T cell recognition of MHC class II-associated peptides is independent of peptide affinity for MHC and sodium dodecyl sulfate stability of the peptide/MHC complex. Effects of conservative amino acid substitutions at anchor position 1 of influenza matrix protein19-31. J Immunol 1996 May 15;156(10):3815-20
Date
05/15/1996Pubmed ID
8621918Scopus ID
2-s2.0-0029963942 (requires institutional sign-in at Scopus site) 22 CitationsAbstract
T cells recognize peptide fragments of Ags bound to MHC-encoded molecules. Pockets in the MHC peptide-binding groove accommodate a limited set of amino acid side chains present at anchor positions in peptide; however, the functional significance of accommodation of different side chains at an anchor position in peptide is not clear. A panel of T cell clones was evaluated to test the effect of conservative amino acid substitution at a primary peptide anchor position. Results of T cell stimulation studies were correlated with two well studied characteristics of the peptide/MHC complex, which are the affinity of peptide binding to MHC and the stability of the resulting complex upon PAGE in the presence of SDS. We found that formation of a functional complex required neither high affinity peptide binding nor SDS stability. Furthermore, T cell clones differed in their ability to recognize individual peptide variants, suggesting that some structural aspect of the peptide/MHC complex is influenced by interactions between peptide anchor residues and MHC pockets.
Author List
Wu S, Gorski J, Eckels DD, Newton-Nash DKAuthor
Debra K. Newman PhD Investigator in the Blood Research Institute department at BloodCenter of WisconsinMESH terms used to index this publication - Major topics in bold
Amino Acid SequenceAmino Acids
Drug Stability
Electrophoresis, Polyacrylamide Gel
HLA-DR Antigens
HLA-DRB1 Chains
Humans
Influenza A virus
Molecular Sequence Data
Peptides
Protein Binding
Sodium Dodecyl Sulfate
T-Lymphocytes
Viral Matrix Proteins
