Evidence map›Paper›PMID 32918944›Full record

ArticleVirus research2020

SARS-CoV-2 host tropism: An in silico analysis of the main cellular factors.

H R Rangel, J T Ortega, S Maksoud, F H Pujol, M L Serrano

Open access · greenAbstract readComparative Study
In one paragraph

Article in Virus research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.4field-weighted citation impact, top 26% 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

10 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
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  4. Efficacy of mRNA, adenoviral vector, and perfusion protein COVID-19 vaccines.Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · 2022
    Review
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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

5 authors at 4 institutions in 2 countries.

H R RangelLaboratorio de Virología Molecular, Centro de Microbiología y Biología Celular, Instituto Venezolano de Investigaciones Científicas, Caracas, Venezuela.
J T OrtegaDepartment of Pharmacology, School of Medicine, Case Western Reserve University, Cleveland, OH 44106, USA.
S MaksoudDepartment of Neurology and Experimental Therapeutics and Molecular Imaging Laboratory, Massachusetts General Hospital, MA 02129, USA.
F H PujolLaboratorio de Virología Molecular, Centro de Microbiología y Biología Celular, Instituto Venezolano de Investigaciones Científicas, Caracas, Venezuela.
M L SerranoUnidad de Química Medicinal, Facultad de Farmacia, Universidad Central de Venezuela, Caracas 1041-A, Venezuela. Electronic address: maria.serrano@ucv.ve.
Instituto Venezolano de Investigaciones Científicas · VECase Western Reserve University · USCentral University of Venezuela · VEMassachusetts General Hospital · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Recent reports have shown that small and big felines could be infected by SARS-CoV-2, while other animals, like swines and mice, are apparently not susceptible to this infection. These findings raise the question of the role of cell factors associated with early stages of the viral infection in host selectivity. The cellular receptor for SARS-CoV-2 is the Angiotensin Converting Enzyme (ACE2). Transmembrane protease serine 2 (TMPRSS2) has been shown to prime the viral spike for its interaction with its receptor. GRP78 has also been proposed as a possible co-receptor. In this study, we used several bioinformatics approaches to bring clues in the interaction of ACE2, TMPRSS2, and GRP78 with SARS-CoV-2. We selected several mammalian hosts that could play a key role in viral spread by acting as secondary hosts (cats, dogs, pigs, mice, and ferrets) and evaluated their predicted permissiveness by in silico analysis. Results showed that ionic pairs (salt bridges, N-O pair, and long-range interactions) produced between ACE2 and the viral spike has an essential function in the host interaction. On the other hand, TMPRSS2 and GRP78 are proteins with high homology in all the evaluated hosts. Thus, these proteins do not seem to play a role in host selectivity, suggesting that other factors may play a role in the non-permissivity in some of these hosts. These proteins represent however interesting cell targets that could be explored in order to control the virus replication in humans and in the intermediary hosts.

Indexed as

Viral TropismAmino Acid SequenceAngiotensin-Converting Enzyme 2AnimalsAntiviral AgentsBenzamidinesBetacoronavirusCatsCoronavirus InfectionsCOVID-19DogsEndoplasmic Reticulum Chaperone BiPFerretsGuanidinesHeat-Shock ProteinsHumansACE2 protein, humanAce2 protein, mouseAngiotensin-Converting Enzyme 2Antiviral AgentsBenzamidinesEndoplasmic Reticulum Chaperone BiPGuanidinesHeat-Shock ProteinsHSPA5 protein, humanHspa5 protein, mousenafamostatPeptidyl-Dipeptidase AReceptors, VirusSerine EndopeptidasesSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2TMPRSS2 protein, humanCOVID-19GRP78Receptor ACE2SARS-CoV-2TMPRSS2

Identifiers

PMID32918944
PMCPMC7480320
OpenAlexW3084170252

What OpenQuestion holds

Textmetadata
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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.