Publication: Glycosylation of gp116 and gp64 envelope proteins of yellow head virus of Penaeus monodon shrimp
Issued Date
2010-10-01
Resource Type
ISSN
14652099
00221317
00221317
Other identifier(s)
2-s2.0-77956823187
Rights
Mahidol University
Rights Holder(s)
SCOPUS
Bibliographic Citation
Journal of General Virology. Vol.91, No.10 (2010), 2463-2473
Suggested Citation
Chumporn Soowannayan, Jeff A. Cowley, Roger D. Pearson, Tristan P. Wallis, Jeffrey J. Gorman, Wojtek P. Michalski, Peter J. Walker Glycosylation of gp116 and gp64 envelope proteins of yellow head virus of Penaeus monodon shrimp. Journal of General Virology. Vol.91, No.10 (2010), 2463-2473. doi:10.1099/vir.0.022111-0 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/29190
Research Projects
Organizational Units
Authors
Journal Issue
Thesis
Title
Glycosylation of gp116 and gp64 envelope proteins of yellow head virus of Penaeus monodon shrimp
Abstract
Yellow head virus (YHV) is a highly virulent pathogen of Penaeus monodon shrimp that is classified in the genus Okavirus, family Roniviridae, in the order Nidovirales. Separation of virion proteins treated with peptide-N-glycosidase-F (PNGase-F) in SDS-polyacrylamide gels and the use of glycoprotein-specific staining methods indicated that the gp116 and gp64 envelope glycoproteins possess N-linked rather than O-linked glycans. Competitive binding inhibition of lectins with various oligosaccharide specificities indicated that glycans linked to gp64 are mannose-rich, whilst glycans linked to gp116 possess terminal N-acetylgalactosamine and N-acetylglucosamine in addition to terminal mannose-type sugars. Mass spectrometry analyses of peptides generated from YHV proteins before and after deglycosylation with PNGase-F, using combinations of the endoproteinases trypsin, Asp-N and Lys-C, confirmed occupancy of six of the seven potential N-linked glycosylation sites in gp116 and three of the four potential sites in gp64. © 2010 CSIRO.