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Sequence diversity, predicted two-dimensional protein structure, and epitope mapping of neisserial Opa proteins.

ABSTRACT: The sequence diversity of 45 Opa outer membrane proteins from Neisseria meningitidis, Neisseria gonorrhoeae, Neisseria sicca, and Neisseria flava indicates that horizontal genetic exchange of opa alleles has been rare between these species. A two-dimensional structural model containing four surface-exposed loops was constructed based on rules derived from porin crystal structure and on conservation of sequence homology within transmembrane beta-strands. The minimal continuous epitopes recognized by 23 monoclonal antibodies were mapped to loops 2 and 3. Some of these epitopes are localized on the bacterial cell surface, in support of the model.

SUBMITTER: Malorny B

PROVIDER: S-EPMC107023 | biostudies-literature | 1998 Mar

REPOSITORIES: biostudies-literature

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Sequence diversity, predicted two-dimensional protein structure, and epitope mapping of neisserial Opa proteins.

Malorny B B Morelli G G Kusecek B B Kolberg J J Achtman M M

Journal of bacteriology 19980301 5

The sequence diversity of 45 Opa outer membrane proteins from Neisseria meningitidis, Neisseria gonorrhoeae, Neisseria sicca, and Neisseria flava indicates that horizontal genetic exchange of opa alleles has been rare between these species. A two-dimensional structural model containing four surface-exposed loops was constructed based on rules derived from porin crystal structure and on conservation of sequence homology within transmembrane beta-strands. The minimal continuous epitopes recognized ...[more]

PMID: 9495774

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