Evidence map›Paper›PMID 21697467›Full record

ArticleJournal of virology2011

Binding of the mannose-specific lectin, griffithsin, to HIV-1 gp120 exposes the CD4-binding site.

Kabamba Bankoledi Alexandre, Elin S Gray, Ralph Pantophlet, Penny L Moore, James B McMahon, Ereck Chakauya, Barry R O'Keefe, Rachel Chikwamba, Lynn Morris

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
2.5field-weighted citation impact, top 11% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

41 citing papers in PubMed, 60 citations in OpenAlex.

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  17. Design of Poly(lactic-Pharmaceutics · 2019
    Article
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  19. Lectins from red algae and their biomedical potential.Journal of applied phycology · 2018
    Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 4 institutions in 3 countries.

Kabamba Bankoledi AlexandreAIDS Virus Research Unit, National Institute for Communicable Diseases, Johannesburg, Private Bag X4, Sandringham 2131, Johannesburg, South Africa.
Elin S Gray
Ralph Pantophlet
Penny L Moore
James B McMahon
Ereck Chakauya
Barry R O'Keefe
Rachel Chikwamba
Lynn Morris
National Institute for Communicable DiseasesCenter for Cancer Research · USCouncil for Scientific and Industrial Research · ZASimon Fraser University · CA

Funding

Molecular Targets ProgramZICBC010469 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI OKEEFE, BARRY · 2009 to 2018
$31.4M
TUBERCULOSIS SUPPLEMENTD43TW000231 · FIC · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI ABDOOL KARIM, QUARRAISHA · 1993 to 2014
$13.1M
FIC NIH HHS D43 TW000231FIC NIH HHS D43TW00231Intramural NIH HHS
6 · The paper itself

Abstract

The glycans on HIV-1 gp120 play an important role in shielding neutralization-sensitive epitopes from antibody recognition. They also serve as targets for lectins that bind mannose-rich glycans. In this study, we investigated the interaction of the lectin griffithsin (GRFT) with HIV-1 gp120 and its effects on exposure of the CD4-binding site (CD4bs). We found that GRFT enhanced the binding of HIV-1 to plates coated with anti-CD4bs antibodies b12 and b6 or the CD4 receptor mimetic CD4-IgG2. The average enhancement of b12 or b6 binding was higher for subtype B viruses than for subtype C, while for CD4-IgG2, it was similar for both subtypes, although lower than observed with antibodies. This GRFT-mediated enhancement of HIV-1 binding to b12 was reflected in synergistic neutralization for 2 of the 4 viruses tested. The glycan at position 386, which shields the CD4bs, was involved in both GRFT-mediated enhancement of binding and neutralization synergism between GRFT and b12. Although GRFT enhanced CD4bs exposure, it simultaneously inhibited ligand binding to the coreceptor binding site, suggesting that GRFT-dependent enhancement and neutralization utilize independent mechanisms. This study shows for the first time that GRFT interaction with gp120 exposes the CD4bs through binding the glycan at position 386, which may have implications for how to access this conserved site.

Indexed as

Algal ProteinsAntibodies, NeutralizingBinding SitesCD4 AntigensHIV AntibodiesHIV Envelope Protein gp120HumansLectinsMannose-Binding LectinsNeutralization TestsPlant LectinsProtein BindingAlgal ProteinsAntibodies, NeutralizingCD4 Antigensgp120 protein, Human immunodeficiency virus 1griffithsin protein, GriffithsiaHIV AntibodiesHIV Envelope Protein gp120LectinsMannose-Binding LectinsPlant Lectins

Identifiers

PMID21697467
PMCPMC3165825
OpenAlexW2147201324

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.