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.
journal_name
Eur J Immunoljournal_title
European journal of immunologyauthors
Morrison J,Elvin J,Latron F,Gotch F,Moots R,Strominger JL,McMichael Adoi
10.1002/eji.1830220404keywords:
subject
Has Abstractpub_date
1992-04-01 00:00:00pages
903-7issue
4eissn
0014-2980issn
1521-4141journal_volume
22pub_type
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