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Tytuł pozycji:

A Comparative Study between Spanish and British SARS-CoV-2 Variants.

Tytuł:
A Comparative Study between Spanish and British SARS-CoV-2 Variants.
Autorzy:
Jimenez Ruiz JA; Research Group on Electronic Technology and Industrial Computing (TIC-150), Department of Artificial Intelligence, University of Seville, 41013 Sevilla, Spain.
Lopez Ramirez C; Unidad Médico-Quirúrgica de Enfermedades Respiratorias, Instituto de Biomedicina de Sevilla (IBiS), Hospital Universitario Virgen del Rocío/Universidad de Sevilla, 41013 Sevilla, Spain.; Centro de Investigación Biomédica en Red de Enfermedades Respiratorias (CIBERES), Instituto de Salud Carlos III, 28029 Madrid, Spain.
Lopez-Campos JL; Unidad Médico-Quirúrgica de Enfermedades Respiratorias, Instituto de Biomedicina de Sevilla (IBiS), Hospital Universitario Virgen del Rocío/Universidad de Sevilla, 41013 Sevilla, Spain.; Centro de Investigación Biomédica en Red de Enfermedades Respiratorias (CIBERES), Instituto de Salud Carlos III, 28029 Madrid, Spain.
Źródło:
Current issues in molecular biology [Curr Issues Mol Biol] 2021 Nov 16; Vol. 43 (3), pp. 2036-2047. Date of Electronic Publication: 2021 Nov 16.
Typ publikacji:
Comparative Study; Journal Article
Język:
English
Imprint Name(s):
Publication: 2021- : Basel, Switzerland : MDPI
Original Publication: Wymondham, Norfolk, UK : Caister Academic Press,
MeSH Terms:
Virus Internalization*
COVID-19/*virology
SARS-CoV-2/*genetics
SARS-CoV-2/*physiology
Amino Acid Sequence ; Angiotensin-Converting Enzyme 2/metabolism ; Base Sequence ; COVID-19/epidemiology ; COVID-19/metabolism ; COVID-19/pathology ; Computational Biology ; Humans ; Protein Binding ; SARS-CoV-2/isolation & purification ; SARS-CoV-2/metabolism ; Sequence Alignment ; Spain/epidemiology ; Spike Glycoprotein, Coronavirus/genetics ; Spike Glycoprotein, Coronavirus/metabolism ; United Kingdom/epidemiology
References:
Bull World Health Organ. 2020 Jul 01;98(7):495-504. (PMID: 32742035)
Gene Rep. 2020 Jun;19:100682. (PMID: 32300673)
Cell. 2020 Apr 16;181(2):281-292.e6. (PMID: 32155444)
Epidemics. 2021 Sep;36:100484. (PMID: 34375814)
Nat Biotechnol. 2004 Aug;22(8):1035-6. (PMID: 15286655)
PLoS Comput Biol. 2010 Aug 26;6(8):. (PMID: 20865174)
J Clin Microbiol. 2021 Oct 19;59(11):e0092121. (PMID: 34379531)
Bioinformatics. 2020 Mar 1;36(6):1765-1771. (PMID: 31697312)
Curr Med Sci. 2021 Dec;41(6):1037-1051. (PMID: 34241776)
Bioinform Biol Insights. 2021 Jun 22;15:11779322211025876. (PMID: 34220199)
Microbiol Spectr. 2021 Sep 3;9(1):e0031521. (PMID: 34378966)
Nature. 2020 May;581(7807):215-220. (PMID: 32225176)
Nature. 2020 Mar;579(7798):265-269. (PMID: 32015508)
Adv Protein Chem Struct Biol. 2018;110:203-249. (PMID: 29412997)
J Biol Regul Homeost Agents. 2021 Feb 24;35(1):1-4. (PMID: 33377359)
Science. 2020 Mar 13;367(6483):1260-1263. (PMID: 32075877)
Biotechnol J. 2021 Nov;16(11):e2100207. (PMID: 34379353)
Bioinformatics. 2007 Nov 1;23(21):2947-8. (PMID: 17846036)
Int J Mol Sci. 2021 Feb 08;22(4):. (PMID: 33567580)
J Biol Chem. 1968 Jul 10;243(13):3557-9. (PMID: 5658538)
Nature. 2022 Feb;602(7896):294-299. (PMID: 34818667)
Cell Mol Immunol. 2020 Jun;17(6):621-630. (PMID: 32415260)
Virology. 2021 Sep;561:107-116. (PMID: 34217923)
J Cell Immunol. 2021;3(2):103-108. (PMID: 33969357)
J Clin Invest. 2021 Sep 15;131(18):. (PMID: 34375308)
Microb Pathog. 2021 Apr;153:104741. (PMID: 33588026)
Rev Med Virol. 2021 May;31(3):e2183. (PMID: 33594794)
Microbiol Spectr. 2021 Sep 3;9(1):e0047221. (PMID: 34378968)
Acta Crystallogr D Biol Crystallogr. 2013 May;69(Pt 5):701-9. (PMID: 23633579)
Science. 2021 Apr 9;372(6538):. (PMID: 33658326)
Nucleic Acids Res. 2003 Jul 1;31(13):3381-5. (PMID: 12824332)
Nat Commun. 2021 Aug 9;12(1):4886. (PMID: 34373458)
Methods Mol Biol. 2016;1414:47-62. (PMID: 27094285)
PLoS One. 2021 Aug 11;16(8):e0253574. (PMID: 34379620)
Biophys J. 2010 May 19;98(9):1921-30. (PMID: 20441756)
Science. 1992 Jun 5;256(5062):1443-5. (PMID: 1604319)
Nucleic Acids Res. 2013 Jul;41(Web Server issue):W597-600. (PMID: 23671338)
Proteins. 2022 May;90(5):1044-1053. (PMID: 34375467)
Cell Mol Life Sci. 2021 Jan;78(2):531-544. (PMID: 32780149)
Contributed Indexing:
Keywords: COVID-19; SARS-CoV-2; computational docking; genomics characterization; in silico
Substance Nomenclature:
0 (Spike Glycoprotein, Coronavirus)
0 (spike protein, SARS-CoV-2)
EC 3.4.17.23 (ACE2 protein, human)
EC 3.4.17.23 (Angiotensin-Converting Enzyme 2)
SCR Organism:
SARS-CoV-2 variants
Entry Date(s):
Date Created: 20211210 Date Completed: 20211222 Latest Revision: 20220716
Update Code:
20240105
PubMed Central ID:
PMC8929045
DOI:
10.3390/cimb43030140
PMID:
34889898
Czasopismo naukowe
The study of the interaction between the SARS-CoV-2 spike protein and the angiotensin-converting enzyme 2 (ACE2) receptor is key to understanding binding affinity and stability. In the present report, we sought to investigate the differences between two already sequenced genome variants (Spanish and British) of SARS-CoV-2. Methods: In silico model evaluating the homology, identity and similarity in the genome sequence and the structure and alignment of the predictive spike by computational docking methods. Results: The identity results between the Spanish and British variants of the Spike protein were 28.67%. This close correspondence in the results between the Spanish and British SARS-CoV-2 variants shows that they are very similar (99.99%). The alignment obtained results in four deletions. There were 23 nucleotide substitutions also predicted which could affect the functionality of the proteins produced from this sequence. The interaction between the binding receptor domain from the spike protein and the ACE2 receptor produces some of the mutations found and, therefore, the energy of this ligand varies. However, the estimated antigenicity of the British variant is higher than its Spanish counterpart. Conclusions: Our results indicate that minimal mutations could interfere in the infectivity of the virus due to changes in the fitness between host cell recognition and interaction proteins. In particular, the N501Y substitution, situated in the RBD of the spike of the British variant, might be the reason for its extraordinary infective potential.

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