JBC Ideal method for primary cell transfection

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J Biol Chem, Vol. 274, Issue 51, 36422-36427, December 17, 1999

Poor Binding of a HER-2/neu Epitope (GP2) to HLA-A2.1 Is due to a Lack of Interactions with the Center of the Peptide*

Jennifer J. KuhnsDagger , Michael A. Batalia§, Shuqin YanDagger , and Edward J. CollinsDagger §||

From the Dagger  Department of Microbiology and Immunology, § Lineberger Comprehensive Cancer Center, and the  Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, North Carolina 27599

Class I major histocompatibility complex (MHC) molecules bind short peptides derived from proteins synthesized within the cell. These complexes of peptide and class I MHC (pMHC) are transported from the endoplasmic reticulum to the cell surface. If a clonotypic T cell receptor expressed on a circulating T cell binds to the pMHC complex, the cell presenting the pMHC is killed. In this manner, some tumor cells expressing aberrant proteins are recognized and removed by the immune system. However, not all tumors are recognized efficiently. One reason hypothesized for poor T cell recognition of tumor-associated peptides is poor binding of those peptides to class I MHC molecules. Many peptides, derived from the proto-oncogene HER-2/neu have been shown to be recognized by cytotoxic T cells derived from HLA-A2+ patients with breast cancer and other adenocarcinomas. Seven of these peptides were found to bind with intermediate to poor affinity. In particular, GP2 (HER-2/neu residues 654-662) binds very poorly even though it is predicted to bind well based upon the presence of the correct HLA-A2.1 peptide-binding motif. Altering the anchor residues to those most favored by HLA-A2.1 did not significantly improve binding affinity. The crystallographic structure shows that unlike other class I-peptide structures, the center of the peptide does not assume one specific conformation and does not make stabilizing contacts with the peptide-binding cleft.

* This work was supported by National Institutes of Health Grants AI 29324 and CA 58223 and Department of Defense Grants DAMD17-970-1-7052 (to E. J. C.) and DAMD17-98-1-8219 (to M. A. B.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The atomic coordinates and structure factors (code 1QR1) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org).

|| To whom correspondence should be addressed: Dept. of Microbiology and Immunology, University of North Carolina, CB#7290, 804 M. E. Jones Bldg, Chapel Hill, NC 27599. Tel.: 919-966-6869; Fax: 919-962-8103; E-mail: collins1@med.unc.edu.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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