Class I MHC can present an endogenous peptide to cytotoxic T lymphocytes.
Since class I MHC glycoproteins may function by "screening and selecting" degraded proteins, we wished to determine whether very short peptides made within a cell were detected and bound by MHC, and presented for T cell perusal. We show that a 22 amino acid viral sequence containing a Db-restricted nonameric CTL epitope is sufficient to direct CTL recognition/lysis of H2b target cells. The mechanism of epitope presentation is by the "natural" endogenous route, and appears to direct lysis as effectively as wild-type virus infection, in which the epitope is part of a 236 residue glycoprotein.
Whitton
J L
JL
Research Institute of Scripps Clinic, La Jolla, California 92037.
Oldstone
M B
MB
D000818:Animals; D000939:Epitopes / Q000032:analysis*; D005805:Genes, MHC Class I; D006801:Humans; D008217:Lymphocytic choriomeningitis virus / Q000235:genetics; D051379:Mice; D008807:Mice, Inbred BALB C; D008810:Mice, Inbred C57BL; D013602:T-Lymphocytes, Cytotoxic / Q000276:immunology*; D014764:Viral Proteins / Q000276:immunology*
D000939:Epitopes; D014764:Viral Proteins