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• W2048198160 abstract "CD46 and CD134 mediate attachment of Human Herpesvirus 6A (HHV-6A) and HHV-6B to host cell, respectively. But many cell types interfere with viral infection through rapid degradation of viral DNA. Hence, not all cells expressing these receptors are permissive to HHV-6 DNA replication and production of infective virions suggesting the involvement of additional factors that influence HHV-6 propagation. Here, we used a proteomics approach to identify other host cell proteins necessary for HHV-6 binding and entry. We found host cell chaperone protein GP96 to interact with HHV-6A and HHV-6B and to interfere with virus propagation within the host cell. In human peripheral blood mononuclear cells (PBMCs), GP96 is transported to the cell surface upon infection with HHV-6 and interacts with HHV-6A and -6B through its C-terminal end. Suppression of GP96 expression decreased initial viral binding but increased viral DNA replication. Transient expression of human GP96 allowed HHV-6 entry into CHO-K1 cells even in the absence of CD46. Thus, our results suggest an important role for GP96 during HHV-6 infection, which possibly supports the cellular degradation of the virus." @default.
• W2048198160 created "2016-06-24" @default.
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• W2048198160 date "2014-12-03" @default.
• W2048198160 modified "2023-09-25" @default.
• W2048198160 title "GP96 Interacts with HHV-6 during Viral Entry and Directs It for Cellular Degradation" @default.
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• W2048198160 doi "https://doi.org/10.1371/journal.pone.0113962" @default.
• W2048198160 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4254946" @default.
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• W2048198160 hasPublicationYear "2014" @default.
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