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Expert Rev Proteomics. 2006 Dec;3(6):641-52.

Direct class I HLA antigen discovery to distinguish virus-infected and cancerous cells.

Author information

1
University of Oklahoma, Department of Microbiology and Immunology, University of Oklahoma Health Sciences Center, 975 NE, 10 Street, BRC Room 317, Oklahoma City, OK 73104, USA. angela-gilb@ouhsc.edu

Abstract

Class I human leukocyte antigen molecules are nature's proteome-scanning chips, presenting thousands of endogenously loaded peptides on the surface of virtually every cell in the body. Cytotoxic T cells survey the class I human leukocyte antigen peptide cargo presented, recognize peptides unique to unhealthy cells and destroy diseased cells. A precise understanding of how class I molecules distinguish diseased cells is positioned to drive immune-based diagnostics, therapies and vaccines. When identifying epitopes unique to unhealthy cells, the most experimentally direct approach is to examine the class I-presented peptides of infected/cancerous cells. Here we discuss the strategies adapted for protein production, protein/peptide purification, peptide separation and for maintaining experimental reproducibility during the direct characterization of class I human leukocyte antigen peptides.

PMID:
17181478
DOI:
10.1586/14789450.3.6.641
[Indexed for MEDLINE]

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