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Journal of Virology, February 2002, p. 1691-1696, Vol. 76, No. 4
0022-538X/01/$04.00+0     DOI: 10.1128/JVI.76.4.1691-1696.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Identification of Immunodominant Neutralizing Epitopes on the Hemagglutinin Protein of Rinderpest Virus

Makoto Sugiyama,1* Naoto Ito,1 Nobuyuki Minamoto,1 and Seiichi Tanaka2

Department of Veterinary Public Health, Faculty of Agriculture, Gifu University, Gifu 501-1193 ,1 Animal Laboratory Center, Oita Medical University, Oita 879-5593, Japan2

Received 20 September 2001/ Accepted 15 November 2001

The immunodominant epitopes on the hemagglutinin protein of rinderpest virus (RPV-H) were determined by analyzing selected monoclonal antibody (MAb)-resistant mutants and estimating the level of antibody against each epitope in five RPV-infected rabbits with the competitive enzyme-linked immunosorbent assay (c-ELISA). Six neutralizing epitopes were identified, at residues 474 (epitope A), 243 (B), 548 to 551 (D), 587 to 592 (E), 310 to 313 (G), and 383 to 387 (H), from the data on the amino acid substitutions of hemagglutinin protein of MAb-resistant mutants and the reactivities of MAbs against RPV-H to the other morbilliviruses. The epitopes identified in this study are all positioned on the loop of the propeller-like structure in a hypothetical three-dimensional model of RPV-H (J. P. M. Langedijk et al., J. Virol. 71:6155-6167, 1997). Polyclonal sera obtained from five rabbits infected experimentally with RPV were examined by c-ELISA using a biotinylated MAb against each epitope as a competitor. Although these rabbit sera hardly blocked binding of each MAb to epitopes A and B, they moderately blocked binding of each MAb to epitopes G and D and strongly blocked binding of each MAb to epitopes E and H. These results suggest that epitopes at residues 383 to 387 and 587 to 592 may be immunodominant in humoral immunity to RPV infection.

* Corresponding author. Mailing address: Department of Veterinary Public Health, Faculty of Agriculture, Gifu University, 1-1 Yanagido, Gifu 501-1193, Japan. Phone and fax: 81-58-293-2949. E-mail: sugiyama{at}cc.gifu-u.ac.jp.

Journal of Virology, February 2002, p. 1691-1696, Vol. 76, No. 4
0022-538X/01/$04.00+0     DOI: 10.1128/JVI.76.4.1691-1696.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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