Location of a blocking epitope on outer-membrane protein III of Neisseria gonorrhoeae by synthetic peptide analysis.

Journal of General Microbiology
M Virji, J E Heckels

Abstract

A series of overlapping peptides spanning the deduced amino acid sequence of outer-membrane protein PIII of Neisseria gonorrhoeae have been synthesized on solid-phase supports. The peptides were used in an attempt to locate the epitopes recognized by anti-PIII monoclonal antibodies with defined biological properties. Four bactericidal and two nonbactericidal antibodies were reacted with the synthetic peptides. None of the bactericidal antibodies reacted with the linear peptides. However, the two nonbactericidal antibodies were found to react within the disulphide loop thought to be exposed on the bacterial surface. Monoclonal antibody SM51 recognized a decapeptide corresponding to amino acid residues 24-33, while monoclonal antibody SM50 recognized an octapeptide contained within the decapeptide. The difference in the ability of the two antibodies to block the bactericidal effect of antibodies directed against other surface antigens therefore appears to be related to a difference in their ability to activate complement rather than to the location of the epitope recognized.

Citations

Sep 23, 1998·APMIS : Acta Pathologica, Microbiologica, Et Immunologica Scandinavica·A Z HenriksenL M Wetzler
Mar 1, 1995·Scandinavian Journal of Immunology·S C HuangJ B Harley
Mar 1, 2012·The Journal of Immunology : Official Journal of the American Association of Immunologists·Sunita GulatiSanjay Ram
Mar 7, 2019·Frontiers in Immunology·Angela Lovett, Joseph A Duncan
Jul 21, 2017·PloS One·Daniel O ConnorMarkus von Nickisch-Rosenegk
Sep 16, 2021·Expert Review of Vaccines·Myron ChristodoulidesJohn E Heckels

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