Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

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

Virology - 5 Jan 2004

Jogger Cheryl R, Montgomery Rebecca I, Spear Patricia G

Abstract excerpt

Several cell surface molecules, including HVEM and nectin-1, can serve as entry receptors for herpes simplex virus (HSV) and as receptors for virus-induced or viral glycoprotein-induced cell fusion. The viral ligand for these receptors is the HSV envelope glycoprotein gD. A set of linker-insertion and deletion mutants of HSV type 1 (HSV-1) gD was analyzed for effects of the mutations on binding of gD to HVEM and...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cell Adhesion Molecules
Share to Cell Fusion

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Herpesvirus 1, Human

Share to Membrane Fusion

Share to Nectins

Share to Receptors, Tumor Necrosis Factor

Share to Receptors, Virus

Share to Viral Envelope Proteins

Source

Identifiers

PMID: 14972557
DOI: 10.1016/j.virol.2003.10.004

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Effects of linker-insertion mutations in herpes simplex virus 1 gD on glycoprotein-induced fusion with cells expressing HVEM or nectin-1.PMID 14972557Read ↗

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

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 ↗

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

Contributions of gD receptors and glycosaminoglycan sulfation to cell fusion mediated by herpes simplex virus 1.Semantic proximity Read ↗

Cellular Localization of Nectin-1 and Glycoprotein D during Herpes Simplex Virus InfectionSemantic proximity Read ↗

Use of herpes simplex virus and pseudorabies virus chimeric glycoprotein D molecules to identify regions critical for membrane fusion.Semantic proximity Read ↗

A double mutation in glycoprotein gB compensates for ineffective gD-dependent initiation of herpes simplex virus type 1 infection.Semantic proximity Read ↗

Nectin2alpha (PRR2alpha or HveB) and nectin2delta are low-efficiency mediators for entry of herpes simplex virus mutants carrying the Leu25Pro substitution in glycoprotein D.Semantic proximity Read ↗

The domains of glycoprotein D required to block apoptosis induced by herpes simplex virus 1 are largely distinct from those involved in cell-cell fusion and binding to nectin1.Semantic proximity Read ↗

Mutations in herpes simplex virus gD protein affect receptor binding by different molecular mechanisms.Semantic proximity Read ↗

Generation of Herpesvirus Entry Mediator (HVEM)-Restricted Herpes Simplex Virus Type 1 Mutant Viruses: Resistance of HVEM-Expressing Cells and Identification of Mutations That Rescue Nectin-1 RecognitionSemantic proximity Read ↗

HveA (herpesvirus entry mediator A), a coreceptor for herpes simplex virus entry, also participates in virus-induced cell fusion.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.