Evidence map›Paper›PMID 34386694›Full record

ArticleAntibody therapeutics2021

SARS-CoV-2 receptor-binding mutations and antibody contact sites.

Marios Mejdani, Kiandokht Haddadi, Chester Pham, Radhakrishnan Mahadevan

Abstract read
In one paragraph

Article in Antibody therapeutics, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed.

  1. Article
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  4. Review
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  9. Review
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  11. Article
  12. Implementation of an in-house real-time reverse transcription-PCR assay for the rapid detection of the SARS-CoV-2 Marseille-4 variant.Journal of clinical virology : the official publication of the Pan American Society for Clinical Virology · 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

4 authors.

Marios MejdaniDepartment of Chemical Engineering and Applied Chemistry, University of Toronto, Toronto, ON M5S 3E5, Canada.
Kiandokht HaddadiDepartment of Chemical Engineering and Applied Chemistry, University of Toronto, Toronto, ON M5S 3E5, Canada.
Chester PhamDepartment of Chemical Engineering and Applied Chemistry, University of Toronto, Toronto, ON M5S 3E5, Canada.
Radhakrishnan MahadevanDepartment of Chemical Engineering and Applied Chemistry, University of Toronto, Toronto, ON M5S 3E5, Canada.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) mutations can impact infectivity, viral load, and overall morbidity/mortality during infection. In this analysis, we look at the mutational landscape of the SARS-CoV-2 receptor-binding domain, a structure that is antigenic and allows for viral binding to the host. We develop a bioinformatics platform and analyze 104 193 Global Initiative on Sharing All Influenza Data sequences acquired on 15 October 2020, with a majority of sequences (96%) containing point mutations. We report high frequency mutations with improved binding affinity to ACE2 including S477N, N439K, V367F, and N501Y and address the potential impact of RBD mutations on antibody binding. The high frequency S477N mutation is present in 6.7% of all SARS-CoV-2 sequences, co-occurs with D614G, and is currently present in 14 countries. To address RBD-antibody interactions, we take a subset of human-derived antibodies and define their interacting residues using PDBsum. Our analysis shows that RBD mutations were found in approximately 9% of our dataset, with some mutations improving RBD-ACE2 interactions. We also show that antibody-mediated immunity against SARS-CoV-2 enlists broad coverage of the RBD, with multiple antibodies targeting a variety of RBD regions. These data suggest that it is unlikely for neutralization/RBD antibody binding to be significantly impacted, as a whole, in the presence of RBD point mutations that conserve the RBD structure.

Indexed as

antigenic evolutionbioinformaticsCOVID-19mutationsreceptor-binding domainSARS-CoV-2

Identifiers

PMID34386694
PMCPMC8353666

What OpenQuestion holds

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LicenceCC BY-NC
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.