Publication: Identification and analysis of gp116 and gp64 structural glycoproteins of yellow head nidovirus of Penaeus monodon shrimp
Issued Date
2003-04-01
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ISSN
00221317
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2-s2.0-0037385667
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Mahidol University
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SCOPUS
Bibliographic Citation
Journal of General Virology. Vol.84, No.4 (2003), 863-873
Suggested Citation
Sarawut Jitrapakdee, Sasimanas Unajak, Nusra Sittidilokratna, Richard A.J. Hodgson, Jeff A. Cowley, Peter J. Walker, Sakol Panyim, Vichai Boonsaeng Identification and analysis of gp116 and gp64 structural glycoproteins of yellow head nidovirus of Penaeus monodon shrimp. Journal of General Virology. Vol.84, No.4 (2003), 863-873. doi:10.1099/vir.0.18811-0 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/20909
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Title
Identification and analysis of gp116 and gp64 structural glycoproteins of yellow head nidovirus of Penaeus monodon shrimp
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Abstract
Yellow head virus (YHV) is a major agent of disease in farmed penaeid shrimp. YHV virions purified from infected shrimp contain three major structural proteins of molecular mass 116 kDa (gp116), 64 kDa (gp64) and 20 kDa (p20). Two different staining methods indicated that the gp116 and gp64 proteins are glycosylated. Here we report the complete nucleotide sequence of ORF3, which encodes a polypeptide of 1666 amino acids with a calculated molecular mass of 185 713 Da (pl = 6.68). Hydropathy analysis of the deduced ORF3 protein sequence identified six potential transmembrane helices and three ectodomains containing multiple sites for potential N-linked and O-linked glycosylation. N-terminal sequence analysis of mature gp116 and gp64 proteins indicated that each was derived from ORF3 by proteolytic cleavage of the polyprotein between residues Ala228 and Thr229, and Ala1127 and Leu1128, located at the C-terminal side of transmembrane helices 3 and 5, respectively. Comparison with the deduced ORF3 protein sequence of Australian gill-associated virus (GAV) indicated 83 % amino acid identity in gp64 and 71 % identity in gp116, which featured two significant sequence deletions near the N terminus. Database searches revealed no significant homology with other proteins. Recombinant gp64 expressed in E. coli with and without the C-terminal transmembrane region was shown to react with antibody raised against native gp64 purified from virions.