Dual Function of the pUL7-pUL51 Tegument Protein Complex in Herpes Simplex Virus 1 Infection

摘要: The tegument of herpesviruses is a highly complex structural layer between the nucleocapsid and envelope virions. Tegument proteins play both regulatory functions during replication spread, but interactions many these are poorly understood. Here we focus on two from herpes simplex virus 1 (HSV-1), pUL7 pUL51, which have homologues in all other herpesviruses. We now identified that HSV-1 pUL51 form stable direct protein-protein interaction, their expression levels rely presence each other, they function as infected cells. demonstrate pUL7-pUL51 important for efficient assembly plaque formation. Furthermore, also discovered localizes to focal adhesions at plasma membrane cells absence viral proteins. stabilize maintain cell morphology with viruses lacking and/or round up more rapidly than wild-type HSV-1. Our data suggest that, addition previously reported spread maintaining attachment surroundings through modulating activity adhesion complexes. Importance Herpesviridae large family successful human animal pathogens. Virions composed different proteins, most contained within tegument, particles. roles assembling particles well modifying host promote spread. However, little known about replication. study focuses conserved herpesviruses: pUL51. directly interact functional modulation morphology. Further, identify first time herpesvirus localize cytoplasmic juxtanuclear membranes