Department of Swine Infectious Diseases, Shanghai Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Shanghai 200241, China.
Virology. 2012 Jul 20;429(1):1-11. doi: 10.1016/j.virol.2012.03.010. Epub 2012 Apr 25.
It has been proposed that the N-linked glycan of the minor proteins of porcine reproductive and respiratory syndrome virus (PRRSV) is important for the production of infectious virus. In this study, we showed that N-linked glycosylation of GP2 is not essential for virus viability and none of the individual glycosylation sites in GP3 has a vital effect on the production of infectious virus. Moreover, mutations of single and double glycosylation sites in GP4 are not critically important for infectious virus recovery, triple and quadruple mutations are lethal. The bimolecular fluorescence complementation (BiFC) analysis also showed that GP4, but might be not GP2, is involved in interaction with cellular receptor CD163 and that glycosylation of GP4 might not play a vital role in the interaction with CD163. The study further revealed that none of the N-glycosylation sites in the minor proteins is critical for the susceptibility of mutants to neutralizing antibody.
有人提出，猪繁殖与呼吸综合征病毒（PRRSV）的次要蛋白的 N 连接聚糖对于产生感染性病毒很重要。在这项研究中，我们表明 GP2 的 N 连接糖基化对于病毒的生存力不是必需的，GP3 中的单个糖基化位点都没有对产生感染性病毒产生至关重要的影响。此外，GP4 中单个和双糖基化位点的突变对于恢复感染性病毒并不至关重要，而三重和四重突变是致命的。双分子荧光互补（BiFC）分析还表明，GP4 （而可能不是 GP2）参与与细胞受体 CD163 的相互作用，并且 GP4 的糖基化可能在与 CD163 的相互作用中不起关键作用。该研究还进一步表明，次要蛋白中的任何 N 连接糖基化位点都不是突变体对中和抗体敏感性的关键。
