Evidence map›Paper›PMID 34188776›Full record

ArticleComputational and structural biotechnology journal2021

Evolution, correlation, structural impact and dynamics of emerging SARS-CoV-2 variants.

Austin N Spratt, Saathvik R Kannan, Lucas T Woods, Gary A Weisman, Thomas P Quinn, Christian L Lorson, Anders Sönnerborg, Siddappa N Byrareddy, Kamal Singh

Open access · goldAbstract read
In one paragraph

Article in Computational and structural biotechnology journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed, 1 pooled it
1.8field-weighted citation impact, top 13% 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

21 citing papers in PubMed, 1 synthesis or guideline pooled it, 28 citations in OpenAlex.

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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 at 2 institutions in 2 countries.

Austin N SprattChristopher S. Bond Life Sciences Center, University of Missouri, Columbia, MO 65211, USA.
Saathvik R KannanChristopher S. Bond Life Sciences Center, University of Missouri, Columbia, MO 65211, USA.
Lucas T WoodsChristopher S. Bond Life Sciences Center, University of Missouri, Columbia, MO 65211, USA.
Gary A WeismanChristopher S. Bond Life Sciences Center, University of Missouri, Columbia, MO 65211, USA.
Thomas P QuinnDepartment of Biochemistry, University of Missouri, Columbia, MO 65211, USA.
Christian L LorsonChristopher S. Bond Life Sciences Center, University of Missouri, Columbia, MO 65211, USA.
Anders SönnerborgDivision of Infectious Diseases, Department of Medicine, Karolinska Institute, Huddinge 14186, Stockholm, Sweden.
Siddappa N ByrareddyDivision of Clinical Microbiology, Department of Laboratory Medicine, Karolinska Institute, Huddinge 14186, Stockholm, Sweden.
Kamal SinghChristopher S. Bond Life Sciences Center, University of Missouri, Columbia, MO 65211, USA.
University of Missouri · USKarolinska Institutet · SE

Funding

VIP RECEPTORS AND SUBMANDIBULAR GLAND FUNCTIONR01DE007389 · NIDCR · UNIVERSITY OF MISSOURI-COLUMBIA · PI WEISMAN, GARY ANDREW · 1988 to 2020
$7.6M
NIDCR NIH HHS R01 DE007389
6 · The paper itself

Abstract

Severe Acute Respiratory Syndrome Coronavirus-2 (SARS-CoV-2) infections remain unmanageable in some parts of the world. As with other RNA viruses, mutations in the SARS-CoV-2 gene have been continuously evolving. Recently, four variants have been identified, B.1.1.7, B.1.351, P.1 and CAL.20C. These variants appear to be more infectious and transmissible than the original Wuhan-Hu-1 virus. Using a combination of bioinformatics and structural analyses, we show that the new SARS-CoV-2 variants emerged in the background of an already known Spike protein mutation D614G together with another mutation P323L in the RNA polymerase of SARS-CoV-2. The phylogenetic analysis showed that the CAL.20C and B.1.351 shared one common ancestor, whereas the B.1.1.7 and P.1 shared a different ancestor. Structural comparisons did not show any significant difference between the wild-type and mutant ACE2/Spike complexes. Structural analysis indicated that the N501Y mutation may increase hydrophobic interactions at the ACE2/Spike interface. However, reported greater binding affinity of N501Y Spike with ACE2 does not seem to be entirely due to increased hydrophobic interactions, given that Spike mutation R417T in P.1 or K417N in B.1.351 results in the loss of a salt-bridge interaction between ACE2 and S-RBD. The calculated change in free energy did not provide a clear trend of S protein stability of mutations in the variants. As expected, we show that the CAL.20C generally migrated from the west coast to the east coast of the USA. Taken together, the analyses suggest that the evolution of variants and their infectivity is complex and may depend upon many factors.

Indexed as

B.1.1.7B.1.351, P.1, CAL.20CCOVID-19SARS-CoVSARS-CoV-2

Identifiers

PMID34188776
PMCPMC8225291
OpenAlexW3177306668

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.