Chumporn SoowannayanJeff A. CowleyRoger D. PearsonTristan P. WallisJeffrey J. GormanWojtek P. MichalskiPeter J. WalkerCSIRO Livestock IndustriesMahidol UniversityThailand National Center for Genetic Engineering and BiotechnologyUniversity of QueenslandQIMR Berghofer Medical Research Institute2018-09-242018-09-242010-10-01Journal of General Virology. Vol.91, No.10 (2010), 2463-247314652099002213172-s2.0-77956823187https://repository.li.mahidol.ac.th/handle/20.500.14594/29190Yellow 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.Mahidol UniversityImmunology and MicrobiologyGlycosylation of gp116 and gp64 envelope proteins of yellow head virus of Penaeus monodon shrimpArticleSCOPUS10.1099/vir.0.022111-0