The JI
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     
 

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Jiang, W.
Right arrow Articles by Gorevic, P. D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Jiang, W.
Right arrow Articles by Gorevic, P. D.

The Journal of Immunology, Vol 144, Issue 1 284-289, Copyright © 1990 by American Association of Immunologists

ARTICLES

Cross-antigenicity between the major surface proteins (ospA and ospB) and other proteins of Borrelia burgdorferi

W Jiang, BJ Luft, P Munoz, RJ Dattwyler and PD Gorevic
Department of Medicine, State University of New York, Stony Brook 11794.

Two of the major surface Ag of Borrelia burgdorferi, the 31-kDa OspA and 34-kDa OspB proteins, are encoded by a 49-kb plasmid. In this study, mAb and monospecific polyclonal antibodies were used to define cross-antigenicity of the OspA and OspB protein to each other and to other lower molecular mass proteins by Western blot analysis. Two mAb studied, 105.5 and 184.1, were directed predominantly against the 31- kDa OspA protein. However, each also reacted with other minor bands, though with different specificities. Using V8 protease digestion and cleavage by cyanogen bromide, we demonstrated that each mAb reacted to the 31-kDa protein differently. Monospecific polyclonal rabbit and human antibodies directed against the 34-, 31-, 22-, and 20-kDa proteins were eluted from blots and used to further corroborate the cross-reactivity among these Ag. Rabbit antibodies to the 31- and 22- kDa Ag gave remarkably similar peptide maps after V8 protease digestion of the 31-kDa OspA protein, as did mAb 184.1, suggesting that this mAb recognized an immunodominant epitope common to the 22- and 31-kDa proteins. It seems likely therefore that the humoral immune response to Borrelia surface Ag may be due to a limited number of cross-reactive epitopes on distinct, but related, gene products.


This article has been cited by other articles:


Home page
 J. Clin. Microbiol.Home page
M. J. C. Gomes-Solecki, G. P. Wormser, M. Schriefer, G. Neuman, L. Hannafey, J. D. Glass, and R. J. Dattwyler
Recombinant Assay for Serodiagnosis of Lyme Disease Regardless of OspA Vaccination Status
J. Clin. Microbiol., January 1, 2002; 40(1): 193 - 197.
[Abstract] [Full Text] [PDF]

Home page
 Arch Intern MedHome page
M. J. C. Gomes-Solecki, G. P. Wormser, D. H. Persing, B. W. Berger, J. D. Glass, X. Yang, and R. J. Dattwyler
A First-Tier Rapid Assay for the Serodiagnosis of Borrelia burgdorferi Infection
Arch Intern Med, September 10, 2001; 161(16): 2015 - 2020.
[Abstract] [Full Text] [PDF]

Home page
 J. Clin. Microbiol.Home page
M. J. C. Gomes-Solecki, J. J. Dunn, B. J. Luft, J. Castillo, D. E. Dykhuizen, X. Yang, J. D. Glass, and R. J. Dattwyler
Recombinant Chimeric Borrelia Proteins for Diagnosis of Lyme Disease
J. Clin. Microbiol., July 1, 2000; 38(7): 2530 - 2535.
[Abstract] [Full Text]

Home page
 Proc. Natl. Acad. Sci. USAHome page
H. Li, J. J. Dunn, B. J. Luft, and C. L. Lawson
Crystal structure of Lyme disease antigen outer surface protein A complexed with an Fab
PNAS, April 15, 1997; 94(8): 3584 - 3589.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
This Website Copyright © 1990 by The American Association of Immunologists, Inc. All rights reserved.
All Contents Copyright © 1990 by The American Association of Immunologists, Inc. All rights reserved.