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

• 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
• ISSN: 0042-6822; 1096-0341
• DOI: 10.1016/j.virol.2008.03.018

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.