Abstract:
:Glycoprotein E (gE) of HSV plays a key role in cell-to-cell spread and virus-induced cell fusion. Here, we report that this function of gE requires the cooperation of tegument proteins UL11, UL16, and UL21. We found that the four proteins come together with very high efficiency to form a complex in transfected cells and in a manner that is regulated and coordinated. In particular, the inefficient interaction of UL16 with each membrane protein (UL11 and gE) observed in pairwise transfections became efficient when other binding partners were present. The significance of these interactions was revealed in studies of viral mutants, which showed that each of these tegument proteins is critical for processing, transport, and biological activity of gE. These findings provide insights into the mechanisms of how gE executes its function and also have implications in understanding HSV assembly and budding.
journal_name
Proc Natl Acad Sci U S Aauthors
Han J,Chadha P,Starkey JL,Wills JWdoi
10.1073/pnas.1212900109subject
Has Abstractpub_date
2012-11-27 00:00:00pages
19798-803issue
48eissn
0027-8424issn
1091-6490pii
1212900109journal_volume
109pub_type
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