Evidence map›Paper›PMID 30540944›Full record

ArticleCell reports2018

V2-Directed Vaccine-like Antibodies from HIV-1 Infection Identify an Additional K169-Binding Light Chain Motif with Broad ADCC Activity.

Charmaine van Eeden, Constantinos Kurt Wibmer, Cathrine Scheepers, Simone I Richardson, Molati Nonyane, Bronwen Lambson, Nonhlanhla N Mkhize, Balakrishnan Vijayakumar, Zizhang Sheng, Sherry Stanfield-Oakley and 17 more

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Cell reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed, 29 citations in OpenAlex.

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  17. The antibody response in HIV-1-infected donors.Current opinion in HIV and AIDS · 2019
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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

27 authors at 6 institutions in 2 countries.

Charmaine van EedenNational Institute for Communicable Diseases of the National Health Laboratory Service, Johannesburg 2131, South Africa; Faculty of Health Sciences, University of the Witwatersrand, Johannesburg 2000, South Africa.
Constantinos Kurt WibmerNational Institute for Communicable Diseases of the National Health Laboratory Service, Johannesburg 2131, South Africa; Faculty of Health Sciences, University of the Witwatersrand, Johannesburg 2000, South Africa.
Cathrine ScheepersNational Institute for Communicable Diseases of the National Health Laboratory Service, Johannesburg 2131, South Africa; Faculty of Health Sciences, University of the Witwatersrand, Johannesburg 2000, South Africa.
Simone I RichardsonNational Institute for Communicable Diseases of the National Health Laboratory Service, Johannesburg 2131, South Africa; Faculty of Health Sciences, University of the Witwatersrand, Johannesburg 2000, South Africa.
Molati NonyaneNational Institute for Communicable Diseases of the National Health Laboratory Service, Johannesburg 2131, South Africa.
Bronwen LambsonNational Institute for Communicable Diseases of the National Health Laboratory Service, Johannesburg 2131, South Africa; Faculty of Health Sciences, University of the Witwatersrand, Johannesburg 2000, South Africa.
Nonhlanhla N MkhizeNational Institute for Communicable Diseases of the National Health Laboratory Service, Johannesburg 2131, South Africa; Faculty of Health Sciences, University of the Witwatersrand, Johannesburg 2000, South Africa.
Balakrishnan VijayakumarProtein Structure-Function Research Unit, University of the Witwatersrand, Johannesburg 2000, South Africa.
Zizhang ShengDepartment of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10027, USA; Department of Systems Biology, Zukerman Mind Brain Behavior Institute, Columbia University, New York, NY 10027, USA.
Sherry Stanfield-OakleyDuke Human Vaccine Institute, Duke University, Durham, NC 27710, USA.
Jinal N BhimanNational Institute for Communicable Diseases of the National Health Laboratory Service, Johannesburg 2131, South Africa; Faculty of Health Sciences, University of the Witwatersrand, Johannesburg 2000, South Africa.
Valerie BekkerNational Institute for Communicable Diseases of the National Health Laboratory Service, Johannesburg 2131, South Africa.
Tandile HermanusNational Institute for Communicable Diseases of the National Health Laboratory Service, Johannesburg 2131, South Africa.
Batsirai MabvakureNational Institute for Communicable Diseases of the National Health Laboratory Service, Johannesburg 2131, South Africa; Faculty of Health Sciences, University of the Witwatersrand, Johannesburg 2000, South Africa.
Arshad IsmailNational Institute for Communicable Diseases of the National Health Laboratory Service, Johannesburg 2131, South Africa.
M Anthony MoodyDuke Human Vaccine Institute, Duke University, Durham, NC 27710, USA.
Kevin WieheDuke Human Vaccine Institute, Duke University, Durham, NC 27710, USA.
Nigel GarrettCentre for the AIDS Programme of Research in South Africa (CAPRISA), University of KwaZulu Natal, Durban 4041, South Africa.
Salim Abdool KarimCentre for the AIDS Programme of Research in South Africa (CAPRISA), University of KwaZulu Natal, Durban 4041, South Africa.
Heini DirrProtein Structure-Function Research Unit, University of the Witwatersrand, Johannesburg 2000, South Africa.
Manuel A FernandesMolecular Sciences Institute, School of Chemistry, University of the Witwatersrand, Johannesburg 2000, South Africa.
Yasien SayedProtein Structure-Function Research Unit, University of the Witwatersrand, Johannesburg 2000, South Africa.
Lawrence ShapiroDepartment of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10027, USA; Vaccine Research Center, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20892-9806, USA.
Guido FerrariDuke Human Vaccine Institute, Duke University, Durham, NC 27710, USA.
Barton F HaynesDuke Human Vaccine Institute, Duke University, Durham, NC 27710, USA.
Penny L MooreNational Institute for Communicable Diseases of the National Health Laboratory Service, Johannesburg 2131, South Africa; Faculty of Health Sciences, University of the Witwatersrand, Johannesburg 2000, South Africa; Centre for the AIDS Programme of Research in South Africa (CAPRISA), University of KwaZulu Natal, Durban 4041, South Africa.
Lynn MorrisNational Institute for Communicable Diseases of the National Health Laboratory Service, Johannesburg 2131, South Africa; Faculty of Health Sciences, University of the Witwatersrand, Johannesburg 2000, South Africa; Centre for the AIDS Programme of Research in South Africa (CAPRISA), University of KwaZulu Natal, Durban 4041, South Africa. Electronic address: lynnm@nicd.ac.za.
National Health Laboratory Service · ZAUniversity of the Witwatersrand · ZADuke University · USCentre for the AIDS Programme of Research in South Africa · ZAColumbia University · USUniversity of KwaZulu-Natal · ZA

Funding

The Viral Set Point in HIV-1 Subtype C InfectionU19AI051794 · NIAID · UNIVERSITY OF KWAZULU-NATAL · PI ABDOOL KARIM, SALIM S · 2002 to 2007
$22.5M
TUBERCULOSIS SUPPLEMENTD43TW000231 · FIC · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI ABDOOL KARIM, QUARRAISHA · 1993 to 2014
$13.1M
Evolution of glycan-reactive broadly neutralizing anti-v2 antibodies in HIV infecR01AI104387 · NIAID · WITS HEALTH CONSORTIUM (PTY), LTD · PI MORRIS, LYNN · 2013 to 2016
$2.0M
Data commons for 'omic, microscopy and analysis core facilitiesS10OD018164 · OD · DUKE UNIVERSITY · PI WRAY, GREGORY A. · 2014 to 2014
$598k
FIC NIH HHS D43 TW000231NIAID NIH HHS R01 AI104387NIAID NIH HHS U19 AI051794NIH HHS S10 OD018164
6 · The paper itself

Abstract

Antibodies that bind residue K169 in the V2 region of the HIV-1 envelope correlated with reduced risk of infection in the RV144 vaccine trial but were restricted to two ED-motif-encoding light chain genes. Here, we identify an HIV-infected donor with high-titer V2 peptide-binding antibodies and isolate two antibody lineages (CAP228-16H/19F and CAP228-3D) that mediate potent antibody-dependent cell-mediated cytotoxicity (ADCC). Both lineages use the IGHV5-51 heavy chain germline gene, similar to the RV144 antibody CH58, but one lineage (CAP228-16H/19F) uses a light chain without the ED motif. A cocrystal structure of CAP228-16H bound to a V2 peptide identified a IGLV3-21 gene-encoded DDxD motif that is used to bind K169, with a mechanism that allows CAP228-16H to recognize more globally relevant V2 immunotypes. Overall, these data further our understanding of the development of cross-reactive, V2-binding, antiviral antibodies and effectively expand the human light chain repertoire able to respond to RV144-like immunogens.

Indexed as

AIDS VaccinesAllelesAmino Acid SequenceAntibody-Dependent Cell CytotoxicityHIV AntibodiesHIV Envelope Protein gp120HIV InfectionsHumansImmunoglobulin Light ChainsLysineModels, MolecularPeptidesProtein BindingTissue DonorsAIDS VaccinesHIV AntibodiesHIV Envelope Protein gp120Immunoglobulin Light ChainsLysinePeptidesADCCantibody evolutionCAP228CH58ED motifHIVK169RV144 vaccine responseV2 antibodiesV2 structure

Identifiers

PMID30540944
PMCPMC6342559
OpenAlexW2903937718

What OpenQuestion holds

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Registered trials

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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.