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Article

Mutations in herpes simplex virus glycoprotein D that prevent cell entry via nectins and alter cell tropism.

Proceedings of the National Academy of Sciences of the United States of America - 24 Aug 2004

Manoj Sharmila, Jogger Cheryl R, Myscofski Dawn, Yoon Miri, Spear Patricia G

Abstract excerpt

Glycoprotein D (gD) determines which cells can be infected by herpes simplex virus (HSV) by binding to one of the several cell surface receptors that can mediate HSV entry or cell fusion. These receptors include the herpesvirus entry mediator (HVEM), nectin-1, nectin-2, and sites in heparan sulfate generated by specific 3-O-sulfotransferases. The objective of the present study was to identify residues in gD that...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Identifiers

PMID: 15273289
DOI: 10.1073/pnas.0404211101
PMCID: PMC515077

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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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Mutations in herpes simplex virus glycoprotein D that prevent cell entry via nectins and alter cell tropism.PMID 15273289Read ↗

Mutations in the N termini of herpes simplex virus type 1 and 2 gDs alter functional interactions with the entry/fusion receptors HVEM, nectin-2, and 3-O-sulfated heparan sulfate but not with nectin-1.Semantic proximity Read ↗

Structure-based mutagenesis of herpes simplex virus glycoprotein D defines three critical regions at the gD-HveA/HVEM binding interface.Semantic proximity Read ↗

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Mutations in the N-terminal domains of nectin-1 and nectin-2 reveal differences in requirements for entry of various alphaherpesviruses and for nectin-nectin interactions.Semantic proximity Read ↗

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Effects of linker-insertion mutations in herpes simplex virus 1 gD on glycoprotein-induced fusion with cells expressing HVEM or nectin-1.Semantic proximity Read ↗

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