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Science 14 August 1992:
Vol. 257. no. 5072, pp. 964 - 967
DOI: 10.1126/science.1380181
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Articles

Science, Vol 257, Issue 5072, 964-967
Copyright © 1992 by American Association for the Advancement of Science

articles

A critical role for conserved residues in the cleft of HLA-A2 in presentation of a nonapeptide to T cells

F Latron, L Pazmany, J Morrison, R Moots, MA Saper, A McMichael, and JL Strominger

Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA 02115.

The peptide binding cleft of the class I human histocompatibility antigen, HLA-A2, contains conserved amino acid residues clustered in the two ends of the cleft in pockets A and F as well as polymorphic residues. The function of two conserved tyrosines in the A pocket was investigated by mutating them to phenylalanines and of a conserved tyrosine and threonine in the F pocket by mutating them to phenylalanine and valine, respectively. Presentation of influenza virus peptides and of intact virus to cytolytic T lymphocytes (CTLs) was then examined. The magnitude of the reduction seen by the mutation of the two tyrosines in the A pocket suggests that hydrogen bonds involving them have a critical function in the binding of the NH2-terminal NH3+ of the peptide nonamer and possibly of all bound peptide nonamers. In contrast, the mutations in the F pocket had no effect on CTL recognition.


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