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T Cells1
*
Division of Rheumatology, Department of Internal Medicine and the Interdisciplinary Group in Immunology, University of Iowa College of Medicine, Iowa City, IA 52242;
Structural and Cell Biology Program, Department of Biomedical Sciences, Wadsworth Center, New York State Department of Health, Albany, NY 12201;
Center for Advanced Research in Biotechnology, University of Maryland Biotechnology Institute, Rockville, MD 20850; and
Department of Immunology and Cell Biology, Kyoto University Medical School, Kyoto, Japan
Human V
2V
2+ T cells proliferate in vivo during
many microbial infections. We have found that V2V2+ T
cells recognize nonpeptide prenyl pyrophosphates and alkylamines. We
now have defined structural features that determine the antigenicity of
prenyl pyrophosphates by testing synthetic analogs for bioactivity. We
find that the carbon chain closest to the pyrophosphate moiety plays
the major role in determining bioactivity. Changes in this area, such
as the loss of a double bond, abrogated bioactivity. The loss of a
phosphate from the pyrophosphate moiety also decreased antigenicity
100- to 200-fold. However, nucleotide monophosphates could be added
with minimal changes in bioactivity. Longer prenyl pyrophosphates also
retained bioactivity. Despite differences in CDR3 sequence,
V2V2+ clones and a transfectant responded similarly.
Ag docking into a V2V2 TCR model reveals a potential binding site
in germline regions of the V2J1.2 CDR3 and V2 CDR2 loops.
Thus, V2V2+ T cells recognize a core carbon chain and
pyrophosphate moiety. This recognition is relatively unaffected by
additions at distal positions to the core Ag unit.
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