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 role of individual carbohydrate-binding sites in the function of the potent anti-HIV lectin griffithsin.

Molecular pharmaceutics - 4 Sept 2012

Xue Jie, Gao Yongguang, Hoorelbeke Bart, Kagiampakis Ioannis, Zhao Bo, Demeler Borries, Balzarini Jan, Liwang Patricia J

Abstract excerpt

Griffithsin (GRFT) is a lectin that has been shown to inhibit HIV infection by binding to high mannose glycan structures on the surface of gp120, and it is among the most potent HIV entry inhibitors reported so far. However, important biochemical details on the antiviral mechanism of GRFT action remain unexplored. In order to understand the role of the three individual carbohydrate-binding sites (CBS) in GRFT,...

Read the complete abstract on PubMed

Topics

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

Share to Anti-HIV Agents
Share to Carbohydrates

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to HIV Envelope Protein gp120

Share to HIV Infections

Share to Magnetic Resonance Spectroscopy

Share to Mannose

Share to Plant Lectins

Source

Open in PubMed Open full text

Identifiers

PMID: 22827601
DOI: 10.1021/mp300194b
PMCID: PMC3474606

Genes

CBS
SPR

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The role of individual carbohydrate-binding sites in the function of the potent anti-HIV lectin griffithsin.PMID 22827601Read ↗

Potent inhibition of HIV-1 fusion by cyanovirin-N requires only a single high affinity carbohydrate binding site: characterization of low affinity carbohydrate binding site knockout mutants.Semantic proximity Read ↗

Carbohydrate-binding agents cause deletions of highly conserved glycosylation sites in HIV GP120: a new therapeutic concept to hit the achilles heel of HIV.Semantic proximity Read ↗

Solution and crystal structures of a sugar binding site mutant of cyanovirin-N: no evidence of domain swapping.Semantic proximity Read ↗

Conformational gating of dimannose binding to the antiviral protein cyanovirin revealed from the crystal structure at 1.35 A resolution.Semantic proximity Read ↗

The highly conserved glycan at asparagine 260 of HIV-1 gp120 is indispensable for viral entry.Semantic proximity Read ↗

Mutational pathways, resistance profile, and side effects of cyanovirin relative to human immunodeficiency virus type 1 strains with N-glycan deletions in their gp120 envelopes.Semantic proximity Read ↗

Rational and computational design of stabilized variants of cyanovirin-N that retain affinity and specificity for glycan ligands.Semantic proximity Read ↗

Identification of N-acetylglucosamine binding residues in Griffonia simplicifolia lectin II.Semantic proximity Read ↗

Actinohivin: specific amino acid residues essential for anti-HIV activity.Semantic proximity Read ↗

Stacking interactions between carbohydrate and protein quantified by combination of theoretical and experimental methods.Semantic proximity Read ↗

Removal of Clinically Relevant SARS-CoV-2 Variants by An Affinity Resin Containing <i>Galanthus nivalis</i> AgglutininSemantic proximity Read ↗

It depends on the hinge: a structure-functional analysis of galectin-8, a tandem-repeat type lectin.Semantic proximity Read ↗

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