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Article

N-terminal mutants of herpes simplex virus type 2 gH are transported without gL but require gL for function.

Journal of virology - 1 May 2007

Cairns Tina M, Friedman Lisa S, Lou Huan, Whitbeck J Charles, Shaner Marie S, Cohen Gary H, Eisenberg Roselyn J

Abstract excerpt

Glycoprotein H (gH) is conserved among all herpesviruses and is essential for virus entry and cell fusion along with gL, gB, and, in most alphaherpesviruses, gD. Within the gH/gL heterodimer, it is thought that gH accounts for the fusion function and gL acts as a chaperone for the folding and transport of gH. Here, we found that the N terminus of gH2 contains important elements involved in both its folding and...

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Identifiers

PMID: 17344290
DOI: 10.1128/JVI.00097-07
PMCID: PMC1900195

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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