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.

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