Identification of the nonamer peptide from influenza A matrix protein and the role of pockets of HLA-A2 in its recognition by cytotoxic T lymphocytes

Eur J Immunol. 1992 Apr;22(4):903-7. doi: 10.1002/eji.1830220404.

Abstract

Influenza matrix peptide 58-66 is shown to be the optimal nonamer for binding to HLA-A2 and presentation to cytotoxic T lymphocytes (CTL). If titered out to 2 x 10(-10) - 4 x 10(-10) M in CTL-mediated lysis assays and to 3 x 10(-9) M in an HLA-A2 assembly-stabilization assay in cell lysates. The peptide was shown to make probable contacts with its carboxy terminus close to residue 116 in the floor of the cleft of HLA-A2, close to the F pocket. The side chain of the amino-terminal amino acid was unimportant, but its free amino and carbonyl groups in the A pocket appeared important in optimizing peptide presentation. The B pocket probably accommodates the side chain of residue 2 (isoleucine) and was shown to be critical in peptide presentation.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Antigens, Viral / chemistry
  • Antigens, Viral / immunology*
  • Cells, Cultured
  • Cytotoxicity, Immunologic
  • Epitopes
  • HLA-A2 Antigen / chemistry
  • HLA-A2 Antigen / immunology*
  • In Vitro Techniques
  • Influenza A virus / immunology*
  • Molecular Sequence Data
  • Peptides / chemistry
  • Peptides / immunology
  • Structure-Activity Relationship
  • T-Lymphocytes, Cytotoxic / immunology*
  • Viral Matrix Proteins / chemistry
  • Viral Matrix Proteins / immunology*

Substances

  • Antigens, Viral
  • Epitopes
  • HLA-A2 Antigen
  • M-protein, influenza virus
  • Peptides
  • Viral Matrix Proteins