SARS-CoV 2 spike protein S1 subunit as an ideal target for stable vaccines: A bioinformatic study.
Phylogenetic and 3D modelling
SARS-CoV-2
Spike glycoprotein
Journal
Materials today. Proceedings
ISSN: 2214-7853
Titre abrégé: Mater Today Proc
Pays: England
ID NLM: 101668762
Informations de publication
Date de publication:
2022
2022
Historique:
pubmed:
27
7
2021
medline:
27
7
2021
entrez:
26
7
2021
Statut:
ppublish
Résumé
The Covid-19 a pandemic infectious disease and affected life across the world resulting in over 188.65 million confirmed cases across 223 countries, territories and areas with 4.06 million deaths. It is caused by a severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and spike (S) protein of SARS-CoV-2, which plays a key role in the receptor recognition and cell membrane fusion process, is composed of two subunits, S1 and S2. The S1 subunit contains a receptor-binding domain (RBD) that recognizes and binds to the host receptor angiotensin-converting enzyme 2 (ACE2), while the S2 subunit mediates viral cell membrane fusion. Hence, it is a key target for developing neutralizing antibodies. Here, we have performed phylogenetic analysis and structural modeling of the SARS-CoV-2 spike glycoprotein, which is found highly conserved. The overall percent protein sequence identity from the SARS-CoV-2 spike protein sequences from the NCBI database was 99.68%. The functional domains of the S protein reveal that the S1 subunit was highly conserved (99.70%) than the S2 subunit (99.66%). Further, the 319-541 residues (RBD) of amino acids within the S1 domain were 100% similar among the spike protein. The 3D modeling of SARS-CoV-2 spike glycoprotein indicated that S protein has four domains with five protein units and the S1 subunit from 1 to 289 amino acid of domain 1 is highly conserved without any change in the ligand interaction site. This analysis clearly suggests that the S1 subunit (RBD 319-541) can be used as a target region for stable and safe vaccine development.
Identifiants
pubmed: 34307057
doi: 10.1016/j.matpr.2021.07.163
pii: S2214-7853(21)05022-7
pmc: PMC8279943
doi:
Types de publication
Journal Article
Langues
eng
Pagination
904-912Informations de copyright
© 2021 Elsevier Ltd. All rights reserved. Selection and peer-review under responsibility of the scientific committee of the Web International Conference on Accelerating Innovations in Material Science – 2020.
Déclaration de conflit d'intérêts
The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
Références
Antiviral Res. 2020 Jun;178:104792
pubmed: 32272173
Nat Protoc. 2015 Jun;10(6):845-58
pubmed: 25950237
Nature. 2020 Oct;586(7830):567-571
pubmed: 32756549
Protein Sci. 2015 Oct;24(10):1549-59
pubmed: 26174372
Nat Rev Drug Discov. 2020 May;19(5):305-306
pubmed: 32273591
Front Immunol. 2020 Oct 07;11:576622
pubmed: 33117378
Microbes Infect. 2020 Jul - Aug;22(6-7):245-253
pubmed: 32437926
Nat Rev Microbiol. 2019 Mar;17(3):181-192
pubmed: 30531947
EBioMedicine. 2020 Aug;58:102890
pubmed: 32707445
Virology. 2015 May;479-480:498-507
pubmed: 25866377
J Virol. 2003 Aug;77(16):8801-11
pubmed: 12885899
Emerg Microbes Infect. 2020 Dec;9(1):900-902
pubmed: 32380903
N Engl J Med. 2020 May 21;382(21):1969-1973
pubmed: 32227757
Mol Biol Evol. 2018 Jun 1;35(6):1547-1549
pubmed: 29722887
Emerg Infect Dis. 2005 Jul;11(7):1016-20
pubmed: 16022774
Lancet. 2020 Feb 22;395(10224):565-574
pubmed: 32007145
Biochem Biophys Res Commun. 2007 Jul 20;359(1):174-9
pubmed: 17533109
Bioinformatics. 2011 Jan 1;27(1):132-3
pubmed: 21075745
Biochimie. 2009 Jul;91(7):876-87
pubmed: 19383526
Sci Immunol. 2020 Jun 11;5(48):
pubmed: 32527802
Cell Rep. 2020 Jun 2;31(9):107725
pubmed: 33500101
Front Immunol. 2020 May 12;11:1022
pubmed: 32574260
J Mol Biol. 2020 May 1;432(10):3309-3325
pubmed: 32320687
Nature. 2020 Aug;584(7821):353-363
pubmed: 32659783
3 Biotech. 2021 Feb;11(2):44
pubmed: 33457171
Cell. 2020 Apr 16;181(2):281-292.e6
pubmed: 32155444
Nat Rev Microbiol. 2009 Mar;7(3):226-36
pubmed: 19198616
J Biol Chem. 2004 Jan 30;279(5):3197-201
pubmed: 14670965
Nature. 2014 Oct 23;514(7523):455-61
pubmed: 25296255
Trends Immunol. 2020 May;41(5):355-359
pubmed: 32249063
Viruses. 2012 Jun;4(6):1011-33
pubmed: 22816037
Mol Biol Evol. 1987 Jul;4(4):406-25
pubmed: 3447015
J Virol. 2013 Jun;87(11):6150-60
pubmed: 23536651
Cell. 2020 Aug 6;182(3):722-733.e11
pubmed: 32645327
Proc Natl Acad Sci U S A. 2020 May 26;117(21):11727-11734
pubmed: 32376634
Cell Mol Immunol. 2020 Jun;17(6):613-620
pubmed: 32203189
Nucleic Acids Res. 2006 Jul 1;34(Web Server issue):W75-8
pubmed: 16845113
Hum Vaccin Immunother. 2020 Dec 1;16(12):3055-3060
pubmed: 32845733
Nucleic Acids Res. 2018 Jan 4;46(D1):D708-D717
pubmed: 29040670
Bioinformatics. 2006 Jan 15;22(2):129-33
pubmed: 16301202
Front Public Health. 2020 May 28;8:216
pubmed: 32574299
Nat Commun. 2020 Mar 27;11(1):1620
pubmed: 32221306
Science. 2020 Jul 17;369(6501):330-333
pubmed: 32366695
Evolution. 1985 Jul;39(4):783-791
pubmed: 28561359
Cell. 2020 Apr 16;181(2):271-280.e8
pubmed: 32142651
Cell Rep Med. 2021 Apr 20;2(4):100252
pubmed: 33842900
Cell Mol Immunol. 2020 Jul;17(7):765-767
pubmed: 32047258
Immunity. 2020 Apr 14;52(4):583-589
pubmed: 32259480
Nature. 2020 Mar;579(7798):265-269
pubmed: 32015508