Role of a reducing environment in disassembly of the herpesvirus tegument.
Initiation of infection by herpes family viruses involves a step in which most of the virus tegument becomes detached from the capsid. Detachment takes place in the host cell cytosol near the virus entry site and it is followed by dispersal of tegument proteins and disappearance of the tegument as a distinct entity. Here we describe the results of experiments designed to test the idea that the reducing environment of the cytosol may contribute to tegument detachment and disassembly. Non-ionic detergent was used to remove the membrane of purified herpes simplex virus under control and reducing conditions. The effects on the tegument were then examined by SDS-PAGE and electron microscopy. Protein analysis demonstrated that most major tegument proteins were removed under both oxidizing and reducing conditions except for UL49 which required a reducing environment. It is proposed therefore that the reducing conditions in the cytosol are involved in removal of UL49 protein. Electron microscopic analysis revealed that capsids produced under oxidizing conditions contained a coating of protein that was absent in reduced virions and which correlated uniquely with the presence of UL49. This capsid-associated layer is suggested to be the location of UL49 in the extracted virion.
Department of Microbiology Immunology and Cancer Biology, University of Virginia Health System, Box 800734, 1300 Jefferson Park Ave., Charlottesville, VA 22908, USA.
William W
WW
Newcomb
Lisa M
LM
Jones
Alexander
A
Dee
Farid
F
Chaudhry
Jay C
JC
Brown
D002213:Capsid / Q000378:metabolism*; D003600:Cytosol / Q000737:chemistry*; D004591:Electrophoresis, Polyacrylamide Gel; D006564:Herpesviridae / Q000502:physiology* / Q000648:ultrastructure; D008854:Microscopy, Electron; D010084:Oxidation-Reduction; D015678:Viral Structural Proteins / Q000378:metabolism*; D053586:Virus Internalization
D015678:Viral Structural Proteins