Bovine herpesvirus type-1 glycoprotein K (gK) interacts with UL20 and is required for infectious virus production

• Published in: Virology (New York, N.Y.) Vol. 499; pp. 156 - 164
• Main Authors: Haque, Muzammel, Stanfield, Brent, Kousoulas, Konstantin G
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.12.2016
• Subjects: 60 APPLIED LIFE SCIENCES; Animals; BHV-1; CATTLE; Cell Line; CODONS; Cytoplasmic envelopment; Dogs; Egress protein-protein interaction; GENES; Genetic Vectors; Genome, Viral; GLYCOPROTEINS; HERPES SIMPLEX; Herpesvirus 1, Bovine - physiology; Humans; IN VITRO; In vitro translation; Infectious Disease; MEMBRANES; MICROSCOPY; Mutagenesis; MUTANTS; Protein Binding; Protein Conformation, alpha-Helical; UL20; Viral Proteins - chemistry; Viral Proteins - genetics; Viral Proteins - metabolism; Virus Replication; VIRUSES; BHV-1; UL20; In vitro translation; gK; Cytoplasmic envelopment; Egress protein-protein interaction
• ISSN: 0042-6822; 1096-0341
• DOI: 10.1016/j.virol.2016.09.003

Abstract We have previously shown that the HSV-1 gK and UL20 proteins interact and function in virion envelopment, membrane fusion, and neuronal entry. Alignment of the predicted secondary structures of gKs encoded by BoHV-1, HSV-1, HSV-2, EHV-1 and VZV indicated a high degree of domain conservation. Two BoHV-1 gK-null mutant viruses were created by either gK gene deletion or stop codon insertion. In addition, a V5 epitope-tag was inserted at the carboxyl terminus of gK gene to detect gK. The engineered gK-null mutant viruses failed to replicate and produce viral plaques. Co-immunoprecipitation of gK and UL20 expressed via different methods revealed that gK and UL20 physically interacted in the presence or absence of other viral proteins. Confocal microscopy showed that gK and UL20 colocalized in infected cells. These results indicate that BoHV-1 gK and UL20 may function in a similar manner to other alphaherpesvirus orthologues specified by HSV-1, PRV and EHV-1.