Literature DB >> 1956286

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

R C Judd1, J C Strange, R K Pettit, W M Shafer.   

Abstract

A previous study in our laboratory identified a surface-exposed peptidoglycan-associated protein of Neisseria gonorrhoeae which had an apparent molecular mass of 44,000 daltons (44kDa) (Hill and Judd, 1989). This paper reports results which confirm that the 44kDa 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 it 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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Year:  1991        PMID: 1956286     DOI: 10.1111/j.1365-2958.1991.tb01881.x

Source DB:  PubMed          Journal:  Mol Microbiol        ISSN: 0950-382X            Impact factor:   3.501


  2 in total

1.  A dominant sulfhydryl-containing protein in the outer membrane of Neisseria gonorrhoeae.

Authors:  E P Norrod; S L Browne; A Feldweg; J Leonard
Journal:  J Bacteriol       Date:  1993-02       Impact factor: 3.490

2.  A Lysine Cluster in Domain II of Bacillus subtilis PBP4a Plays a Role in the Membrane Attachment of This C1-PBP.

Authors:  Arnaud Vanden Broeck; Edwige Van der Heiden; Eric Sauvage; Marjorie Dauvin; Bernard Joris; Colette Duez
Journal:  PLoS One       Date:  2015-10-13       Impact factor: 3.240

  2 in total

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