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- Several natural SL9 variants were shown to bind comparably well to soluble HLA-A2 and D3 TCR. All variants had remarkably similar peptide conformations as evidenced by high resolution crystal structures of soluble interacting proteins. These structures were shown to differ from other peptide-MHC-TCR structures. SL9 variation was shown to be partially restricted by its context in the HIV p17 matrix protein, and the preservation of peptide conformation despite epitope variation may contribute to the persistence of SL9-mediated immune responses.
- 11 Natural variants of SLYNTVATL were tested. They were SLYNTiATL (SL9-6I), SLYNTiAvL (SL9-6I/8V), SLYNTVAvL (SL9-8V), SLfNTVATL (SL9-3F), SLfNTiAvL (SL9-3F/6I/8V), SLfNTiATL (SL9-3F/6I), SLfNTVAvL (SL9-3F/8V), SLYNaVATL (SL9-5A), SLYNsVATL (SL9-5S), SLYNaiATL (SL9-5A/6I), SLYNlVAvL (SL9-5L/8V). Only variants at P5 where Threonine is substituted by Alanine or Leucine abrogated activity, while all others variants were active. No natural variants had substitutions at P4, while P1, P2 and P9 were also conserved. 9 synthetic variants were also tested.
- This degenerate recognition of the HIV Gag epitope by CTL is different from other viral peptide-degeneracies in that several CTL clones can perform equally well in recognition of the SL9 pMHC, and there is not necessarily one dominant recognition.
Erik Martinez-Hackert, Nadia Anikeeva, Spyros A. Kalams, Bruce D. Walker, Wayne A. Hendrickson, and Yuri Sykulev. Structural Basis for Degenerate Recognition of Natural HIV Peptide Variants by Cytotoxic Lymphocytes. J. Biol. Chem., 281(29):20205-20212, 21 Jul 2006. PubMed ID: 16702212.
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