Evidence map›Paper›PMID 27041594›Full record

ArticleStructure (London, England : 1993)2016

Paring Down HIV Env: Design and Crystal Structure of a Stabilized Inner Domain of HIV-1 gp120 Displaying a Major ADCC Target of the A32 Region.

William D Tolbert, Neelakshi Gohain, Maxime Veillette, Jean-Philippe Chapleau, Chiara Orlandi, Maria L Visciano, Maryam Ebadi, Anthony L DeVico, Timothy R Fouts, Andrés Finzi and 2 more

Open access · hybridAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
5.0field-weighted citation impact, top 4% 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

49 citing papers in PubMed, 71 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

12 authors at 4 institutions in 2 countries.

William D TolbertDivision of Vaccine Research, Institute of Human Virology, University of Maryland School of Medicine, Baltimore, MD 21201, USA; Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, Baltimore, MD 21201, USA.
Neelakshi GohainDivision of Vaccine Research, Institute of Human Virology, University of Maryland School of Medicine, Baltimore, MD 21201, USA; Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, Baltimore, MD 21201, USA.
Maxime VeilletteCentre de Recherche du CHUM, Université de Montréal, Montreal, QC H2X 0A9, Canada; Department of Microbiology, Infectiology and Immunology, Université de Montréal, Montreal, QC H2X 0A9, Canada.
Jean-Philippe ChapleauCentre de Recherche du CHUM, Université de Montréal, Montreal, QC H2X 0A9, Canada; Department of Microbiology, Infectiology and Immunology, Université de Montréal, Montreal, QC H2X 0A9, Canada.
Chiara OrlandiDivision of Vaccine Research, Institute of Human Virology, University of Maryland School of Medicine, Baltimore, MD 21201, USA; Department of Microbiology and Immunology, University of Maryland School of Medicine, Baltimore, MD 21201, USA.
Maria L ViscianoDivision of Vaccine Research, Institute of Human Virology, University of Maryland School of Medicine, Baltimore, MD 21201, USA; Department of Microbiology and Immunology, University of Maryland School of Medicine, Baltimore, MD 21201, USA.
Maryam EbadiDivision of Vaccine Research, Institute of Human Virology, University of Maryland School of Medicine, Baltimore, MD 21201, USA; Department of Medicine, University of Maryland School of Medicine, Baltimore, MD 21201, USA.
Anthony L DeVicoDivision of Vaccine Research, Institute of Human Virology, University of Maryland School of Medicine, Baltimore, MD 21201, USA; Department of Medicine, University of Maryland School of Medicine, Baltimore, MD 21201, USA.
Timothy R FoutsProfectus BioSciences, Inc., Baltimore, MD 21224, USA.
Andrés FinziCentre de Recherche du CHUM, Université de Montréal, Montreal, QC H2X 0A9, Canada; Department of Microbiology, Infectiology and Immunology, Université de Montréal, Montreal, QC H2X 0A9, Canada; Department of Microbiology and Immunology, McGill University, Montreal, QC H2X 0A9, Canada.
George K LewisDivision of Vaccine Research, Institute of Human Virology, University of Maryland School of Medicine, Baltimore, MD 21201, USA; Department of Microbiology and Immunology, University of Maryland School of Medicine, Baltimore, MD 21201, USA.
Marzena PazgierDivision of Vaccine Research, Institute of Human Virology, University of Maryland School of Medicine, Baltimore, MD 21201, USA; Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, Baltimore, MD 21201, USA. Electronic address: mpazgier@ihv.umaryland.edu.
University of Maryland, Baltimore · USUniversité de Montréal · CACentre Hospitalier de l’Université de Montréal · CAProfectus Biosciences (United States) · US

Funding

Project 3- Mucosal Determinants of Virus TransmissionP01AI124912 · NIAID · UNIVERSITY OF MARYLAND BALTIMORE · PI GALLO, ROBERT C · 2016 to 2019
$14.4M
Broadly Neutralizing Monoclonal Antibodies Against HIV-1R01AI087181 · NIAID · UNIVERSITY OF MARYLAND BALTIMORE · PI LEWIS, GEORGE K · 2010 to 2014
$2.7M
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
CIHR 119334CIHR 134117CIHR 291485NIAID NIH HHS P01 AI124912NIAID NIH HHS R01 AI087181NIAID NIH HHS R01 AI116274NIAID NIH HHS R01 AI129769
6 · The paper itself

Abstract

Evidence supports a role of antibody-dependent cellular cytotoxicity (ADCC) toward transitional epitopes in the first and second constant (C1-C2) regions of gp120 (A32-like epitopes) in preventing HIV-1 infection and in vaccine-induced protection. Here, we describe the first successful attempt at isolating the inner domain (ID) of gp120 as an independent molecule that encapsulates the A32-like region within a minimal structural unit of the HIV-1 Env. Through structure-based design, we developed ID2, which consists of the ID expressed independently of the outer domain and stabilized in the CD4-bound conformation by an inter-layer disulfide bond. ID2 expresses C1-C2 epitopes in the context of CD4-triggered full-length gp120 but without any known neutralizing epitope present. Thus, ID2 represents a novel probe for the analysis and/or selective induction of antibody responses to the A32 epitope region. We also present the crystal structure of ID2 complexed with mAb A32, which defines its epitope.

Indexed as

Molecular Docking SimulationAntibodies, MonoclonalAntigen-Antibody ComplexBinding Sites, AntibodyCD4 AntigensEpitopesHIV Envelope Protein gp120Antibodies, MonoclonalAntigen-Antibody ComplexCD4 AntigensEpitopesgp120 protein, Human immunodeficiency virus 1HIV Envelope Protein gp120

Identifiers

PMID27041594
PMCPMC4856543
OpenAlexW2312381581

What OpenQuestion holds

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LicenceCC BY
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.