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

A nanobody specific to prefusion glycoprotein B neutralizes HSV-1 and HSV-2

3 Sept 2025

Abstract excerpt

Abstract The nine human herpesviruses, including herpes simplex virus 1 and 2, human cytomegalovirus and Epstein–Barr virus, present a significant burden to global public health 1 . Their envelopes contain at least ten different glycoproteins, which are necessary for host cell tropism, attachment and entry 2 . The best conserved among them, glycoprotein B (gB), is essential as it performs membrane fusion by...

Read the complete abstract on PubMed

Topics

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

Share to Cytomegalovirus and herpesvirus research
Share to Hepatitis Viruses Studies and Epidemiology
Share to Herpesvirus Infections and Treatments

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 40903574
DOI: 10.1038/s41586-025-09438-5

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A nanobody specific to prefusion glycoprotein B neutralizes HSV-1 and HSV-2PMID 40903574Read ↗

Structure-based design of soluble prefusion-stabilized herpes simplex virus type 2 glycoprotein B antigensSemantic proximity Read ↗

The Fusion Loops of the Initial Prefusion Conformation of Herpes Simplex Virus 1 Fusion Protein Point Toward the MembraneSemantic proximity Read ↗

The native conformational landscape and priming mechanism of herpes simplex virus glycoprotein B.Semantic proximity Read ↗

Design, Structure, and Immunogenicity of a Soluble Prefusion-stabilized EBV gB AntigenSemantic proximity Read ↗

Structure-based design of a soluble human cytomegalovirus glycoprotein B antigen stabilized in a prefusion-like conformationSemantic proximity Read ↗

Herpes Simplex Virus Glycoprotein B Mutations Define Structural Sites in Domain I, the Membrane Proximal Region, and the Cytodomain That Regulate Entry.Semantic proximity Read ↗

Crystal Structure of the Human Cytomegalovirus Glycoprotein BSemantic proximity Read ↗

Mechanism of neutralization of herpes simplex virus by antibodies directed at the fusion domain of glycoprotein B.Semantic proximity Read ↗

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

Interplay between the Herpes Simplex Virus 1 gB Cytodomain and the gH Cytotail during Cell-Cell Fusion.Semantic proximity Read ↗

Antibody evasion by the N terminus of murid herpesvirus-4 glycoprotein B.Semantic proximity Read ↗

Prefusion-Stabilized Lassa Virus Trimer Identifies Neutralizing Nanobodies and Reveals an Apex-Situated Site of VulnerabilitySemantic proximity Read ↗

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