Evidence map›Paper›PMID 34491988›Full record

ArticlePLoS computational biology2021

Structural and energetic profiling of SARS-CoV-2 receptor binding domain antibody recognition and the impact of circulating variants.

Rui Yin, Johnathan D Guest, Ghazaleh Taherzadeh, Ragul Gowthaman, Ipsa Mittra, Jane Quackenbush, Brian G Pierce

Open access · goldAbstract read
In one paragraph

Article in PLoS computational biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.0field-weighted citation impact, top 20% 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

10 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
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  9. Article
  10. Neutralizing activity of Sputnik V vaccine sera against SARS-CoV-2 variants.medRxiv : the preprint server for health sciences · 2021
    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

7 authors at 1 institution in 1 country.

Rui YinUniversity of Maryland Institute for Bioscience and Biotechnology Research, Rockville, Maryland, United States of America.ORCID 0000-0001-5330-8306
Johnathan D GuestUniversity of Maryland Institute for Bioscience and Biotechnology Research, Rockville, Maryland, United States of America.ORCID 0000-0003-1521-5242
Ghazaleh TaherzadehUniversity of Maryland Institute for Bioscience and Biotechnology Research, Rockville, Maryland, United States of America.
Ragul GowthamanUniversity of Maryland Institute for Bioscience and Biotechnology Research, Rockville, Maryland, United States of America.
Ipsa MittraUniversity of Maryland Institute for Bioscience and Biotechnology Research, Rockville, Maryland, United States of America.ORCID 0000-0002-0482-4037
Jane QuackenbushUniversity of Maryland Institute for Bioscience and Biotechnology Research, Rockville, Maryland, United States of America.
Brian G PierceUniversity of Maryland Institute for Bioscience and Biotechnology Research, Rockville, Maryland, United States of America.ORCID 0000-0003-4821-0368
Advanced Bioscience Laboratories (United States) · US

Funding

High Resolution Modeling and Design of T-Cell ReceptorsR01GM126299 · NIGMS · UNIV OF MARYLAND, COLLEGE PARK · PI PIERCE, BRIAN G. · 2018 to 2021
$1.3M
NIGMS NIH HHS R01 GM126299
6 · The paper itself

Abstract

The SARS-CoV-2 pandemic highlights the need for a detailed molecular understanding of protective antibody responses. This is underscored by the emergence and spread of SARS-CoV-2 variants, including Alpha (B.1.1.7) and Delta (B.1.617.2), some of which appear to be less effectively targeted by current monoclonal antibodies and vaccines. Here we report a high resolution and comprehensive map of antibody recognition of the SARS-CoV-2 spike receptor binding domain (RBD), which is the target of most neutralizing antibodies, using computational structural analysis. With a dataset of nonredundant experimentally determined antibody-RBD structures, we classified antibodies by RBD residue binding determinants using unsupervised clustering. We also identified the energetic and conservation features of epitope residues and assessed the capacity of viral variant mutations to disrupt antibody recognition, revealing sets of antibodies predicted to effectively target recently described viral variants. This detailed structure-based reference of antibody RBD recognition signatures can inform therapeutic and vaccine design strategies.

Indexed as

Antibodies, ViralSpike Glycoprotein, CoronavirusBinding SitesCluster AnalysisComputational BiologyCOVID-19HumansModels, MolecularProtein BindingSARS-CoV-2Antibodies, ViralSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2

Identifiers

PMID34491988
PMCPMC8448325
OpenAlexW3197834953

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.