Glycosylation of ALV-J Envelope Protein at Sites 17 and 193 Is Pivotal in the Virus Infection
Moru Xu, Kun Qian, Hongxia Shao, Yongxiu Yao, Venugopal Nair, Jianqiang Ye, Aijian Qin
Abstract
of the strain TBC-J6 can largely influence the titer of this virus. Deglycosylation at N193 weakened Env-receptor binding while mutation at N17 influenced Env protein processing. This study systemically analyzed the function of NGSs in ALV-J in different aspects, which may help us to understand the life cycle of ALV-J and provide antiviral targets for the control of ALV-J.
Topics & Concepts
BiologyGlycosylationVirologyEnvelope (radar)VirusViral envelopeGlycoproteinPosttranslational modificationEnzymeBiochemistryTelecommunicationsComputer scienceRadarVirus-based gene therapy researchCytomegalovirus and herpesvirus researchHIV Research and Treatment