• Medientyp: E-Artikel
  • Titel: Sequence Diversity, Predicted Two-Dimensional Protein Structure, and Epitope Mapping of Neisserial Opa Proteins
  • Beteiligte: Malorny, Burkhard; Morelli, Giovanna; Kusecek, Barica; Kolberg, Jan; Achtman, Mark
  • Erschienen: American Society for Microbiology, 1998
  • Erschienen in: Journal of Bacteriology
  • Sprache: Englisch
  • DOI: 10.1128/jb.180.5.1323-1330.1998
  • ISSN: 0021-9193; 1098-5530
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  • Beschreibung: <jats:title>ABSTRACT</jats:title> <jats:p> The sequence diversity of 45 Opa outer membrane proteins from <jats:italic>Neisseria meningitidis</jats:italic> , <jats:italic>Neisseria gonorrhoeae</jats:italic> , <jats:italic>Neisseria sicca</jats:italic> , and <jats:italic>Neisseria flava</jats:italic> indicates that horizontal genetic exchange of <jats:italic>opa</jats:italic> 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 β-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. </jats:p>
  • Zugangsstatus: Freier Zugang