Evidence map›Paper›PMID 29056481›Full record

ArticleStructure (London, England : 1993)2017

Targeting the Late Stage of HIV-1 Entry for Antibody-Dependent Cellular Cytotoxicity: Structural Basis for Env Epitopes in the C11 Region.

William D Tolbert, Neelakshi Gohain, Nirmin Alsahafi, Verna Van, Chiara Orlandi, Shilei Ding, Loïc Martin, Andrés Finzi, George K Lewis, Krishanu Ray and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

30 citing papers in PubMed, 45 citations in OpenAlex.

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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

11 authors at 4 institutions in 3 countries.

William D TolbertDivision of Vaccine Research, Institute of Human Virology, Baltimore, MD, USA; Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, 725 West Lombard Street, Baltimore, MD 21201, USA.
Neelakshi GohainDivision of Vaccine Research, Institute of Human Virology, Baltimore, MD, USA; Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, 725 West Lombard Street, Baltimore, MD 21201, USA.
Nirmin AlsahafiCentre de Recherche du CHUM, Université de Montréal, Montreal, QC, Canada; CEA, Joliot, Service d'Ingénierie Moléculaire des Protéines, 91191 Gif-sur-Yvette, France.
Verna VanDivision of Vaccine Research, Institute of Human Virology, Baltimore, MD, USA; Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, 725 West Lombard Street, Baltimore, MD 21201, USA.
Chiara OrlandiDivision of Vaccine Research, Institute of Human Virology, Baltimore, MD, USA; Department of Microbiology and Immunology, University of Maryland School of Medicine, Baltimore, MD, USA.
Shilei DingCentre de Recherche du CHUM, Université de Montréal, Montreal, QC, Canada; Department of Microbiology, Infectiology and Immunology, Université de Montréal, Montreal, QC, Canada.
Loïc MartinCEA, Joliot, Service d'Ingénierie Moléculaire des Protéines, 91191 Gif-sur-Yvette, France.
Andrés FinziCentre de Recherche du CHUM, Université de Montréal, Montreal, QC, Canada; Department of Microbiology, Infectiology and Immunology, Université de Montréal, Montreal, QC, Canada; Department of Microbiology and Immunology, McGill University, Montreal, QC, Canada.
George K LewisDivision of Vaccine Research, Institute of Human Virology, Baltimore, MD, USA; Department of Microbiology and Immunology, University of Maryland School of Medicine, Baltimore, MD, USA.
Krishanu RayDepartment of Biochemistry and Molecular Biology, University of Maryland School of Medicine, 725 West Lombard Street, Baltimore, MD 21201, USA.
Marzena PazgierDivision of Vaccine Research, Institute of Human Virology, Baltimore, MD, USA; Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, 725 West Lombard Street, Baltimore, MD 21201, USA. Electronic address: mpazgier@ihv.umaryland.edu.
University of Maryland, Baltimore · USCentre Hospitalier de l’Université de Montréal · CACommissariat à l'Énergie Atomique et aux Énergies Alternatives · FRMcGill University · CA

Funding

ZWITTERION SURFACTANT DDMAB FOR IMPROV STABIL OF PROTEINP41RR001209 · NCRR · STANFORD UNIVERSITY · PI GONZALEZ, ANA M · 1985 to 2011
$38.9M
Physical Resources CoreP01AI120756 · NIAID · DUKE UNIVERSITY · PI TOMARAS, GEORGIA DORIS · 2016 to 2020
$17.1M
Project 3- Mucosal Determinants of Virus TransmissionP01AI124912 · NIAID · UNIVERSITY OF MARYLAND BALTIMORE · PI GALLO, ROBERT C · 2016 to 2019
$14.4M
Unlocking Envelope: A New Strategy for a Functional Cure Through Antibody-Dependent Cell-Mediated CytotoxicityR01AI129769 · NIAID · UNIVERSITY OF MARYLAND BALTIMORE · PI PAZGIER, MARZENA ELZBIETA · 2017 to 2021
$2.3M
Structural Targeting of Potentially Protective gp120 Epitopes in the C1/C2 RegionR01AI116274 · NIAID · UNIVERSITY OF MARYLAND BALTIMORE · PI PAZGIER, MARZENA ELZBIETA · 2016 to 2019
$1.5M
Conformational Dynamics of HIV Envelope by Single Molecule SpectroscopyR01GM117836 · NIGMS · UNIVERSITY OF MARYLAND BALTIMORE · PI RAY, KRISHANU · 2015 to 2018
$1.3M
CIHR 352417NCRR NIH HHS P41 RR001209NIAID NIH HHS P01 AI120756NIAID NIH HHS P01 AI124912NIAID NIH HHS R01 AI116274NIAID NIH HHS R01 AI129769NIGMS NIH HHS R01 GM117836
6 · The paper itself

Abstract

Antibodies can have an impact on HIV-1 infection in multiple ways, including antibody-dependent cellular cytotoxicity (ADCC), a correlate of protection observed in the RV144 vaccine trial. One of the most potent ADCC-inducing epitopes on HIV-1 Env is recognized by the C11 antibody. Here, we present the crystal structure, at 2.9 Å resolution, of the C11-like antibody N12-i3, in a quaternary complex with the HIV-1 gp120, a CD4-mimicking peptide M48U1, and an A32-like antibody, N5-i5. Antibody N12-i3 recognizes an epitope centered on the N-terminal "eighth strand" of a critical β sandwich, which our analysis indicates to be emblematic of a late-entry state, after the gp120 detachment. In prior entry states, this sandwich comprises only seven strands, with the eighth strand instead pairing with a portion of the gp120 C terminus. The conformational gymnastics of HIV-1 gp120 thus includes altered β-strand pairing, possibly to reduce immunogenicity, although nevertheless still recognized by the human immune system.

Indexed as

Amino Acid SequenceAntibodies, MonoclonalAntibodies, ViralAntibody-Dependent Cell CytotoxicityBinding SitesCD4 AntigensCell LineCrystallography, X-RayEpitopesHIV-1HIV AntibodiesHIV Envelope Protein gp120HumansImmunity, InnateModels, MolecularMolecular MimicryAntibodies, MonoclonalAntibodies, ViralCD4 AntigensEpitopesHIV AntibodiesHIV Envelope Protein gp120Peptidesantibody-dependent cellular cytotoxicity (ADCC)C11 epitope regionC11-like antibodycluster A epitopescrystal structureHIV-1 entryN12-i3 antibody

Identifiers

PMID29056481
PMCPMC5677539
OpenAlexW2766647922

What OpenQuestion holds

Textmetadata
LicenceTDM
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.