Conserved lipoprotein H.8 of pathogenic Neisseria consists entirely of pentapeptide repeats

J. P. Woods, Stanley Spinola, S. M. Strobel, J. G. Cannon

Research output: Contribution to journalArticle

27 Citations (Scopus)

Abstract

The pathogenic Neisseria, N, gonorrhoeae and N. meningitidis, possess an outer membrane protein (OMP), designated H.8, with a conserved monoclonal antibody (MAb)-binding epitope. We determined the DNA sequence of a gonococcal H.8 gene, and confirmed the relationship between the cloned gene and the H.8 OMP by constructing a gonococcal mutant lacking H.8. The predicted H.8 OMP is a lipoprotein 71 amino acids in length, composed of 13 repeats of a consensus sequence AAEAP with perfect 5-residue periodicity. The AAEAP units form a repeating epitope that comprises the entire predicted sequence of the protein.

Original languageEnglish (US)
Pages (from-to)43-48
Number of pages6
JournalMolecular Microbiology
Volume3
Issue number1
StatePublished - 1989
Externally publishedYes

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Neisseria
Lipoproteins
Membrane Proteins
Epitopes
Neisseria gonorrhoeae
Consensus Sequence
Periodicity
Genes
Monoclonal Antibodies
Amino Acids
Proteins

ASJC Scopus subject areas

  • Molecular Biology
  • Microbiology

Cite this

Conserved lipoprotein H.8 of pathogenic Neisseria consists entirely of pentapeptide repeats. / Woods, J. P.; Spinola, Stanley; Strobel, S. M.; Cannon, J. G.

In: Molecular Microbiology, Vol. 3, No. 1, 1989, p. 43-48.

Research output: Contribution to journalArticle

Woods, J. P. ; Spinola, Stanley ; Strobel, S. M. ; Cannon, J. G. / Conserved lipoprotein H.8 of pathogenic Neisseria consists entirely of pentapeptide repeats. In: Molecular Microbiology. 1989 ; Vol. 3, No. 1. pp. 43-48.
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