The Journal of Experimental Medicine
Avanti Polar Lipids, Inc.
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents
This Article
Right arrow Full Text
Right arrow Full Text (PDF, 144K)
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 HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Crowley, M. P.
Right arrow Articles by Chien, Y.-h.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Crowley, M. P.
Right arrow Articles by Chien, Y.-h.
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, 0022-1007/1997/4/1223/ $5.00
The Journal of Experimental Medicine, Volume 185, Number 7, April 7, 1997 1223-1230

Article

The Recognition of the Nonclassical Major Histocompatibility Complex (MHC) Class I Molecule, T10, by the {gamma}{delta} T Cell, G8

Michael P. Crowley*, Ziv Reich{ddagger}, Nasim Mavaddat§, John D. Altman§, and Yueh-hsiu Chien*,§

From the * Program in Immunology; {ddagger} The Howard Hughes Medical Institute; and the § Department of Microbiology and Immunology, Stanford University School of Medicine, Stanford, California 94305

Recent studies have shown that many nonclassical major histocompatibility complex (MHC) (class Ib) molecules have distinct antigen-binding capabilities, including the binding of nonpeptide moieties and the binding of peptides that are different from those bound to classical MHC molecules. Here, we show that one of the H-2T region–encoded molecules, T10, when produced in Escherichia coli, can be folded in vitro with β2-microglobulin (β2m) to form a stable heterodimer in the absence of peptide or nonpeptide moieties. This heterodimer can be recognized by specific antibodies and is stimulatory to the {gamma}{delta} T cell clone, G8. Circular dichroism analysis indicates that T10/β2m has structural features distinct from those of classical MHC class I molecules. These results suggest a new way for MHC-like molecules to adopt a peptide-free structure and to function in the immune system.

Address correspondence to Dr. Y.-h. Chien, D333 Fairchild Building, Department of Microbiology and Immunology, Stanford University, School of Medicine, Stanford, California 94305. The current address of N. Mavaddat is the Walter and Eliza Hall Institute of Medical Research, The Royal Melbourne Hospital, Victoria 3050, Australia.

M.P. Crowley was supported by a fellowship from the National Science Foundation. Z. Reich was supported by The Rothchild Foundation, Israel, and is currently supported by The Howard Hughes Medical Institute. N. Mavaddat is supported by the National Health and Medical Research Council of Australia. We also thank the National Institutes of Health for grant support.

1Abbreviations used in this paper: CD, circular dichroic; FcRn, rat neonatal Fc receptor; IPTG, isopropyl β-D-thiogalactopyranoside.


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?


This article has been cited by other articles:



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