Evidence map›Paper›PMID 32837536›Full record

ArticleEvolutionary applications2020

SARS-CoV-2, an evolutionary perspective of interaction with human ACE2 reveals undiscovered amino acids necessary for complex stability.

Vinicio Armijos-Jaramillo, Justin Yeager, Claire Muslin, Yunierkis Perez-Castillo

Open access · goldAbstract read
In one paragraph

Article in Evolutionary applications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.3field-weighted citation impact, top 11% 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

29 citing papers in PubMed, 53 citations in OpenAlex.

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  19. Can the SARS-CoV-2 Spike Protein Bind Integrins Independent of the RGD Sequence?Frontiers in cellular and infection microbiology · 2021
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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

4 authors at 1 institution in 1 country.

Vinicio Armijos-JaramilloGrupo de Bio-Quimioinformática Carrera de Ingeniería en Biotecnología Facultad de Ingeniería y Ciencias Agropecuarias Universidad de Las Américas Quito Ecuador.ORCID https://orcid.org/0000-0003-2965-2515
Justin YeagerBiodiversidad Medio Ambiente y Salud (BIOMAS) Dirección General de Investigación Universidad de Las Américas Quito Ecuador.ORCID https://orcid.org/0000-0001-8692-6311
Claire MuslinOne Health Research Group Faculty of Health Sciences Universidad de Las Américas Quito Ecuador.ORCID https://orcid.org/0000-0002-2746-6914
Yunierkis Perez-CastilloGrupo de Bio-Quimioinformática y Escuela de Ciencias Físicas y Matemáticas Universidad de Las Américas Quito Ecuador.ORCID https://orcid.org/0000-0002-3710-0035
Universidad de Las Américas · EC

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The emergence of SARS-CoV-2 has resulted in nearly 1,280,000 infections and 73,000 deaths globally so far. This novel virus acquired the ability to infect human cells using the SARS-CoV cell receptor hACE2. Because of this, it is essential to improve our understanding of the evolutionary dynamics surrounding the SARS-CoV-2 hACE2 interaction. One way theory predicts selection pressures should shape viral evolution is to enhance binding with host cells. We first assessed evolutionary dynamics in select betacoronavirus spike protein genes to predict whether these genomic regions are under directional or purifying selection between divergent viral lineages, at various scales of relatedness. With this analysis, we determine a region inside the receptor-binding domain with putative sites under positive selection interspersed among highly conserved sites, which are implicated in structural stability of the viral spike protein and its union with human receptor ACE2. Next, to gain further insights into factors associated with recognition of the human host receptor, we performed modeling studies of five different betacoronaviruses and their potential binding to hACE2. Modeling results indicate that interfering with the salt bridges at hot spot 353 could be an effective strategy for inhibiting binding, and hence for the prevention of SARS-CoV-2 infections. We also propose that a glycine residue at the receptor-binding domain of the spike glycoprotein can have a critical role in permitting bat SARS-related coronaviruses to infect human cells.

Indexed as

ACE2coronavirusmolecular dynamicspositive selectionpurifying selectionSARS‐CoV‐2spike protein

Identifiers

PMID32837536
PMCPMC7262083
OpenAlexW3015464442

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.