ORF9p Phosphorylation by ORF47p Is Crucial for the Formation and Egress of Varicella-Zoster Virus Viral Particles

摘要: ABSTRACT The role of the tegument during herpesvirus lytic cycle is still not clearly established, particularly at late phase infection, when newly produced viral particles need to be fully assembled before being released from infected cell. varicella-zoster virus (VZV) protein coded by open reading frame (ORF) 9 (ORF9p) an essential protein, and, even though its mRNA most expressed productive little known about functions. Using a GalK positive/negative selection technique, we modified bacterial artificial chromosome (BAC) containing complete VZV genome create viruses expressing mutant versions ORF9p. We showed that ORF9p hyperphosphorylated especially through interaction with Ser/Thr kinase ORF47p; identified consensus site within recognized ORF47p and demonstrated importance for phosphorylation. Strikingly, ultrastructural analysis revealed mutation this (glutamate 85 arginine) strongly affects assembly release, reproducing ORF47 kinase-dead phenotype. It also slightly diminishes infectivity toward immature dendritic cells. Taken together, our results identify as new substrate suggest determinant phosphorylation infectivity, process particle formation egress.