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

The Cytoplasmic Tail Domain of Epstein-Barr Virus gH Regulates Membrane Fusion Activity through Altering gH Binding to gp42 and Epithelial Cell Attachment.

mBio - 15 Nov 2016

Chen Jia, Jardetzky Theodore S, Longnecker Richard

Abstract excerpt

Epstein-Barr virus (EBV) is associated with infectious mononucleosis and a variety of cancers as well as lymphoproliferative disorders in immunocompromised patients. EBV mediates viral entry into epithelial and B cells using fusion machinery composed of four glycoproteins: gB, the gH/gL complex, and gp42. gB and gH/gL are required for both epithelial and B cell fusion. The specific role of gH/gL in fusion has...

Read the complete abstract on PubMed

Topics

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

Share to CHO Cells
Share to Cricetulus
Share to Epithelial Cells

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

Share to Herpesvirus 4, Human

Share to Membrane Fusion

Share to Molecular Chaperones

Share to Viral Envelope Proteins

Share to Virus Attachment

Source

Open in PubMed Open full text

Identifiers

PMID: 27935841
DOI: 10.1128/mBio.01871-16
PMCID: PMC5111410

Provenance

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.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The Cytoplasmic Tail Domain of Epstein-Barr Virus gH Regulates Membrane Fusion Activity through Altering gH Binding to gp42 and Epithelial Cell Attachment.PMID 27935841Read ↗

The Epstein-Barr virus (EBV) glycoprotein B cytoplasmic C-terminal tail domain regulates the energy requirement for EBV-induced membrane fusion.Semantic proximity Read ↗

The KGD Motif of Epstein-Barr Virus gH/gL Is Bifunctional, Orchestrating Infection of B Cells and Epithelial CellsSemantic proximity Read ↗

The amino terminus of Epstein-Barr virus glycoprotein gH is important for fusion with epithelial and B cells.Semantic proximity Read ↗

Epstein-Barr Virus Fusion with Epithelial Cells Triggered by gB Is Restricted by a gL Glycosylation Site.Semantic proximity Read ↗

Structural and Mechanistic Insights into the Tropism of Epstein-Barr VirusSemantic proximity Read ↗

Structural basis for Epstein-Barr virus host cell tropism mediated by gp42 and gHgL entry glycoproteins.Semantic proximity Read ↗

Assembly and Architecture of the EBV B Cell Entry Triggering ComplexSemantic proximity Read ↗

Mutational dissection of HCMV gB and gH cytoplasmic tails highlights conserved and divergent features of fusion regulation.Semantic proximity Read ↗

The Cytoplasmic Domain of Varicella-Zoster Virus Glycoprotein H Regulates Syncytia Formation and Skin PathogenesisSemantic proximity Read ↗

R9AP is a common receptor for EBV infection in epithelial cells and B cellsSemantic proximity Read ↗

Structure of a trimeric variant of the Epstein–Barr virus glycoprotein BSemantic proximity Read ↗

Cell-surface expression of a mutated Epstein-Barr virus glycoprotein B allows fusion independent of other viral proteins.Semantic proximity Read ↗

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