Abstract:
:Glycoprotein D (gD) of herpes simplex virus type 1 (HSV-1) plays a key role in multiple events during infection including virus entry, cell-to-cell spread, and virus-induced syncytia formation. Here, we provide evidence that an arginine/lysine cluster located at the transmembrane-cytoplasm interface of gD critically contributes to viral spread and cell-cell fusion. Our studies began with the discovery that packaging of gD into virions is almost completely blocked in the absence of tegument protein UL16. We subsequently identified a novel, direct, and regulated interaction between UL16 and gD, but this was not important for syncytia formation. However, a mutational analysis of the membrane-proximal basic residues of gD revealed that they are needed for the gBsyn phenotype, salubrinal-induced fusion of HSV-infected cells, and cell-to-cell spread. Finally, we found that these same gD tail basic residues are not required for cell fusion induced by a gKsyn variant.
journal_name
Virologyjournal_title
Virologyauthors
Carmichael JC,Starkey J,Zhang D,Sarfo A,Chadha P,Wills JW,Han Jdoi
10.1016/j.virol.2018.09.018subject
Has Abstractpub_date
2019-01-15 00:00:00pages
64-76eissn
0042-6822issn
1096-0341pii
S0042-6822(18)30297-6journal_volume
527pub_type
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