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J. Biol. Chem., Vol. 277, Issue 44, 41489-41496, November 1, 2002

This Article Full Text Full Text (PDF) All Versions of this Article: 277/44/41489    most recent M207104200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Cho, W. J. Articles by Park, J. W. Search for Related Content PubMed PubMed Citation Articles by Cho, W. J. Articles by Park, J. W. Social Bookmarking                      What's this?

Molecular Cloning of a Novel Chaperone-like Protein Induced by Rhabdovirus Infection with Sequence Similarity to the Bacterial Extracellular Solute-binding Protein Family 5^*

Wha Ja Cho^§, Won Joon Yoon^§, Chang Hoon Moon, Seung Ju Cha, Hebok Song, Hong Rae Cho^¶, Soo Jin Jang, Dae Kyun Chung, Choon Soo Jeong, and Jeong Woo Park^**

From the  Department of Biological Sciences and Immunomodulation Research Center, University of Ulsan, Ulsan 680-749, Korea, ^¶ Department of Surgery, College of Medicine, Ulsan University Hospital, Ulsan 682-060, Korea, and the  Department of Genetic Engineering and RNA Inc., Kyung Hee University, Yongin-gun, Kyungki-do 449-701, Korea

Previously we demonstrated that a novel stress protein is induced in fish cells by the infection of a fish rhabdovirus (Cho W. J., Cha, S. J., Do, J. W., Choi, J. Y., Lee, J. Y., Jeong, C. S., Cho, K. J., Choi, W. S., Kang, H. S., Kim, H. D., and Park, J. W. (1997) Biochem. Biophys. Res. Commun. 233, 316-319). In this paper, we present the molecular cloning and characterization of a gene encoding this protein named virus-inducible stress protein (VISP). The VISP was purified partially by immunoprecipitation using a monoclonal antibody against the VISP and further purified by the electroelution from a SDS-PAGE gel. The protein was subjected to internal protein sequencing, and the sequence of three peptides was determined. Degenerate oligonucleotides based on the three peptide sequences were used to screen a cDNA library from rhabdovirus-infected CHSE-214 fish cells, and a cDNA of a 2193-bp open reading frame encoding the VISP with 730 amino acid residues (M_r = 79.84) was identified. Whereas the nucleotide sequence of VISP shows no similarity with other genes in the GenBank^TM, the amino acid sequence of the VISP has similarity with the bacterial extracellular solute-binding protein family 5 (SBP_bac_5) that is proposed to have chaperone activity. Thus, we explored whether the VISP also had chaperone-like activity. Purified recombinant VISP expressed in Escherichia coli promoted the functional folding of -glucosidase after urea denaturation and also prevented thermal aggregation of alcohol dehydrogenase. These results suggest that the VISP has amino acid sequence similarity with SBP_bac_5 and that it has chaperone activity that may play a role in virus infection.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AF527060.

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