Evidence map›Paper›PMID 17372000›Full record

ArticleJournal of immunology (Baltimore, Md. : 1950)2007

The role of antibody polyspecificity and lipid reactivity in binding of broadly neutralizing anti-HIV-1 envelope human monoclonal antibodies 2F5 and 4E10 to glycoprotein 41 membrane proximal envelope epitopes.

S Munir Alam, Mildred McAdams, David Boren, Michael Rak, Richard M Scearce, Feng Gao, Zenaido T Camacho, Daniel Gewirth, Garnett Kelsoe, Pojen Chen and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Journal of immunology (Baltimore, Md. : 1950), 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 166 papers.

0numbers the graph read from it
0cells of the map it votes in
166citing papers in PubMed
9.1field-weighted citation impact, top 1% 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

166 citing papers in PubMed, 257 citations in OpenAlex.

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106 more citing papers are in PubMed but not listed here.

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

11 authors at 2 institutions in 1 country.

S Munir AlamDepartment of Medicine, Duke Human Vaccine Institute, Duke University School of Medicine, RP1 Circuit Drive, Durham, NC 27710, USA. alam0004@mc.duke.edu
Mildred McAdams
David Boren
Michael Rak
Richard M Scearce
Feng Gao
Zenaido T Camacho
Daniel Gewirth
Garnett Kelsoe
Pojen Chen
Barton F Haynes
Duke University · USUniversity of California, Los Angeles · US

Funding

Viral Sequencing CoreU19AI067854 · NIAID · DUKE UNIVERSITY · PI BHARDWAJ, NINA · 2006 to 2011
$290.5M
HIV, TB, and Malaria Vaccine Development for AfricaP01AI052816 · NIAID · DUKE UNIVERSITY · PI HAYNES, BARTON F · 2003 to 2007
$14.5M
Duke University Center for Translational ResearchP30AI051445 · NIAID · DUKE UNIVERSITY · PI FROTHINGHAM, RICHARD · 2002 to 2006
$8.1M
NIAID NIH HHS AI 06785-01NIAID NIH HHS AI 51445NIAID NIH HHS P01 AI052816NIAID NIH HHS P01 AI 52816NIAID NIH HHS P30 AI051445NIAID NIH HHS U19 AI067854
6 · The paper itself

Abstract

Two neutralizing human mAbs, 2F5 and 4E10, that react with the HIV-1 envelope gp41 membrane proximal region are also polyspecific autoantibodies that bind to anionic phospholipids. To determine the autoantibody nature of these Abs, we have compared their reactivities with human anti-cardiolipin mAbs derived from a primary antiphospholipid syndrome patient. To define the role of lipid polyreactivity in binding of 2F5 and 4E10 mAbs to HIV-1 envelope membrane proximal epitopes, we determined the kinetics of binding of mAbs 2F5 and 4E10 to their nominal gp41 epitopes vs liposome-gp41 peptide conjugates. Both anti-HIV-1 mAbs 2F5 and 4E10 bound to cardiolipin with K(d) values similar to those of autoimmune anti-cardiolipin Abs, IS4 and IS6. Binding kinetics studies revealed that mAb 2F5 and 4E10 binding to their respective gp41 peptide-lipid conjugates could best be defined by a two-step (encounter-docking) conformational change model. In contrast, binding of 2F5 and 4E10 mAbs to linear peptide epitopes followed a simple Langmuir model. A mouse mAb, 13H11, that cross-blocks mAb 2F5 binding to the gp41 epitope did not cross-react with lipids nor did it neutralize HIV-1 viruses. Taken together, these data demonstrate the similarity of 2F5 and 4E10 mAbs to known anti-cardiolipin Abs and support the model that mAb 2F5 and 4E10 binding to HIV-1 involves both viral lipid membrane and gp41 membrane proximal epitopes.

Indexed as

Antibody SpecificityAmino Acid SequenceAnimalsAntibodies, MonoclonalAntiphospholipid SyndromeAutoantibodiesCardiolipinsHIV-1HIV AntibodiesHIV Envelope Protein gp41HumansLipidsLiposomesMiceMolecular Sequence DataAntibodies, MonoclonalAutoantibodiesCardiolipinsHIV AntibodiesHIV Envelope Protein gp41LipidsLiposomes

Identifiers

PMID17372000
PMCPMC2262928
OpenAlexW2095910488

What OpenQuestion holds

Textmetadata
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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.