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Rat and human cytomegalovirus ORF116 encodes a virion envelope glycoprotein required for infectivity
Virology. 2021 Feb 9;557:23-33. doi: 10.1016/j.virol.2020.12.014. Online ahead of print.ABSTRACTHerpesviruses encode multiple glycoproteins required for different stages of viral attachment, fusion, and envelopment. The protein encoded by the human cytomegalovirus (HCMV) open reading frame UL116 forms a stable complex with glycoprotein H that is incorporated into virions. However, the function of this complex remains unknown. Herein, we characterize R116, the rat CMV (RCMV) putative homolog of UL116. Two R116 transcripts were identified in fibroblasts with three proteins expressed with molecular weights of 42, 58, and 82 k...
Source: Virology - February 18, 2021 Category: Virology Authors: Philippe Gatault Iris K A Jones Christine Meyer Craig Kreklywich Timothy Alexander Patricia P Smith Michael Denton Josh Powell Susan L Orloff Daniel N Streblow Source Type: research

Epstein-Barr virus glycoprotein gM can interact with the cellular protein p32 and knockdown of p32 impairs virus.
We report here that the long predicted cytoplasmic tail of gM is not required for complex formation and that it interacts with the cellular protein p32, which has been reported to be involved in nuclear egress of human cytomegalovirus and herpes simplex virus. Although redistribution of p32 and colocalization with gM was not observed in virus infected cells, knockdown of p32 expression by siRNA or lentivirus-delivered shRNA recapitulated the phenotype of a virus lacking expression of gNgM. A proportion of virus released from cells sedimented with characteristics of virus lacking an intact envelope and there was an increase...
Source: Virology - January 13, 2016 Category: Virology Authors: Changotra H, Turk SM, Artigues A, Thakur N, Gore M, Muggeridge MI, Hutt-Fletcher LM Tags: Virology Source Type: research