Identification and characterization of a conserved outer-membrane protein of Neisseria gonorrhoeae

Authors

  • R. C. Judd,

    Corresponding author
    1. Division of Biological Sciences, University of Montana, Missoula, Montana 59812. USA.
    • *For correspondence. Tel. (406) 243 2347; Fax (406) 243 4184.

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  • J. C. Strange,

    1. Division of Biological Sciences, University of Montana, Missoula, Montana 59812. USA.
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  • R. K. Pettit,

    1. Division of Biological Sciences, University of Montana, Missoula, Montana 59812. USA.
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  • W. M. Shafer

    1. Department of Microbiology and Immunology and Medicine, Emory University School of Medicine, Atlanta, Georgia 30322, USA.
    2. Research Services, Laboratories of Microbial Pathogenesis. Veterans Administration Medical Center (Atlanta). Decatur, Georgia 30033, USA.
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Summary

A previous study in our laboratory identified a surface-exposed peptidoglycan-associated protein of Neisseria gonorrhoeae which had an apparent molecular mass of 44000 daltons (44kDa) (Hill and Judd, 1989). This paper reports results which confirm that the 44 kDa protein is surface-exposed, and that the protein is expressed in, and is structurally invariant among, 14 strains of N. gonorrhoeae. The fact that the 44kDa outer-membrane protein is found in a conserved form in all gonococci examined strongly suggests that ft is crucial to the bacterium's survival. Moreover, it appears that this protein is a penicillin-binding protein (PBP3) (Shafer and Judd, 1991). This invariant, surface-exposed, peptidoglycan-associated outer-membrane protein deserves further investigation to elucidate its role in the immunobiology of N. gonorrhoeae, and its possible use as an immunoprophylactic reagent.

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