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A more recent version of this article appeared on December 1, 2003

Published online before print September 12, 2003
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© by The Society for Leukocyte Biology
Journal of Leukocyte Biology, doi:10.1189/jlb.0403138

Received for publication April 4, 2003.
Revised July 3, 2003.
Accepted for publication August 4, 2003.

Article

Human CD8+ T cells recognize epitopes of the 28-kDa hemolysin and the 38-kDa antigen of Mycobacterium tuberculosis

Homayoun Shams *{dagger}@, Peter F. Barnes *{dagger}{ddagger}, Stephen E. Weis §, Peter Klucar *{dagger}, and Benjamin Wizel *{dagger}

*Center for Pulmonary and Infectious Disease Control, Departments of {dagger}Microbiology and Immunology and {ddagger}Medicine, University of Texas Health Center, Tyler; and §Department of Internal Medicine, University of North Texas Health Sciences Center, Fort Worth

@ To whom correspondence should be addressed. E-mail: amir.shams{at}uthct.edu.


  Abstract

Mycobacterium tuberculosis antigens that are recognized by human CD8+ T cells are potentially important vaccine target molecules. We used a motif-based strategy to screen selected proteins of M. tuberculosis for peptides predicted to bind to human leukocyte antigen (HLA)-A*0201. We identified two 10 amino acid peptides that elicited cytolytic T lymphocyte activity and interferon-{gamma} production by CD8+ T cells from HLA-A*0201+ healthy tuberculin reactors. These peptides were derived from the 38-kDa antigen and the 28-kDa hemolysin, the latter being a novel target for CD8+ T cells. We speculate that hemolysins may alter the phagosomal membrane surrounding intracellular M. tuberculosis, allowing themselves and other antigens to gain access to the major histocompatibility complex class I processing pathway.

Key Words: cytolytic T lymphocyte • HLA-A*0201 • bacillus Calmette-Guerin






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