Evidence map›Paper›PMID 34281393›Full record

ArticlemBio2021

Near-Pan-neutralizing, Plasma Deconvoluted Antibody N49P6 Mimics Host Receptor CD4 in Its Quaternary Interactions with the HIV-1 Envelope Trimer.

William D Tolbert, Dung N Nguyen, Zahra Rikhtegaran Tehrani, Mohammad M Sajadi, Marzena Pazgier

Open access · goldAbstract read
In one paragraph

Article in mBio, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.7field-weighted citation impact, top 35% 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

4 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
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

5 authors at 2 institutions in 1 country.

William D Tolbert *Infectious Disease Division, Department of Medicine, Uniformed Services University of the Health Sciencesgrid.265436.0, Bethesda, Maryland, USA.
Dung N Nguyen *Infectious Disease Division, Department of Medicine, Uniformed Services University of the Health Sciencesgrid.265436.0, Bethesda, Maryland, USA.
Zahra Rikhtegaran TehraniDivision of Vaccine Research, Institute of Human Virology, University of Maryland School of Medicine, Baltimore, Maryland, USA.
Mohammad M SajadiDivision of Vaccine Research, Institute of Human Virology, University of Maryland School of Medicine, Baltimore, Maryland, USA.
Marzena PazgierInfectious Disease Division, Department of Medicine, Uniformed Services University of the Health Sciencesgrid.265436.0, Bethesda, Maryland, USA.
Uniformed Services University of the Health Sciences · USUniversity of Maryland, Baltimore · US

Funding

Physical Resources CoreP01AI120756 · NIAID · DUKE UNIVERSITY · PI TOMARAS, GEORGIA DORIS · 2016 to 2020
$17.1M
Novel bNAB-based treatment and prevention of HIV-1R01AI155150 · NIAID · UNIVERSITY OF MARYLAND BALTIMORE · PI SAJADI, MOHAMMAD MOHSENI · 2021 to 2024
$2.8M
Engineering of pan-neutralizing anti-HIV envelope antibodiesR01AI147870 · NIAID · UNIVERSITY OF MARYLAND BALTIMORE · PI SAJADI, MOHAMMAD MOHSENI · 2020 to 2024
$2.5M
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
Multispecific antibodies as therapeutic agents for HIV-1I01BX004525 · VA · BALTIMORE VA MEDICAL CENTER · PI Mohammad Mohseni Sajadi · 2020 to 2027
–
BLRD VA I01 BX004525NIAID NIH HHS P01 AI120756NIAID NIH HHS R01 AI116274NIAID NIH HHS R01 AI129769NIAID NIH HHS R01 AI147870NIAID NIH HHS R01 AI155150
6 · The paper itself

Abstract

The first step in HIV-1 entry is the attachment of the envelope (Env) trimer to target cell CD4. As such, the CD4-binding site (CD4bs) remains one of the few universally accessible sites for antibodies (Abs). We recently described a method of isolating Abs directly from the circulating plasma and described a panel of broadly neutralizing Abs (bnAbs) from an HIV-1 "elite neutralizer" referred to as patient N49 (N49 Ab lineage [M. M. Sajadi, A. Dashti, Z. R. Tehrani, W. D. Tolbert, et al., Cell 173:1783-1795.e14, 2018, https://doi.org/10.1016/j.cell.2018.03.061]). Here, we describe the molecular details of antigen recognition by N49P6, an Ab of the N49 lineage that recapitulates most of the neutralization breadth and potency of the donor's plasma IgG. Our studies done in the context of monomeric and trimeric antigens indicate that N49P6 combines many characteristics of known CD4bs-specific bnAbs with features that are unique to the N49 Ab lineage to achieve its remarkable neutralization breadth. These include the omission of the CD4 Phe

Indexed as

Antibodies, NeutralizingBinding SitesBinding Sites, AntibodyCD4 AntigensCrystallizationEpitopesHIV-1HIV AntibodiesHIV Envelope Protein gp120Host Microbial InteractionsHumansNeutralization TestsProtein MultimerizationAntibodies, NeutralizingCD4 AntigensEpitopesHIV AntibodiesHIV Envelope Protein gp120CD4-binding siteHIVN49P lineagenear-pan-neutralizingneutralizing antibodies

Identifiers

PMID34281393
PMCPMC8406290
OpenAlexW3185070783

What OpenQuestion holds

Textmetadata
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.