title: A conserved region of the herpes simplex virus type 1 tegument protein VP22 facilitates interaction with the cytoplasmic tail of glycoprotein E (gE).
abstract: Herpes simplex virus type 1 (HSV-1) virions, contain a proteinaceous layer termed the tegument that lies between the nucleocapsid and viral envelope. Current evidence suggests that viral glycoprotein tails play a role in the recruitment of tegument-coated capsids to the site of final envelopment; vesicles derived from the trans-Golgi network. We have identified an interaction between VP22, an abundant tegument protein and the cytoplasmic tail of glycoprotein E (gE). This interaction was identified by coimmunoprecipitation studies and confirmed by a glutathione-S-transferase (GST) pulldown from infected cell lysates. Truncation mutagenesis suggests that residues 165-270 of VP22 facilitate the interaction with the cytoplasmic tail of gE. In fact, this region of VP22 is sufficient to bind to gE in the absence of additional viral proteins. Using a transfection/infection-based virion incorporation assay, residues 165-270 of VP22 fused to GFP competed efficiently with wild-type VP22 for packaging into assembling virus particles.
authors.affiliation: Department of Microbiology and Immunology, The Pennsylvania State University College of Medicine, 500 University Drive, Hershey, PA 17033, USA.
authors.forename: Kevin J
authors.initials: KJ
authors.lastname: O'Regan
authors.forename: Michelle A
authors.initials: MA
authors.lastname: Bucks
authors.forename: Michael A
authors.initials: MA
authors.lastname: Murphy
authors.forename: John W
authors.initials: JW
authors.lastname: Wills
authors.forename: Richard J
authors.initials: RJ
authors.lastname: Courtney
mesh_terms: D000818:Animals; D015153:Blotting, Western; D002457:Cell Extracts / Q000737:chemistry; D002522:Chlorocebus aethiops; D018259:Herpesvirus 1, Human / Q000502:physiology*; D047468:Immunoprecipitation; D011485:Protein Binding; D025941:Protein Interaction Mapping; D017434:Protein Structure, Tertiary; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D017384:Sequence Deletion; D014709:Vero Cells; D014759:Viral Envelope Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D015678:Viral Structural Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D019065:Virus Assembly / Q000502:physiology
chemical_list: D002457:Cell Extracts; D011993:Recombinant Fusion Proteins; D014759:Viral Envelope Proteins; D015678:Viral Structural Proteins; C044768:glycoprotein E, herpes simplex virus type 1; C073413:herpes simplex virus type 1 protein VP22