The Journal of Experimental Medicine
Torrey Pines Biolabs
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents

This Article
Right arrow Full Text
Right arrow Full Text (PDF, 158K)
Right arrow PPT slides of all figures
Right arrow Alert me when this article is cited
Right arrow Citation Map
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new content in the JEM
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Hodtsev, A. S.
Right arrow Articles by Posnett, D. N.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hodtsev, A. S.
Right arrow Articles by Posnett, D. N.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Facebook   Add to Reddit   Add to Technorati   Add to Twitter  
What's this?
© The Rockefeller University Press, 0022-1007/1998/2/319/ $5.00
The Journal of Experimental Medicine, Volume 187, Number 3, February 2, 1998 319-327


Articles

Mycoplasma Superantigen Is a CDR3-dependent Ligand for the T Cell Antigen Receptor

Andrew S. Hodtsev*, Yongwon Choi{ddagger}, Eugenia Spanopoulou§, and David N. Posnett||

From the * Ruttenberg Cancer Center, Mount Sinai School of Medicine, New York 10029; the {ddagger} Howard Hughes Medical Institute, The Rockefeller University, New York 10021; the § Howard Hughes Medical Institute, Ruttenberg Cancer Center, Mount Sinai School of Medicine, New York 10029; and the || Immunology Program, Graduate School of Medical Sciences, and the Department of Medicine, Cornell University Medical College, New York 10021

Superantigens are defined as proteins that activate a large number of T cells through interaction with the Vβ region of the T cell antigen receptor (TCR). Here we demonstrate that the superantigen produced by Mycoplasma arthritidis (MAM), unlike six bacterial superantigens tested, interacts not only with the Vβ region but also with the CDR3 (third complementarity-determining region) of TCR-β. Although MAM shares typical features with other superantigens, direct interaction with CDR3-β is a feature of nominal peptide antigens situated in the antigen groove of major histocompatibility complex (MHC) molecules rather than superantigens. During peptide recognition, Vβ and V{alpha} domains of the TCR form contacts with MHC and the complex is stabilized by CDR3–peptide interactions. Similarly, recognition of MAM is Vβ-dependent and is apparently stabilized by direct contacts with the CDR3-β region. Thus, MAM represents a new type of ligand for TCR, distinct from both conventional peptide antigens and other known superantigens.


Address correspondence to Andrew S. Hodtsev, Mount Sinai School of Medicine, Ruttenberg Cancer Center, 1 Gustave Levy Place, New York, NY 10029. Phone: 212-824-8123; Fax: 212-849-2446; E-mail: andrew_hodtsev{at}smtplink.mssm.edu

1 Abbreviations used in this paper: MAM, Mycoplasma arthritidis mitogen; MMTV, mouse mammary tumor virus; SE, staphylococcal enterotoxin.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Facebook Facebook   Add to Reddit Reddit   Add to Technorati Technorati   Add to Twitter Twitter    What's this?




  Home | Help | Feedback | Subscriptions | Archive | Search
TABLE OF CONTENTS