Evidence map›Paper›PMID 33270653›Full record

ArticlePLoS computational biology2020

Insights on cross-species transmission of SARS-CoV-2 from structural modeling.

João P G L M Rodrigues, Susana Barrera-Vilarmau, João M C Teixeira, Marija Sorokina, Elizabeth Seckel, Panagiotis L Kastritis, Michael Levitt

Open access · goldAbstract read
In one paragraph

Article in PLoS computational biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
1.5field-weighted citation impact, top 10% 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

43 citing papers in PubMed, 65 citations in OpenAlex.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 4 institutions in 4 countries.

João P G L M RodriguesDepartment of Structural Biology, Stanford University School of Medicine, Stanford, California, United States of America.ORCID 0000-0001-9796-3193
Susana Barrera-VilarmauInstitute of Advanced Chemistry of Catalonia (IQAC), CSIC, Barcelona, Spain.ORCID 0000-0003-4868-6593
João M C TeixeiraProgram in Molecular Medicine, The Hospital for Sick Children, Toronto, Ontario, Canada.ORCID 0000-0002-9113-0622
Marija SorokinaZIK HALOMEM & Institute of Biochemistry and Biotechnology, Martin Luther University Halle-Wittenberg, Biozentrum, Halle (Saale), Germany.ORCID 0000-0003-0195-0094
Elizabeth SeckelDepartment of Obstetrics and Gynecology, Stanford University School of Medicine, Stanford, California, United States of America.ORCID 0000-0001-5910-649X
Panagiotis L KastritisZIK HALOMEM & Institute of Biochemistry and Biotechnology, Martin Luther University Halle-Wittenberg, Biozentrum, Halle (Saale), Germany.ORCID 0000-0002-1463-8422
Michael LevittDepartment of Structural Biology, Stanford University School of Medicine, Stanford, California, United States of America.ORCID 0000-0002-8414-7397
Stanford University · USMartin Luther University Halle-Wittenberg · DEHospital for Sick Children · CAInstitute of Advanced Chemistry of Catalonia · ES

Funding

Emergent Properties of Complex Systems: From Atoms to Macromolecules; from Humans to SocietiesR35GM122543 · NIGMS · STANFORD UNIVERSITY · PI MICHAEL LEVITT · 2017 to 2026
$5.1M
NIGMS NIH HHS R35 GM122543
6 · The paper itself

Abstract

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is responsible for the ongoing global pandemic that has infected more than 31 million people in more than 180 countries worldwide. Like other coronaviruses, SARS-CoV-2 is thought to have been transmitted to humans from wild animals. Given the scale and widespread geographical distribution of the current pandemic and confirmed cases of cross-species transmission, the question of the extent to which this transmission is possible emerges, as well as what molecular features distinguish susceptible from non-susceptible animal species. Here, we investigated the structural properties of several ACE2 orthologs bound to the SARS-CoV-2 spike protein. We found that species known not to be susceptible to SARS-CoV-2 infection have non-conservative mutations in several ACE2 amino acid residues that disrupt key polar and charged contacts with the viral spike protein. Our models also allow us to predict affinity-enhancing mutations that could be used to design ACE2 variants for therapeutic purposes. Finally, our study provides a blueprint for modeling viral-host protein interactions and highlights several important considerations when designing these computational studies and analyzing their results.

Indexed as

COVID-19SARS-CoV-2Angiotensin-Converting Enzyme 2AnimalsBinding SitesComputational BiologyConserved SequenceGenetic Predisposition to DiseaseHost-Pathogen InteractionsHumansMolecular Dynamics SimulationMutationSpike Glycoprotein, CoronavirusViral ZoonosesAngiotensin-Converting Enzyme 2Spike Glycoprotein, Coronavirusspike protein, SARS-CoV-2

Identifiers

PMID33270653
PMCPMC7714162
OpenAlexW3109674309

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.