title: The interaction of the HSV-1 tegument proteins pUL36 and pUL37 is essential for secondary envelopment during viral egress.
abstract: The herpes simplex virus type 1 (HSV-1) tegument proteins pUL36 (VP1/2) and pUL37 are essential for viral egress. We previously defined a minimal domain in HSV-1 pUL36, residues 548-572, as important for binding pUL37. Here, we investigated the role of this region in binding to pUL37 and facilitating viral replication. We deleted residues 548-572 in frame in a virus containing a mRFP tag at the N-terminus of the capsid protein VP26 and an eGFP tag at the C-terminus of pUL37 (HSV-1pUL36∆548-572). This mutant virus was unable to generate plaques in Vero cells, indicating that deletion of this region of pUL36 blocks viral replication. Imaging of HSV-1pUL36∆548-572-infected Vero cells, in comparison to parental and resucant, revealed a block in secondary envelopment of cytoplasmic capsids. In addition, immunoblot analysis suggested that failure to bind pUL37 affected the stability of pUL36. This study provides further insight into the role of this essential interaction.
authors.affiliation: Centre for Virus Research, Westmead Millennium Institute, The University of Sydney and Westmead Hospital, Westmead, NSW 2145, Australia.
authors.forename: Barbara J
authors.initials: BJ
authors.lastname: Kelly
authors.affiliation: Institute of Cell Biology, Hannover Medical School, Carl-Neuberg-Str. 1, D-30625 Hannover, Germany.
authors.forename: Rudolf
authors.initials: R
authors.lastname: Bauerfeind
authors.affiliation: Institute of Virology, Hannover Medical School, Carl-Neuberg-Str. 1, D-30625 Hannover, Germany.
authors.forename: Anne
authors.initials: A
authors.lastname: Binz
authors.affiliation: Institute of Virology, Hannover Medical School, Carl-Neuberg-Str. 1, D-30625 Hannover, Germany.
authors.forename: Beate
authors.initials: B
authors.lastname: Sodeik
authors.affiliation: Institute of Virology, University of Zurich, 8057 Zurich, Switzerland.
authors.forename: Andrea S
authors.initials: AS
authors.lastname: Laimbacher
authors.affiliation: Institute of Virology, University of Zurich, 8057 Zurich, Switzerland.
authors.forename: Cornel
authors.initials: C
authors.lastname: Fraefel
authors.affiliation: Centre for Virus Research, Westmead Millennium Institute, The University of Sydney and Westmead Hospital, Westmead, NSW 2145, Australia. Electronic address: russell.diefenbach@sydney.edu.au.
authors.forename: Russell J
authors.initials: RJ
authors.lastname: Diefenbach
mesh_terms: D000818:Animals; D002522:Chlorocebus aethiops; D004252:DNA Mutational Analysis; D018259:Herpesvirus 1, Human / Q000502:physiology*; D014709:Vero Cells; D010948:Viral Plaque Assay; D014764:Viral Proteins / Q000378:metabolism*; D015678:Viral Structural Proteins / Q000378:metabolism*; D057074:Virus Release
chemical_list: C078035:UL36 protein, Human herpesvirus 1; C084763:UL37 protein, Human herpesvirus 1; D014764:Viral Proteins; D015678:Viral Structural Proteins
keywords: Herpes simplex virus; Tegument; Virus assembly; pUL36; pUL37