This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Tamura, M. Articles by Ennis, F. A. Search for Related Content PubMed PubMed Citation Articles by Tamura, M. Articles by Ennis, F. A.

 Previous Article  |  Next Article 

Journal of Virology, November 1998, p. 9404-9406, Vol. 72, No. 11
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Definition of Amino Acid Residues on the Epitope Responsible for Recognition by Influenza A Virus H1-Specific, H2-Specific, and H1- and H2-Cross-Reactive Murine Cytotoxic T-Lymphocyte Clones

Manabu Tamura, Koichi Kuwano, Ichiro Kurane,^§ and Francis A. Ennis^*

Center for Infectious Disease and Vaccine Research, University of Massachusetts Medical Center, Worcester, Massachusetts

Received 27 April 1998/Accepted 12 August 1998

We defined the epitopes recognized by three influenza A virus-specific, H-2K^d-restricted CD8⁺ cytotoxic T-lymphocyte (CTL) clones: H1-specific clone A-12, H2-specific clone F-4, and H1- and H2-cross-reactive clone B7-B7. The A-12 and B7-B7 clones recognized the same peptide, which comprises amino acids 533 to 541 (IYSTVASSL) of A/PR/8 hemagglutinin (HA). The F-4 and B7-B7 clones both recognized the peptide which comprise amino acids 529 to 537 (IYATVAGSL) of A/Jap HA. Amino acids 533 to 541 of A/PR/8 HA are compatible with amino acids 529 to 537 of A/Jap HA. Amino acid S at positions 3 and 7 was responsible for recognition by H1-specific clone A-12, while amino acid G at position 7 was responsible for recognition by H2-specific clone F-4. Two conserved amino acids, T at position 4 and A at position 6, were responsible for recognition by H1-, and H2-cross-reactive clone B7-B7. These results indicate that a single nine-amino-acid region is recognized by HA-specific CTL clones of three different subtype specificities and that the amino acids responsible for the recognition by the CTL clones are different.

---

^* Corresponding author. Mailing address: Center for Infectious Disease and Vaccine Research, University of Massachusetts Medical Center, 55 Lake Ave. North, Worcester, MA 01655. Phone: (508) 856-4182. Fax: (508) 856-4890. E-mail: francis.ennis{at}banyan.ummed.edu.

Present address: Department of Otolaryngology, Osaka University Medical School, Osaka, Japan.

Present address: Department of Bacteriology, Kurume University School of Medicine, Kurume, Japan.

^§ Present address: Department of Virology 1, National Institute of Infectious Diseases, Tokyo, Japan.

---

Journal of Virology, November 1998, p. 9404-9406, Vol. 72, No. 11
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

This article has been cited by other articles:

• Day, S. L., Ramshaw, I. A., Ramsay, A. J., Ranasinghe, C. (2008). Differential Effects of the Type I Interferons {alpha}4, {beta}, and {epsilon} on Antiviral Activity and Vaccine Efficacy. J. Immunol. 180: 7158-7166 [Abstract] [Full Text]  
• Mitaksov, V., Fremont, D. H. (2006). Structural Definition of the H-2Kd Peptide-binding Motif. J. Biol. Chem. 281: 10618-10625 [Abstract] [Full Text]  
• Fujimoto, C., Nakagawa, Y., Ohara, K., Takahashi, H. (2004). Polyriboinosinic polyribocytidylic acid [poly(I:C)]/TLR3 signaling allows class I processing of exogenous protein and induction of HIV-specific CD8+ cytotoxic T lymphocytes. Int Immunol 16: 55-63 [Abstract] [Full Text]