Evidence map›Paper›PMID 29731169›Full record

ArticleCell2018

Identification of Near-Pan-neutralizing Antibodies against HIV-1 by Deconvolution of Plasma Humoral Responses.

Mohammad Mohseni Sajadi, Amir Dashti, Zahra Rikhtegaran Tehrani, William D Tolbert, Michael S Seaman, Xin Ouyang, Neelakshi Gohain, Marzena Pazgier, Dongkyoon Kim, Guy Cavet and 4 more

Abstract read
In one paragraph

Article in Cell, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers.

0numbers the graph read from it
0cells of the map it votes in
86citing papers in PubMed
–field-weighted citation impact
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

86 citing papers in PubMed.

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  14. Structural insights into VRC01-class bnAb precursors with diverse light chains elicited in the IAVI G001 human vaccine trial.Proceedings of the National Academy of Sciences of the United States of America · 2025
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26 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

14 authors.

Mohammad Mohseni SajadiDivisions of Vaccine Research and Clinical Care and Research, Institute of Human Virology, University of Maryland School of Medicine, Baltimore, MD 21201, USA; Department of Medicine, Baltimore VA Medical Center, Baltimore, MD 21201, USA; Department of Medicine, University of Maryland School of Medicine, Baltimore, MD 21201, USA. Electronic address: msajadi@ihv.umaryland.edu.
Amir DashtiDivisions of Vaccine Research and Clinical Care and Research, Institute of Human Virology, University of Maryland School of Medicine, Baltimore, MD 21201, USA.
Zahra Rikhtegaran TehraniDivisions of Vaccine Research and Clinical Care and Research, Institute of Human Virology, University of Maryland School of Medicine, Baltimore, MD 21201, USA; Virology Department, Pasteur Institute of Iran, Tehran, Iran.
William D TolbertDivisions of Vaccine Research and Clinical Care and Research, Institute of Human Virology, University of Maryland School of Medicine, Baltimore, MD 21201, USA.
Michael S SeamanCenter for Virology and Vaccine Research, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA 02115, USA.
Xin OuyangDivisions of Vaccine Research and Clinical Care and Research, Institute of Human Virology, University of Maryland School of Medicine, Baltimore, MD 21201, USA.
Neelakshi GohainDivisions of Vaccine Research and Clinical Care and Research, Institute of Human Virology, University of Maryland School of Medicine, Baltimore, MD 21201, USA.
Marzena PazgierDivisions of Vaccine Research and Clinical Care and Research, Institute of Human Virology, University of Maryland School of Medicine, Baltimore, MD 21201, USA.
Dongkyoon KimAtreca, Inc., Redwood City, CA 94063, USA.
Guy CavetAtreca, Inc., Redwood City, CA 94063, USA.
Jean YaredDepartment of Medicine, University of Maryland School of Medicine, Baltimore, MD 21201, USA.
Robert R RedfieldDivisions of Vaccine Research and Clinical Care and Research, Institute of Human Virology, University of Maryland School of Medicine, Baltimore, MD 21201, USA.
George K LewisDivisions of Vaccine Research and Clinical Care and Research, Institute of Human Virology, University of Maryland School of Medicine, Baltimore, MD 21201, USA.
Anthony L DeVicoDivisions of Vaccine Research and Clinical Care and Research, Institute of Human Virology, University of Maryland School of Medicine, Baltimore, MD 21201, USA.

Funding

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
HIV-1 acidic epitope discovery from broadly neutralizing seroantibodiesR01AI110259 · NIAID · UNIVERSITY OF MARYLAND BALTIMORE · PI SAJADI, MOHAMMAD MOHSENI · 2015 to 2019
$1.9M
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
Discovery of acidic epitopes for HIV-1 broadly neutralizing seroantibodiesI01BX002358 · VA · BALTIMORE VA MEDICAL CENTER · PI SAJADI, MOHAMMAD MOHSENI · 2015 to 2019
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BLRD VA I01 BX002358NIAID NIH HHS P01 AI124912NIAID NIH HHS R01 AI110259NIAID NIH HHS R01 AI116274NIAID NIH HHS R01 AI129769
6 · The paper itself

Abstract

Anti-HIV-1 envelope broadly neutralizing monoclonal antibodies (bNAbs) isolated from memory B cells may not fully represent HIV-1-neutralizing profiles measured in plasma. Accordingly, we characterized near-pan-neutralizing antibodies extracted directly from the plasma of two "elite neutralizers." Circulating anti-gp120 polyclonal antibodies were deconvoluted using proteomics to guide lineage analysis of bone marrow plasma cells. In both subjects, a single lineage of anti-CD4-binding site (CD4bs) antibodies explained the plasma-neutralizing activity. Importantly, members of these lineages potently neutralized 89%-100% of a multi-tier 117 pseudovirus panel, closely matching the specificity and breadth of the circulating antibodies. X-ray crystallographic analysis of one monoclonal, N49P7, suggested a unique ability to bypass the CD4bs Phe43 cavity, while reaching deep into highly conserved residues of Layer 3 of the gp120 inner domain, likely explaining its extreme potency and breadth. Further direct analyses of plasma anti-HIV-1 bNAbs should provide new insights for developing antibody-based antiviral agents and vaccines.

Indexed as

Amino Acid SequenceAntibodies, NeutralizingBinding SitesCD4 AntigensCrystallography, X-RayHIV-1HIV AntibodiesHIV Envelope Protein gp120HumansMolecular Dynamics SimulationProtein BindingProtein Structure, TertiaryRecombinant ProteinsRNA, ViralAntibodies, NeutralizingCD4 AntigensHIV AntibodiesHIV Envelope Protein gp120Recombinant ProteinsRNA, Viralantibodybroadly neutralizing antibodyHIV-1humoral immunitypan-neutralizationrepertoire

Identifiers

PMID29731169
PMCPMC6003858

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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.