Glycoprotein D of HSV-1 is dependent on tegument protein UL16 for packaging and contains a motif that is differentially required for syncytia formation.

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

Virology

journal_title

Virology

authors

Carmichael JC,Starkey J,Zhang D,Sarfo A,Chadha P,Wills JW,Han J

doi

10.1016/j.virol.2018.09.018

subject

Has Abstract

pub_date

2019-01-15 00:00:00

pages

64-76

eissn

0042-6822

issn

1096-0341

pii

S0042-6822(18)30297-6

journal_volume

527

pub_type

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