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 McDonnell, J. M.
Right arrow Articles by Jameson, B. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by McDonnell, J. M.
Right arrow Articles by Jameson, B. A.

The Journal of Immunology, Vol 149, Issue 5 1626-1630, Copyright © 1992 by American Association of Immunologists

ARTICLES

Direct involvement of the CDR3-like domain of CD4 in T helper cell activation

JM McDonnell, KJ Blank, PE Rao and BA Jameson
Jefferson Cancer Institute, Thomas Jefferson University, Philadelphia, PA 19107.

The CD4 glycoprotein, a member of the Ig super-family, has long been known to play an important role in the immunologic activation of Th cells. The precise manner in which CD4 participates in this activation process is not yet understood. In an attempt to further define its role in Th cell activation, we modeled the D1 domain of the murine CD4 protein (L3T4) based on the experimentally determined high resolution structure of the human CD4 protein. Because the D1 domain of CD4 strongly resembles the V kappa chain of an antibody, we addressed the question of whether the CDR-like regions of CD4 are also involved in mediating protein-protein interactions. Consequently, we used the modeled L3T4 structure as a template in the design of conformational mimics of the CDR3-like region (residues 86-94). Only the analog designed to mimic both the sequence and conformation of this region exhibited highly specific inhibition of CD4-dependent responses. Because the inhibitory activity could be localized to the Th cell itself, it appears that this analog acts by uncoupling a CD4 association (independent of an APC) critical to generating a proliferative response.


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
C. Monnet, D. Laune, J. Laroche-Traineau, M. Biard-Piechaczyk, L. Briant, C. Bes, M. Pugniere, J.-C. Mani, B. Pau, M. Cerutti, et al.
Synthetic Peptides Derived from the Variable Regions of an Anti-CD4 Monoclonal Antibody Bind to CD4 and Inhibit HIV-1 Promoter Activation in Virus-infected Cells
J. Biol. Chem., February 5, 1999; 274(6): 3789 - 3796.
[Abstract] [Full Text] [PDF]

Home page
 J. Immunol.Home page
U. Koch, S. Choksi, L. Marcucci, and R. Korngold
A Synthetic CD4-CDR3 Peptide Analog Enhances Skin Allograft Survival Across a MHC Class II Barrier
J. Immunol., July 1, 1998; 161(1): 421 - 429.
[Abstract] [Full Text] [PDF]

Home page
 BloodHome page
U. Koch and R. Korngold
A Synthetic CD4-CDR3 Peptide Analog Enhances Bone Marrow Engraftment Across Major Histocompatibility Barriers
Blood, April 15, 1997; 89(8): 2880 - 2890.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
T. M. Friedman, A. P. Reddy, R. Wassell, B. A. Jameson, and R. Korngold
Identification of a Human CD4-CDR3-like Surface Involved in CD4+ T Cell Function
J. Biol. Chem., September 13, 1996; 271(37): 22635 - 22640.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
This Website Copyright © 1992 by The American Association of Immunologists, Inc. All rights reserved.
All Contents Copyright © 1992 by The American Association of Immunologists, Inc. All rights reserved.