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Cells Directly Recognize the Peptide Backbone in a Conformationally Dependent Manner1
Committee on Immunology and Ben May Institute for Cancer Research, University of Chicago, Chicago, IL 60637
Despite the description of numerous antigenic ligands recognized by
TCR
cells, detailed information concerning the structural nature
of these antigenic epitopes is lacking. In addition, the recent
descriptions of human TCR cells recognizing mycobacterium-derived
low m.w. lipid molecules confirms that the spectrum and nature of
biologic structures that are capable of being recognized by TCR
cells are unclear. We have previously described a murine TCR cell
clone, TgI4.4, that is reactive to herpes simplex virus (HSV)-1
glycoprotein I (gI). Unlike TCR
ß-mediated, MHC-restricted Ag
recognition but similar to Ig Ag recognition, TgI4.4 recognizes
purified gI directly, in the absence of Ag processing or presentation.
Since gI is a complex glycoprotein, the nature of the antigenic epitope
was investigated. First, gI recognition by TgI4.4 is conformationally
dependent, as revealed by denaturation and proteolytic experiments.
Secondly, the epitope recognized by TgI4.4 was mapped to the amino
terminus by using insertion mutants of gI. Lastly, TgI4.4 recognizes
the gI protein directly since completely deglycosylated forms of gI are
efficiently recognized. Therefore, TCR cells are capable of
recognizing a variety of molecular structures, including proteins. The
ability of TgI4.4 to recognize a nonglycosylated form of gI suggests
that HSV-1 recognition by TCR cells in vivo is not limited by
cell-specific glycosylation patterns or glycosylation-dependent
conformational influences.
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