ArticleVirus research2022
Insight towards the effect of the multi basic cleavage site of SARS-CoV-2 spike protein on cellular proteases.
Article in Virus research, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 12 citations in OpenAlex.
- Structure-based virtual screening methods for the identification of novel phytochemical inhibitors targeting furin protease for the management of COVID-19.Frontiers in cellular and infection microbiology · 2024Article
- Fibrinolytic system and COVID-19: From an innovative view of epithelial ion transport.Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · 2023Review
- Urokinase System in Pathogenesis of Pulmonary Fibrosis: A Hidden Threat of COVID-19.International journal of molecular sciences · 2023Article
- The Association ofInternational journal of molecular sciences · 2022Article
- Consensus docking and MM-PBSA computations identify putative furin protease inhibitors for developing potential therapeutics against COVID-19.Structural chemistry · 2022Article
- Vaccines efficacy to SARS-CoV-2 variants require holistic knowledge of viral immunology and protein biochemistry.Human vaccines & immunotherapeutics · 2021Article
- Pathophysiologic mechanisms of cerebral endotheliopathy and stroke due to Sars-CoV-2.Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2021Review
- An in silico deep learning approach to multi-epitope vaccine design: a SARS-CoV-2 case study.Scientific reports · 2021Article
- Should we discount the laboratory origin of COVID-19?Environmental chemistry letters · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection presents an immense global health problem. Spike (S) protein of coronavirus is the primary determinant of its entry into the host as it consists of both receptor binding and fusion domain. Besides tissue tropism, and host range, coronavirus pathogenesis are primarily controlled by the interaction of S protein with the cell receptor. Moreover, the proteolytic activation of S protein by host cell proteases plays a decisive role. The host-cell proteases have shown to be involved in the proteolysis of S protein and cleaving it into two functional subunits, S1 and S2, during the maturation process. In the present study, the interaction of the S protein of SARS-CoV-2 with different host proteases like furin, cathepsin B, and plasmin has been analyzed using molecular docking and molecular dynamics (MD) simulation. Incorporation of the furin cleavage site (R-R-A-R) in the S protein of SARS-CoV-2 has been studied by mutating the individual amino acid. MD simulation results suggest the polytropic nature of the S protein. Our analysis indicated that a single amino acid substitution in the polybasic cleavage site of S protein perturb the binding of cellular proteases. This mutation study might help to generate an attenuated SARS-CoV-2. Besides, targeting host proteases by inhibitors may result in a practical approach to stop the cellular spread of SARS-CoV-2 and develop its antiviral.
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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.