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

Structures of Ebola virus GP and sGP in complex with therapeutic antibodies.

Nature microbiology - 8 Aug 2016

Pallesen Jesper, Murin Charles D, de Val Natalia, Cottrell Christopher A, Hastie Kathryn M, Turner Hannah L, Fusco Marnie L, Flyak Andrew I, Zeitlin Larry, Crowe James E, Andersen Kristian G, Saphire Erica Ollmann, Ward Andrew B

Abstract excerpt

The Ebola virus (EBOV) GP gene encodes two glycoproteins. The major product is a soluble, dimeric glycoprotein (sGP) that is secreted abundantly. Despite the abundance of sGP during infection, little is known regarding its structure or functional role. A minor product, resulting from transcriptional editing, is the transmembrane-anchored, trimeric viral surface glycoprotein (GP). GP mediates attachment to and...

Read the complete abstract on PubMed

Topics

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

Share to Antibody Formation
Share to Cross Reactions

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cryoelectron Microscopy

Share to Ebolavirus

Share to Glycoproteins

Share to Hemorrhagic Fever, Ebola

Share to Models, Structural

Share to Protein Multimerization

Source

Open in PubMed Open full text

Identifiers

PMID: 27562261
DOI: 10.1038/nmicrobiol.2016.128
PMCID: PMC5003320

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

Structures of Ebola virus GP and sGP in complex with therapeutic antibodies.PMID 27562261Read ↗

Techniques and tactics used in determining the structure of the trimeric ebolavirus glycoprotein.Semantic proximity Read ↗

Structure-Based Design of Prefusion-Stabilized Filovirus Glycoprotein Trimers.Semantic proximity Read ↗

Convergence of a common solution for broad ebolavirus neutralization by glycan cap-directed human antibodiesSemantic proximity Read ↗

Structural basis for broad neutralization of ebolaviruses by an antibody targeting the glycoprotein fusion loopSemantic proximity Read ↗

Cryo-Electron Microscopy Structure and Interactions of the Human Cytomegalovirus gHgLgO Trimer with Platelet-Derived Growth Factor Receptor AlphaSemantic proximity Read ↗

Convergence of a common solution to broad ebolavirus neutralization by glycan cap directed human antibodiesSemantic proximity Read ↗

The Roles of Ebola Virus Soluble Glycoprotein in Replication, Pathogenesis, and Countermeasure DevelopmentSemantic proximity Read ↗

Structure-function analysis of the soluble glycoprotein, sGP, of Ebola virus.Semantic proximity Read ↗

Anti-Ebola virus mAb 3A6 with unprecedented potency protects highly viremic animals from fatal outcome and physically lifts its glycoprotein target from the virion membraneSemantic proximity Read ↗

Structure of the hepatitis C virus E1E2 glycoprotein complexSemantic proximity Read ↗

Cross-reactive neutralizing human survivor monoclonal antibody BDBV223 targets the ebolavirus stalkSemantic proximity Read ↗

Single-component multilayered self-assembling nanoparticles presenting rationally designed glycoprotein trimers as Ebola virus vaccinesSemantic proximity Read ↗

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