Bacteriol 1973; 115:717–722
    [Google Scholar]
  10. Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976; 72:248–254
    [Google Scholar]
  11. Laemmli UK. Cleavage of structural proteins during the assembly of the head of the bacteriophage T4. Nature 1970; 227:680–685
    [Google Scholar]
  12. Mietzner TA, Barnes RC, JeanLouis YA, Shafer WM, Morse SA. Distribution of an antigenically related iron-regulated protein among the Neisseria spp. Infect Immun 1986; 51:60–68
    [Google Scholar]
  13. Van Putten JPM, Linders MTJ, Weel JFL, Poolman JT. Differential expression of “Fe-repressible” and “growth-rate-sensitive” proteins in Neisseria meningitidis and Neisseria gonorrhoeae. In: Poolman JT et al. (eds) Gonococci and meningococci Dordrecht, Netherlands, Martinus Nijhoff; Norwell, MA: Kluwer Academic Publishers; 1988781–788
    [Google Scholar]
  14. Cann KJ, Rogers TR. Detection of antibodies to common antigens of pathogenic and commensal Neisseria species. J Med Microbiol 1989; 30:23–31
    [Google Scholar]
  15. Griffiths E, Stevenson P, Ray A. Antigenic and molecular heterogeneity of the transferrin-binding protein of Neisseria meningitidis. FEMS Microbiol Lett in press
    [Google Scholar]
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