Evidence map›Paper›PMID 32320687›Full record

ArticleJournal of molecular biology2020

Phylogenetic Analysis and Structural Modeling of SARS-CoV-2 Spike Protein Reveals an Evolutionary Distinct and Proteolytically Sensitive Activation Loop.

Javier A Jaimes, Nicole M André, Joshua S Chappie, Jean K Millet, Gary R Whittaker

Abstract read
In one paragraph

Article in Journal of molecular biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 280 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
280citing papers in PubMed, 1 pooled it
–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

280 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
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  5. iScience · 2026
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  18. Structural proteins of human coronaviruses: what makes them different?Frontiers in cellular and infection microbiology · 2024
    Review
  19. Infectious Diseases.Advances in neurobiology · 2024
    Review
  20. Review

220 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors.

Javier A JaimesDepartment of Microbiology & Immunology, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853, USA.
Nicole M AndréDepartment of Microbiology & Immunology, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853, USA.
Joshua S ChappieDepartment of Molecular Medicine, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853, USA.
Jean K MilletUniversité Paris-Saclay, INRAE, UVSQ, Virologie et Immunologie Moléculaires, 78350 Jouy-en-Josas, France. Electronic address: jean.millet@inrae.fr.
Gary R WhittakerDepartment of Microbiology & Immunology, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853, USA; Master of Public Health Program, Cornell University, Ithaca, NY 14853, USA. Electronic address: grw7@cornell.edu.

Funding

Structural and Functional Analysis of the Coronavirus Spike Protein Fusion PeptideR01AI135270 · NIAID · CORNELL UNIVERSITY · PI DANIEL, SUSAN, WHITTAKER, GARY R · 2018 to 2021
$2.5M
NIAID NIH HHS R01 AI135270
6 · The paper itself

Abstract

The 2019 novel coronavirus (2019-nCoV/SARS-CoV-2) originally arose as part of a major outbreak of respiratory disease centered on Hubei province, China. It is now a global pandemic and is a major public health concern. Taxonomically, SARS-CoV-2 was shown to be a Betacoronavirus (lineage B) closely related to SARS-CoV and SARS-related bat coronaviruses, and it has been reported to share a common receptor with SARS-CoV (ACE-2). Subsequently, betacoronaviruses from pangolins were identified as close relatives to SARS-CoV-2. Here, we perform structural modeling of the SARS-CoV-2 spike glycoprotein. Our data provide support for the similar receptor utilization between SARS-CoV-2 and SARS-CoV, despite a relatively low amino acid similarity in the receptor binding module. Compared to SARS-CoV and all other coronaviruses in Betacoronavirus lineage B, we identify an extended structural loop containing basic amino acids at the interface of the receptor binding (S1) and fusion (S2) domains. We suggest this loop confers fusion activation and entry properties more in line with betacoronaviruses in lineages A and C, and be a key component in the evolution of SARS-CoV-2 with this structural loop affecting virus stability and transmission.

Indexed as

Amino Acid SequenceAnimalsBetacoronavirusChiropteraCoronavirus InfectionsCOVID-19EutheriaHumansModels, MolecularPandemicsPhylogenyPneumonia, ViralProteolysisSARS-CoV-2Sequence AlignmentSevere acute respiratory syndrome-related coronavirusSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2cleavage sitescoronavirusCOVID-19SARS-CoV-2spike protein

Identifiers

PMID32320687
PMCPMC7166309

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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.