Evidence map›Paper›PMID 35467422›Full record

ArticlemBio2022

Structure of a Vaccine-Induced, Germline-Encoded Human Antibody Defines a Neutralizing Epitope on the SARS-CoV-2 Spike N-Terminal Domain.

Clara G Altomare, Daniel C Adelsberg, Juan Manuel Carreno, Iden A Sapse, Fatima Amanat, Ali H Ellebedy, Viviana Simon, Florian Krammer, Goran Bajic

Abstract read
In one paragraph

Article in mBio, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

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  10. Central tolerance shapes the neutralizing B cell repertoire against a persisting virus in its natural host.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
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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

9 authors.

Clara G AltomareDepartment of Microbiology, Icahn School of Medicine at Mount Sinaigrid.59734.3c, New York, New York, USA.
Daniel C AdelsbergDepartment of Microbiology, Icahn School of Medicine at Mount Sinaigrid.59734.3c, New York, New York, USA.
Juan Manuel CarrenoDepartment of Microbiology, Icahn School of Medicine at Mount Sinaigrid.59734.3c, New York, New York, USA.
Iden A SapseDepartment of Microbiology, Icahn School of Medicine at Mount Sinaigrid.59734.3c, New York, New York, USA.
Fatima AmanatDepartment of Microbiology, Icahn School of Medicine at Mount Sinaigrid.59734.3c, New York, New York, USA.
Ali H EllebedyDepartment of Pathology and Immunology, Washington University School of Medicine, St. Louis, Missouri, USA.
Viviana SimonDepartment of Microbiology, Icahn School of Medicine at Mount Sinaigrid.59734.3c, New York, New York, USA.
Florian KrammerDepartment of Microbiology, Icahn School of Medicine at Mount Sinaigrid.59734.3c, New York, New York, USA.ORCID 0000-0003-4121-776X
Goran BajicDepartment of Microbiology, Icahn School of Medicine at Mount Sinaigrid.59734.3c, New York, New York, USA.ORCID 0000-0003-0480-4324

Funding

COLLABORATIVE INFLUENZA VACCINE INNOVATION CENTER: UNIVERSAL INFLUENZA VACCINE RESEARCH75N93019C00051 · NIAID · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI KRAMMER, FLORIAN · 2019 to 2025
$105.4M
TRAINING PROGRAM: MECHANISMS OF VIRUS-HOST INTERACTIONST32AI007647 · NIAID · MOUNT SINAI SCHOOL OF MEDICINE OF NYU · PI Domenico Tortorella · 2000 to 2026
$11.5M
NIAID NIH HHS 75N93019C00051NIAID NIH HHS HHSN272201400008CNIAID NIH HHS T32 AI007647
6 · The paper itself

Abstract

Structural characterization of infection- and vaccination-elicited antibodies in complex with antigen provides insight into the evolutionary arms race between the host and the pathogen and informs rational vaccine immunogen design. We isolated a germ line-encoded monoclonal antibody (mAb) from plasmablasts activated upon mRNA vaccination against severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and determined its structure in complex with the spike glycoprotein by electron cryomicroscopy (cryo-EM). We show that the mAb engages a previously uncharacterized neutralizing epitope on the spike N-terminal domain (NTD). The high-resolution structure reveals details of the intermolecular interactions and shows that the mAb inserts its heavy complementarity-determining region 3 (HCDR3) loop into a hydrophobic NTD cavity previously shown to bind a heme metabolite, biliverdin. We demonstrate direct competition with biliverdin and that, because of the conserved nature of the epitope, the mAb maintains binding to viral variants B.1.1.7 (alpha), B.1.351 (beta), B.1.617.2 (delta), and B.1.1.529 (omicron). Our study describes a novel conserved epitope on the NTD that is readily targeted by vaccine-induced antibody responses.

Indexed as

COVID-19COVID-19 VaccinesEpitopesSpike Glycoprotein, CoronavirusAntibodies, MonoclonalAntibodies, NeutralizingAntibodies, ViralBiliverdineGerm CellsHumansSARS-CoV-2Antibodies, MonoclonalAntibodies, NeutralizingAntibodies, ViralBiliverdineCOVID-19 VaccinesEpitopesSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2adaptive immunitycoronaviruselectron microscopymonoclonal antibodiesvaccine

Identifiers

PMID35467422
PMCPMC9239078

What OpenQuestion holds

Textmetadata
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.