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*
Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA 02215; and
Wisconsin Regional Primate Research Center and Department of Pathology and Laboratory Medicine, University of Wisconsin, Madison, WI 53715
The ability of an AIDS virus to escape from immune containment by
selective mutation away from recognition by CTL was explored in simian
immunodeficiency virus of macaques (SIVmac)-infected rhesus monkeys.
CTL recognition of a previously defined common viral mutation in an
immunodominant SIVmac Gag epitope was evaluated. CTL were assessed for
their ability to recognize a SIVmac Gag protein with a single residue 2
(T 
A) replacement in the minimal epitope peptide bound by the MHC
class I molecule Mamu-A*01. SIVmac Gag-specific CTL lysed
Mamu-A*01+ target cells infected with recombinant vaccinia
virus expressing the wild-type but not the mutant Gag protein. In
addition, CTL recognized the mutant epitope peptide less efficiently
than the wild-type virus peptide. In studies to determine the mechanism
by which the mutant virus evaded CTL recognition, this peptide was
shown to bind Mamu-A*01 in a manner that was indistinguishable from the
wild-type peptide. However, experiments in which an increasing duration
of delay was introduced between peptide sensitization of target cells
and the assessment of these cells as targets in killing assays suggest
that the mutant peptide with a T A replacement had a higher
off-rate from Mamu-A*01 than the wild-type peptide did. Therefore,
these findings suggest that AIDS viruses can evade virus-specific CTL
responses through the accelerated dissociation of mutant peptide from
MHC class I.
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