The minimum peptide epitope from the influenza virus matrix protein. Extra and intracellular loading of HLA-A2.
Influenza virus matrix protein-derived peptides were synthesized based on the amino acid motifs for HLA-A2 bound self peptides. Among these peptides a nonamer (amino acids 58 through 66: G I L G F V F T L) was found to be 100 to 1000 times more effective than the commonly used peptide 57-68 (K G I L G F V F T L T V) in sensitizing HLA-A2+ target cells to lysis by influenza virus specific cytotoxic T lymphocytes. The sensitizing activity of the 12-mer 57-68 was not due to contamination with shorter and more active peptides. Intracellular expression of peptide 58-66 (mediated by a stable expression plasmid with DNA coding for this peptide) also sensitized HLA-A2+ cells to lysis. Peptide 58-66 stimulated human PBMC to generate CTL that recognized peptides 58-66 and 57-68 in association with HLA-A2.
Bednarek
M A
MA
Department of Biophysical Chemistry, Merck Sharp and Dohme Research Laboratories, Rahway, NJ 07065.
Sauma
S Y
SY
Gammon
M C
MC
Porter
G
G
Tamhankar
S
S
Williamson
A R
AR
Zweerink
H J
HJ
D000595:Amino Acid Sequence; D001483:Base Sequence; D000939:Epitopes / Q000032:analysis*; D015789:HLA-A2 Antigen / Q000276:immunology*; D006801:Humans; D008969:Molecular Sequence Data; D009975:Orthomyxoviridae / Q000276:immunology*; D010446:Peptide Fragments / Q000276:immunology*; D013602:T-Lymphocytes, Cytotoxic / Q000276:immunology; D014763:Viral Matrix Proteins / Q000276:immunology*
D000939:Epitopes; D015789:HLA-A2 Antigen; C031540:M-protein, influenza virus; D010446:Peptide Fragments; D014763:Viral Matrix Proteins