Herpes simplex virus type 1 tegument proteins VP1/2 and UL37 are associated with intranuclear capsids.
The assembly of the tegument of herpes simplex virus type 1 (HSV-1) is a complex process that involves a number of events at various sites within virus-infected cells. Our studies focused on determining whether tegument proteins, VP1/2 and UL37, are added to capsids located within the nucleus. Capsids were isolated from the nuclear fraction of HSV-1-infected cells and purified by rate-zonal centrifugation to separate B capsids (containing the scaffold proteins and no viral DNA) and C capsids (containing DNA and no scaffold proteins). Western blot analyses of these capsids indicated that VP1/2 associated primarily with C capsids and UL37 associated with B and C capsids. The results demonstrate that at least two of the tegument proteins of HSV-1 are associated with capsids isolated from the nuclear fraction, and these capsid-tegument protein interactions may represent initial events of the tegumentation process.
Bucks
Michelle A
MA
Department of Microbiology and Immunology, The Pennsylvania State University College of Medicine, Hershey, PA 17033, USA.
O'Regan
Kevin J
KJ
Murphy
Michael A
MA
Wills
John W
JW
Courtney
Richard J
RJ
D000818:Animals; D002213:Capsid / Q000737:chemistry / Q000502:physiology; D002467:Cell Nucleus / Q000378:metabolism; D002522:Chlorocebus aethiops; D018259:Herpesvirus 1, Human / Q000737:chemistry / Q000502:physiology*; D014709:Vero Cells; D014759:Viral Envelope Proteins / Q000378:metabolism*; D015678:Viral Structural Proteins / Q000276:immunology*; D019065:Virus Assembly
C084763:UL37 protein, Human herpesvirus 1; D014759:Viral Envelope Proteins; D015678:Viral Structural Proteins