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

Convergent HIV-1 Evolution upon Targeted Destabilization of the gp120-gp41 Interface.

Journal of virology - 23 Nov 2021

Torrents de la Peña Alba, Del Moral Sánchez Iván, Burger Judith A, Bontjer Ilja, Isik Gözde, Eggink Dirk, van Gils Marit J, Sanders Rogier W

Abstract excerpt

The HIV-1 envelope glycoprotein (Env) trimer is responsible for viral entry into target cells and is the sole target of neutralizing antibodies. The Env protein is therefore the focus of HIV-1 vaccine design. Env consists of two noncovalently linked subunits (gp120 and gp41) that form a trimer of heterodimers and this 6-subunit complex is metastable and conformationally flexible. Several approaches have been...

Read the complete abstract on PubMed

Topics

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

Share to Antibodies, Neutralizing
Share to HEK293 Cells

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

Share to HIV Envelope Protein gp120

Share to HIV Envelope Protein gp41

Share to Mutagenesis

Share to Protein Conformation

Share to Protein Multimerization

Source

Open in PubMed Open full text

Identifiers

PMID: 34586861
DOI: 10.1128/JVI.00532-21
PMCID: PMC8610599

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

Convergent HIV-1 Evolution upon Targeted Destabilization of the gp120-gp41 Interface.PMID 34586861Read ↗

Increased functional stability and homogeneity of viral envelope spikes through directed evolution.Semantic proximity Read ↗

A Universal Approach to Optimize the Folding and Stability of Prefusion-Closed HIV-1 Envelope TrimersSemantic proximity Read ↗

Functional Stability of HIV-1 Envelope Trimer Affects Accessibility to Broadly Neutralizing Antibodies at Its Apex.Semantic proximity Read ↗

Stabilized HIV-1 envelope glycoprotein trimers lacking the V1V2 domain, obtained by virus evolution.Semantic proximity Read ↗

Alterations in gp120 glycans or the gp41 fusion peptide-proximal region modulate the stability of the human immunodeficiency virus (HIV-1) envelope glycoprotein pretriggered conformationSemantic proximity Read ↗

Residues in the gp41 Ectodomain Regulate HIV-1 Envelope Glycoprotein Conformational Transitions Induced by gp120-Directed InhibitorsSemantic proximity Read ↗

Functional Anatomy of the Trimer Apex Reveals Key Hydrophobic Constraints That Maintain the HIV-1 Envelope Spike in a Closed State.Semantic proximity Read ↗

Structure-Guided Redesign Increases the Propensity of HIV Env To Generate Highly Stable Soluble TrimersSemantic proximity Read ↗

Impact of stabilizing mutations on the antigenic profile and glycosylation of membrane-expressed HIV-1 envelope glycoprotein.Semantic proximity Read ↗

Asymmetric structures and conformational plasticity of the uncleaved full-length human immunodeficiency virus (HIV-1) envelope glycoprotein trimerSemantic proximity Read ↗

Optimization of human immunodeficiency virus type 1 envelope glycoproteins with V1/V2 deleted, using virus evolution.Semantic proximity Read ↗

Global Increases in Human Immunodeficiency Virus Neutralization Sensitivity Due to Alterations in the Membrane-Proximal External Region of the Envelope Glycoprotein Can be Minimized by Distant State 1-Stabilizing ChangesSemantic proximity Read ↗

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