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Journal of Virology, July 2007, p. 6798-6806, Vol. 81, No. 13
0022-538X/07/$08.00+0     doi:10.1128/JVI.02840-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Highly Conserved Configuration of Catalytic Amino Acid Residues among Calicivirus-Encoded Proteases{triangledown}

Tomoichiro Oka,1* Mami Yamamoto,1 Masaru Yokoyama,2 Satoko Ogawa,1 Grant S. Hansman,1 Kazuhiko Katayama,1 Kana Miyashita,1 Hirotaka Takagi,3 Yukinobu Tohya,4 Hironori Sato,2 and Naokazu Takeda1

Department of Virology II, National Institute of Infectious Diseases, Gakuen 4-7-1, Musashi-murayama, Tokyo 208-0011, Japan,1 Center for Pathogen Genomics, National Institute of Infectious Diseases, Gakuen 4-7-1, Musashi-murayama, Tokyo 208-0011, Japan,2 Division of Biosafety Control and Research, National Institute of Infectious Diseases, Toyama 1-23-1, Shinjuku-ku, Tokyo 162-8640, Japan,3 Department of Veterinary Microbiology, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan4

Received 22 December 2006/ Accepted 11 April 2007

A common feature of caliciviruses is the proteolytic processing of the viral polyprotein catalyzed by the viral 3C-like protease encoded in open reading frame 1 (ORF1). Here we report the identification and structural characterization of the protease domains and amino acid residues in sapovirus (SaV) and feline calicivirus (FCV). The in vitro expression and processing of a panel of truncated ORF1 polyproteins and corresponding mutant forms showed that the functional protease domain is 146 amino acids (aa) in SaV and 154 aa in FCV. Site-directed mutagenesis of the protease domains identified four amino acid residues essential to protease activities: H31, E52, C116, and H131 in SaV and H39, E60, C122, and H137 in FCV. A computer-assisted structural analysis showed that despite high levels of diversity in the primary structures of the protease domains in the family Caliciviridae, the configurations of the H, E, C, and H residues are highly conserved, with these residues positioned closely along the inner surface of the potential binding cleft for the substrate. These results strongly suggest that the H, E, C, and H residues are involved in the formation of a conserved catalytic surface of the SaV and FCV 3C-like proteases.

* Corresponding author. Mailing address: Department of Virology II, National Institute of Infectious Diseases, Gakuen 4-7-1, Musashi-murayama, Tokyo 208-0011, Japan. Phone: 81-42-561-0771. Fax: 81-42-561-4729. E-mail: oka-t{at}nih.go.jp

{triangledown} Published ahead of print on 25 April 2007.

Journal of Virology, July 2007, p. 6798-6806, Vol. 81, No. 13
0022-538X/07/$08.00+0     doi:10.1128/JVI.02840-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



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