Evidence map›Paper›PMID 34915409›Full record

ArticleInternational immunopharmacology2022

E484K and N501Y SARS-CoV 2 spike mutants Increase ACE2 recognition but reduce affinity for neutralizing antibody.

Sandipan Chakraborty

Abstract read
In one paragraph

Article in International immunopharmacology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing 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

27 citing papers in PubMed.

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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

1 author.

Sandipan ChakrabortyAmity Institute of Biotechnology, Amity University, Kolkata 700135, India. Electronic address: schakraborty8@kol.amity.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SARS-CoV2 mutants B.1.1.7, B.1.351, and P.1 contain a key mutation N501Y. B.1.135 and P.1 lineages have another mutation, E484K. Here, we decode the effect of these two mutations on the host receptor, ACE2, and neutralizing antibody (B38) recognition. The N501Y RBD mutant binds to ACE2 with higher affinity due to improved π-π stacking and π-cation interactions. The higher binding affinity of the E484K mutant is caused due to the formation of additional hydrogen bond and salt-bridge interactions with ACE2. Both the mutants bind to the B38 antibody with reduced affinity due to the loss of several hydrogen-bonding interactions. The insights obtained from the study are crucial to interpret the increased transmissibility and reduced neutralization efficacy of rapidly emerging SARS-CoV2 VOCs.

Indexed as

Angiotensin-Converting Enzyme 2Antibodies, NeutralizingAntibody AffinityBinding SitesCrystallography, X-RayHumansMutationSARS-CoV-2Spike Glycoprotein, CoronavirusVirus InternalizationACE2 protein, humanAngiotensin-Converting Enzyme 2Antibodies, NeutralizingSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2ACE2 bindingAntibody bindingBinding free energyHydrogen bondsRBD mutationsπ-π and π-cation interactions

Identifiers

PMID34915409
PMCPMC8641390

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.