Antibodies to N-terminal peptides of gonococcal porin are bactericidal when gonococcal lipopolysaccharide is not sialylated
| Autor: | Derek L. Stirewalt, Victor A. Varela, Christopher Elkins, Nicholas H. Carbonetti, P. Frederick Sparling, David G. Klapper |
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| Rok vydání: | 1992 |
| Předmět: |
Lipopolysaccharides
Lipopolysaccharide medicine.drug_class Molecular Sequence Data Porins Biology Monoclonal antibody Microbiology Epitope Epitopes chemistry.chemical_compound medicine Animals Amino Acid Sequence Molecular Biology Antiserum Base Sequence Complement System Proteins Antibodies Bacterial N-Acetylneuraminic Acid Neisseria gonorrhoeae Peptide Fragments Sialic acid carbohydrates (lipids) chemistry Cytidine Monophosphate N-Acetylneuraminic Acid Porin Sialic Acids biology.protein Rabbits Antibody N-Acetylneuraminic acid Bacterial Outer Membrane Proteins |
| Zdroj: | Molecular Microbiology. 6:2617-2628 |
| ISSN: | 1365-2958 0950-382X |
| DOI: | 10.1111/j.1365-2958.1992.tb01439.x |
| Popis: | Six synthetic 25-mer peptides corresponding to certain presumed surface-exposed regions of gonococcal porin protein I (PI) were made from strains FA19 (PIA) and MS11 (PIB). Four peptides were immunogenic in rabbits. Affinity-purified antisera against both PIA and PIB N-terminal peptides were bactericidal for homologous gonococci and many heterologous PI serovars. However, sialylation of gonococcal lipopolysaccharide (LPS) by growth of gonococci in the presence of cytidine monophosphate-neuraminic acid (CMP-NANA) abrogated the bactericidal activity of these antisera. Binding of anti-PI monoclonal antibodies to whole gonococci was reduced two- to fourfold by sialylation of LPS, suggesting that sialylation may inhibit bactericidal activity by masking porin epitopes. However, binding of anti-PII (Opa) monoclonal antibodies was not inhibited, yet complement-mediated killing was inhibited by sialylated LPS. Binding of complement components C3 and C9 was inhibited in the presence of either anti-PI or anti-PII monoclonals when gonococci were grown in the presence of CMP-NANA. Thus sialylation inhibited both anti-PI antibody binding and complement deposition, with a resultant decrease in bactericidal activity. |
| Databáze: | OpenAIRE |
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