Characterization of a new H-2Dk-restricted epitope prominent in primary influenza A virus infection

• Published in: Journal of general virology Vol. 82; no. 7; pp. 1749 - 1755
• Main Authors: Tourdot, Sophie, Herath, Shan, Gould, Keith G
• Format: Journal Article
• Language: English
• Published: Soc General Microbiol 01-07-2001
• ISSN: 0022-1317; 1465-2099
• DOI: 10.1099/0022-1317-82-7-1749

Department of Immunology, Imperial College School of Medicine (St Mary’s Campus), Norfolk Place, London W2 1PG, UK 1
Author for correspondence: Keith Gould. Fax [phone]. e-mail k.gould{at}ic.ac.uk
Influenza A virus infection of mice has been used extensively as a model to investigate the mechanisms of antigen presentation to cytotoxic T lymphocytes (CTL) and the phenomenon of immunodominance in antiviral CTL responses. The different virus-encoded epitopes that are recognized in H-2 b and H-2 d mice have been characterized and their relative immunodominance has been well-studied. In H-2 k mice, four different K k -restricted influenza virus epitopes have been described, but the dominance hierarchy of these epitopes is unknown and there is also an uncharacterized D k -restricted response against the virus. In this study, a D k -restricted epitope derived from the influenza virus A/PR/8/34 polymerase protein PB1, corresponding to amino acid residues 349–357 (ARLGKGYMF), was identified. This peptide is the major epitope within the PB1 polymerase and is at least as dominant as any of the four K k -restricted epitopes that are recognized in CBA mice following primary influenza virus infection. The PB1 epitope is only the fourth D k -presented peptide to be reported and the sequence of this epitope confirms a D k -restricted peptide motif, consisting of arginine at position two, arginine or lysine at position five and a hydrophobic residue at the carboxy terminus.