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 KGD Motif of Epstein-Barr Virus gH/gL Is Bifunctional, Orchestrating Infection of B Cells and Epithelial Cells

4 Jan 2012

Abstract excerpt

ABSTRACT Epstein-Barr virus (EBV), a member of the herpesvirus family, is the causative agent of common human infections and specific malignancies. EBV entry into target cells, including B cells and epithelial cells, requires the interaction of multiple virus-encoded glycoproteins. Glycoproteins H and L (gH/gL) cooperate with glycoprotein B (gB) to mediate fusion of the viral envelope with target cell membranes....

Read the complete abstract on PubMed

Topics

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

Share to Lymphoma Diagnosis and Treatment
Share to Parvovirus B19 Infection Studies
Share to Viral-associated cancers and disorders

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

Source

Identifiers

PMID: 22215569
DOI: 10.1128/mbio.00290-11

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 24 Oct 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 KGD Motif of Epstein-Barr Virus gH/gL Is Bifunctional, Orchestrating Infection of B Cells and Epithelial CellsPMID 22215569Read ↗

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

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

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

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

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

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

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

R9AP is a functional receptor for Epstein-Barr virus infection in both epithelial cells and B cellsSemantic proximity Read ↗

Mutagenesis of human cytomegalovirus glycoprotein L disproportionately disrupts gH/gL/gO over gH/gL/pUL128-131Semantic proximity Read ↗

Mutagenesis of Human Cytomegalovirus Glycoprotein L Disproportionately Disrupts gH/gL/gO over gH/gL/pUL128-131.Semantic proximity Read ↗

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