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Characterization of an anti-Borrelia burgdorferi OspA conformational epitope by limited proteolysis of monoclonal antibody-bound antigen and mass spectrometric peptide mapping

Published online by Cambridge University Press:  01 May 2000

VÉRONIQUE LEGROS
Affiliation:
Institut de Biologie Structurale (CEA-CNRS-UJF), Laboratoire de Spectrométrie de Masse des Protéines, 41 rue Jules Horowitz, 38027 Grenoble Cedex 1, France
COLETTE JOLIVET-REYNAUD
Affiliation:
Unité mixte CNRS-bioMérieux, UMR 103, Ecole Normale Supérieure, 46 allée Italie, 69007 Lyon, France
NICOLE BATTAIL-POIROT
Affiliation:
BioMérieux, Département des Immunoessais, chemin de l'Orme, 69280 Marcy-l'Etoile, France
CHRISTINE SAINT-PIERRE
Affiliation:
Institut de Biologie Structurale (CEA-CNRS-UJF), Laboratoire de Spectrométrie de Masse des Protéines, 41 rue Jules Horowitz, 38027 Grenoble Cedex 1, France
ERIC FOREST
Affiliation:
Institut de Biologie Structurale (CEA-CNRS-UJF), Laboratoire de Spectrométrie de Masse des Protéines, 41 rue Jules Horowitz, 38027 Grenoble Cedex 1, France
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Abstract

Lyme borreliosis is a multisystem disorder caused by the spirochete Borrelia burgdorferi that is transmitted to humans by the tick Ixodes dammini. The immune response against the 31 kDa OspA, which is one of the most abundant B. burgdorferi proteins, appears to be critical in preventing infection and tissue inflammation. Detailed knowledge of the immunological and molecular characteristics of the OspA protein is important for the development of reliable diagnostic assays. In this study, we characterized a new conformational epitope present within the middle part of B. burgdorferi OspA. Our approach used enzymatic proteolyses of the immune complex followed by mass spectrometric identification of the peptides bound to the antibody. It appears to be one of the first reports on the characterization of a discontinuous epitope using mass spectrometry.

Type
Research Article
Copyright
2000 The Protein Society

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