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

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

Nature communications - 8 Dec 2016

Sathiyamoorthy Karthik, Hu Yao Xiong, Möhl Britta S, Chen Jia, Longnecker Richard, Jardetzky Theodore S

Abstract excerpt

Herpesvirus entry into host cells is mediated by multiple virally encoded receptor binding and membrane fusion glycoproteins. Despite their importance in host cell tropism and associated disease pathology, the underlying and essential interactions between these viral glycoproteins remain poorly understood. For Epstein-Barr virus (EBV), gHgL/gp42 complexes bind HLA class II to activate membrane fusion with B...

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 About Contact Helena Bioinformatics

Share to Herpesvirus 4, Human

Share to Mutation

Share to Protein Conformation

Share to Viral Envelope Proteins

Share to Viral Tropism

Source

Open in PubMed Open full text

Identifiers

PMID: 27929061
DOI: 10.1038/ncomms13557
PMCID: PMC5155155

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

Structural basis for Epstein-Barr virus host cell tropism mediated by gp42 and gHgL entry glycoproteins.PMID 27929061Read ↗

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

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

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

Mutational Analyses of Epstein-Barr Virus Glycoprotein 42 Reveal Functional Domains Not Involved in Receptor Binding but Required for Membrane FusionSemantic proximity Read ↗

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 ↗

Cleavage and secretion of Epstein-Barr virus glycoprotein 42 promote membrane fusion with B lymphocytes.Semantic proximity Read ↗

Structural basis of Epstein-Barr virus gp350 receptor recognition and neutralizationSemantic proximity Read ↗

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

Non-overlapping epitopes on the gHgL-gp42 complex for the rational design of a triple-antibody cocktail against EBV infectionSemantic proximity Read ↗

Epstein-Barr Virus Infection of Polarized Epithelial Cells via the Basolateral Surface by Memory B Cell-Mediated Transfer InfectionSemantic proximity Read ↗

Coreceptor restriction within the HLA-DQ locus for Epstein-Barr virus infection.Semantic proximity Read ↗

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

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