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Article

Function of glycoprotein E of herpes simplex virus requires coordinated assembly of three tegument proteins on its cytoplasmic tail.

Proceedings of the National Academy of Sciences of the United States of America - 27 Nov 2012

Han Jun, Chadha Pooja, Starkey Jason L, Wills John W

Abstract excerpt

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...

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Identifiers

PMID: 23150560
DOI: 10.1073/pnas.1212900109
PMCID: PMC3511771

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Function of glycoprotein E of herpes simplex virus requires coordinated assembly of three tegument proteins on its cytoplasmic tail.PMID 23150560Read ↗

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Herpes simplex virus glycoproteins gD and gE/gI serve essential but redundant functions during acquisition of the virion envelope in the cytoplasm.Semantic proximity Read ↗

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Comparative Analysis of <i>UL16</i> Mutants Derived from Multiple Strains of HSV-2 and HSV-1 Reveals Species-Specific Requirements for the UL16 ProteinSemantic proximity Read ↗

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