Evidence map›Paper›PMID 34639178›Full record

ReviewInternational journal of molecular sciences2021

SARS-CoV-2 Virus-Host Interaction: Currently Available Structures and Implications of Variant Emergence on Infectivity and Immune Response.

Luís Queirós-Reis, Priscilla Gomes da Silva, José Gonçalves, Andrea Brancale, Marcella Bassetto, João R Mesquita

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.7field-weighted citation impact, top 8% 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, 45 citations in OpenAlex.

  1. Article
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  6. Efficient Expression inMolecules (Basel, Switzerland) · 2024
    Article
  7. Review
  8. Article
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  11. Article
  12. Review
  13. Review
  14. Article
  15. Review
  16. Article
  17. Spike protein of SARS-CoV-2 variants: a brief review and practical implications.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2022
    Review
  18. Review
  19. Potential inhibitor for blocking binding between ACE2 and SARS-CoV-2 spike protein with mutations.Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · 2022
    Article
  20. Article
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

6 authors at 4 institutions in 3 countries.

Luís Queirós-ReisAbel Salazar Institute of Biomedical Sciences (ICBAS), University of Porto, 4050-313 Porto, Portugal.
Priscilla Gomes da SilvaAbel Salazar Institute of Biomedical Sciences (ICBAS), University of Porto, 4050-313 Porto, Portugal.ORCID 0000-0002-8384-0640
José GonçalvesInstitute of Sustainable Processes, University of Valladolid, 47011 Valladolid, Spain.ORCID 0000-0003-2191-527X
Andrea BrancaleCardiff School of Pharmacy and Pharmaceutical Sciences, Cardiff University, Cardiff CF10 3NB, UK.ORCID 0000-0002-9728-3419
Marcella BassettoDepartment of Chemistry, Faculty of Science and Engineering, Swansea University, Swansea SA2 8PP, UK.ORCID 0000-0002-2491-5868
João R MesquitaAbel Salazar Institute of Biomedical Sciences (ICBAS), University of Porto, 4050-313 Porto, Portugal.ORCID 0000-0001-8769-8103
Universidade do Porto · PTCardiff University · GBSwansea University · GBUniversidad de Valladolid · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Coronavirus disease 19, or COVID-19, is an infection associated with an unprecedented worldwide pandemic caused by the Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2), which has led to more than 215 million infected people and more than 4.5 million deaths worldwide. SARS-CoV-2 cell infection is initiated by a densely glycosylated spike (S) protein, a fusion protein, binding human angiotensin converting enzyme 2 (hACE2), that acts as the functional receptor through the receptor binding domain (RBD). In this article, the interaction of hACE2 with the RBD and how fusion is initiated after recognition are explored, as well as how mutations influence infectivity and immune response. Thus, we focused on all structures available in the Protein Data Bank for the interaction between SARS-CoV-2 S protein and hACE2. Specifically, the Delta variant carries particular mutations associated with increased viral fitness through decreased antibody binding, increased RBD affinity and altered protein dynamics. Combining both existing mutations and mutagenesis studies, new potential SARS-CoV-2 variants, harboring advantageous S protein mutations, may be predicted. These include mutations S13I and W152C, decreasing antibody binding, N460K, increasing RDB affinity, or Q498R, positively affecting both properties.

Indexed as

Host-Pathogen InteractionsAngiotensin-Converting Enzyme 2AnimalsCOVID-19HumansImmunityModels, MolecularMutationSARS-CoV-2Spike Glycoprotein, CoronavirusACE2 protein, humanAngiotensin-Converting Enzyme 2Spike Glycoprotein, Coronavirusspike protein, SARS-CoV-2hACE2protein structuresSARS-CoV-2Spike protein

Identifiers

PMID34639178
PMCPMC8509653
OpenAlexW3207334095

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.