NDLI: Mapping antibody-binding domains of the major outer surface membrane protein (OspA) of Borrelia burgdorferi.

Content Provider	PubMed Central
Author	Schubach, W. H. Mudri, S. Dattwyler, R. J. Luft, B. J.
Abstract	The major outer surface membrane protein of Borrelia burgdorferi, OspA, is one of several antigens recognized by sera from some patients in the chronic phase of Lyme borreliosis. We have expressed the OspA open reading frame in Escherichia coli and generated a series of deletion constructs of the gene and expressed them as trpE fusion proteins in E. coli. These constructs were used to identify antibody-binding sites of both rabbit antiserum and mouse monoclonal antibodies (MAbs) directed against OspA. All antibodies tested failed to bind to a fusion protein containing the first 61 amino acids of OspA, suggesting that the amino-terminal domain of OspA is unexposed to the cell surface. The binding site for one MAb, 184.1, was identified in a region centered around amino acid 61, while the binding site for MAb 105.5 was identified in a region centered around amino acids 214 to 217. Sera from two patients which were reactive to OspA identified distinct epitopes that lie between those recognized by our MAbs.
Starting Page	1911
File Format	PDF
ISSN	10985522
e-ISSN	10985522
Journal	Infection and Immunity
Issue Number	6
Volume Number	59
Language	English
Publisher Date	1991-06-01
Access Restriction	Open
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Infectious Diseases Parasitology Immunology Microbiology

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Mapping antibody-binding domains of the major outer surface membrane protein (OspA) of Borrelia burgdorferi.