J Med Microbiol International Journal of Systematic and Evolutionary Microbiology
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
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
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Lin, Y. S.
Right arrow Articles by Rogers, T. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Lin, Y. S.
Right arrow Articles by Rogers, T. J.
Agricola
Right arrow Articles by Lin, Y. S.
Right arrow Articles by Rogers, T. J.

The Journal of Medical Microbiology, Vol 27, Issue 4 263-270, Copyright © 1988 by Society for General Microbiology

JOURNAL ARTICLE

Production and characterisation of monoclonal antibodies specific for staphylococcal enterotoxin B

Y. S. Lin, M. T. Largen, J. R. Newcomb and T. J. Rogers
Department of Microbiology and Immunology, Temple University School of Medicine, Philadelphia, Pennsylvania 19140.

We have generated monoclonal antibodies (MABs) to staphylococcal enterotoxin B (SEB) in BALB/c mice. Five out of 20 clones which produce anti-SEB MABs have been characterised. Among them, three produce IgG1/kappa, one produces IgM/lambda, and one apparently produces both IgG1/lambda and IgM/lambda MABs. The anti-SEB titres of ascites fluids range from 3200 to greater than 819200 by ELISA. All of the MABs analysed thus far neutralise the mitogenic response of BALB/c splenocytes to a suboptimal dose of SEB. Also, the induction of suppressor cells by SEB in vitro is reversed by pre-incubating SEB with these MABs. Limited digestion with chymotrypsin, trypsin or Staphylococcus aureus V8 protease yields peptide fragments which have been tested by Western-blot analysis. MABs 1FD7 and 2GD9 are specific for the carboxy-terminal end of SEB, and have a similar, but not identical, binding epitope. MABs 2DA3 and 2HA10 bind to intact SEB but not to cleaved products, and are probably specific for antigenic determinants altered by the cleavage or by the denaturing conditions of the electrophoresis, or by both.




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
INT J SYST EVOL MICROBIOL J MED MICROBIOL MICROBIOLOGY J GEN VIROL ALL SGM JOURNALS
Copyright © 1988 Society for General Microbiology.