The HSV-1 tegument protein pUL46 associates with cellular membranes and viral capsids

Abstract The molecular mechanisms responsible for the addition of tegument proteins into nascent herpesvirus particles are poorly understood. To better understand the tegumentation process of herpes simplex virus type 1 (HSV-1) virions, we initiated studies that showed the tegument protein pUL46 (VP...

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Bibliographic Details
Published in:Virology (New York, N.Y.) N.Y.), 2008-07, Vol.376 (2), p.279-289
Main Authors: Murphy, Michael A, Bucks, Michelle A, O'Regan, Kevin J, Courtney, Richard J
Format: Article
Language:English
Subjects:
60 APPLIED LIFE SCIENCES
AFFINITY
Animals
Antigens, Viral - metabolism
Capsid Proteins - metabolism
Cell Line, Tumor
Cell Membrane - metabolism
Cercopithecus aethiops
Envelopment
HERPES SIMPLEX
Herpes Simplex - virology
Herpes simplex virus 1
Herpesvirus
Herpesvirus 1, Human - physiology
HSV-1
Humans
IN VITRO
Infectious Disease
Membrane association
MEMBRANES
PROTEINS
pUL46
Tegument
UL11
UL37
Vero Cells
Viral Proteins - metabolism
Virus Assembly
VIRUSES
VP16
VP22
VP5
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Summary:Abstract The molecular mechanisms responsible for the addition of tegument proteins into nascent herpesvirus particles are poorly understood. To better understand the tegumentation process of herpes simplex virus type 1 (HSV-1) virions, we initiated studies that showed the tegument protein pUL46 (VP11/12) has a similar cellular localization to the membrane-associated tegument protein VP22. Using membrane flotation analysis we found that pUL46 associates with membranes in both the presence and absence of other HSV-1 proteins. However, when purified virions were stripped of their envelope, the majority of pUL46 was found to associate with the capsid fraction. This strong affinity of pUL46 for capsids was confirmed by an in vitro capsid pull-down assay in which purified pUL46-GST was able to interact specifically with capsids purified from the nuclear fraction of HSV-1 infected cells. These results suggest that pUL46 displays a dynamic interaction between cellular membranes and capsids.
ISSN:0042-6822
1096-0341
DOI:10.1016/j.virol.2008.03.018