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http://purl.uniprot.org/citations/17715218http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17715218http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17715218http://www.w3.org/2000/01/rdf-schema#comment"How alphaherpesvirus capsids acquire tegument proteins remains a key question in viral assembly. Using pseudorabies virus (PRV), we have previously shown that the 62 carboxy-terminal amino acids of the VP1/2 large tegument protein are essential for viral propagation and when transiently expressed as a fusion to green fluorescent protein relocalize to nuclear capsid assemblons following viral infection. Here, we show that localization of the VP1/2 capsid-binding domain (VP1/2cbd) into assemblons is conserved in herpes simplex virus type 1 (HSV-1) and that this recruitment is specifically on capsids. Using a mutant virus screen, we find that the protein product of the UL25 gene is essential for VP1/2cbd association with capsids. An interaction between UL25 and VP1/2 was corroborated by coimmunoprecipitation from cells transiently expressing either HSV-1 or PRV proteins. Taken together, these findings suggest that the essential function of the VP1/2 carboxy terminus is to anchor the VP1/2 tegument protein to capsids. Furthermore, UL25 encodes a multifunctional capsid protein involved in not only encapsidation, as previously described, but also tegumentation."xsd:string
http://purl.uniprot.org/citations/17715218http://purl.org/dc/terms/identifier"doi:10.1128/jvi.01113-07"xsd:string
http://purl.uniprot.org/citations/17715218http://purl.org/dc/terms/identifier"doi:10.1128/jvi.01113-07"xsd:string
http://purl.uniprot.org/citations/17715218http://purl.uniprot.org/core/author"Lee J.I."xsd:string
http://purl.uniprot.org/citations/17715218http://purl.uniprot.org/core/author"Lee J.I."xsd:string
http://purl.uniprot.org/citations/17715218http://purl.uniprot.org/core/author"Coller K.E."xsd:string
http://purl.uniprot.org/citations/17715218http://purl.uniprot.org/core/author"Coller K.E."xsd:string
http://purl.uniprot.org/citations/17715218http://purl.uniprot.org/core/author"Smith G.A."xsd:string
http://purl.uniprot.org/citations/17715218http://purl.uniprot.org/core/author"Smith G.A."xsd:string
http://purl.uniprot.org/citations/17715218http://purl.uniprot.org/core/author"Ueda A."xsd:string
http://purl.uniprot.org/citations/17715218http://purl.uniprot.org/core/author"Ueda A."xsd:string
http://purl.uniprot.org/citations/17715218http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17715218http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17715218http://purl.uniprot.org/core/name"J. Virol."xsd:string
http://purl.uniprot.org/citations/17715218http://purl.uniprot.org/core/name"J. Virol."xsd:string
http://purl.uniprot.org/citations/17715218http://purl.uniprot.org/core/pages"11790-11797"xsd:string
http://purl.uniprot.org/citations/17715218http://purl.uniprot.org/core/pages"11790-11797"xsd:string
http://purl.uniprot.org/citations/17715218http://purl.uniprot.org/core/title"The capsid and tegument of the alphaherpesviruses are linked by an interaction between the UL25 and VP1/2 proteins."xsd:string
http://purl.uniprot.org/citations/17715218http://purl.uniprot.org/core/title"The capsid and tegument of the alphaherpesviruses are linked by an interaction between the UL25 and VP1/2 proteins."xsd:string
http://purl.uniprot.org/citations/17715218http://purl.uniprot.org/core/volume"81"xsd:string
http://purl.uniprot.org/citations/17715218http://purl.uniprot.org/core/volume"81"xsd:string
http://purl.uniprot.org/citations/17715218http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17715218
http://purl.uniprot.org/citations/17715218http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17715218