Mutation and Phylogenetic Analysis of Spike Glycoprotein of Indonesian Isolates of Severe-Acute-Respiratory-Syndrome-Coronavirus-2 (SARS-CoV-2)
Abstract
Coronavirus disease-2019 (COVID-19) is an infectious acute respiratory disease caused by SARS-CoV-2. The protein that plays a role in the entry of SARS-CoV-2 into human cells is the surface protein, or the Spike, which is thought to be the effective vaccine target to prevent SARS-CoV-2 infection. Until December 2020, Indonesia has reported 106 SARS-CoV-2 genome sequences identified from COVID-19 positive patients. The purpose of this study was to analyze the phylogenetic relationship of the Spike protein of the Indonesian isolates of SARS-CoV-2 Indonesian, as well as the virus mutations and their effects on changes in the amino acid. The 106 Indonesian SARS-CoV-2 genomes were downloaded from GISAID and the Spike nucleotide and amino acid sequences were analyzed by multiple sequence alignment (MSA) and mutation analysis using the ClustalW method. Phylogenetic trees were created using the Neighbor-Joining method in MEGA-X software. The results showed that 30 of the 106 Indonesian isolate SARS-CoV-2 Spike were 100% identical to the Wuhan-Hu-1, while the remaining 76 had experienced mutations at 1-4 sites. There were 43-point mutations in the Spike gene, 27 of which led to amino acid changes and four had not been reported in other countries. The global mutation D614G was found in 60 Indonesian isolates , of which West Java was the province with the most reports. The phylogenetic of Spike showed that the Indonesian samples have been divided into several branches that are far from Wuhan-Hu-1. This study indicates the possibility of differences in the protein structure of Indonesian isolate SARS-CoV-2 Spike that need to be further studied to manufacture a vaccine against the Indonesian strain of SARS-CoV-2.
Keywords
Full Text:
PDFReferences
Zhou P, Yang XL, Wang XG, Hu B, Zhang L, Zhang W, et al. A pneumonia outbreak associated with a new coronavirus of probable bat origin. Nature. 2020; 579(7798): 270–73.
Lu R, Zhao X, Li J, Niu P, Yang B, Wu H, et al. Genomic characterisation and epidemiology of 2019 novel coronavirus: implications for virus origins and receptor binding. The Lancet. 2020;395(10224): 565–74.
Romano M, Ruggiero A, Squeglia F, Maga G, Berisio R. A structural view of SARS-CoV-2 RNA replication machinery: RNA synthesis, proofreading and final capping. Cells. 2020; 9(1267):1-22.
Wu A, Peng Y, Huang B, Ding X, Wang X, Niu P, et al. Genome composition and divergence of the novel Coronavirus (2019-nCoV) originating in China. Cell Host Microbe. 2020;27:325–28.
Jaimes JA, André NM, Chappie JS, Millet JK, Whittaker GR. Phylogenetic analysis and structural modeling of SARS-CoV-2 Spike protein reveals an evolutionary distinct and proteolytically sensitive activation Loop. J Mol Biol. 2020; 432(10): 3309–25.
Rabi FA, Al Zoubi MS, Kasasbeh GA, Salameh DM, Al-Nasser AD. SARS-CoV-2 and Coronavirus Disease 2019: What We Know So Far. Pathogens. 2020; 9(3):231.
Belouzard S, Millet JK, Licitra BN, Whittaker GR. Mechanisms of coronavirus cell entry mediated by the viral Spike protein. Viruses. 2012; 4(6): 1011–33.
Lan J, Ge J, Yu J, Shan S, Zhou H, Fan S, et al. Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor. Nature. 2020;581(7807):215–20.
Wang M, Fu T, Hao J, Li L, Tian M, Jin N, Ren L, Li C. A recombinant Lactobacillus plantarum strain expressing the spike protein of SARS-CoV-2. International J Biol Macromol. 2020; 160:736–40.
Zha L, Zhao H, Mohsen MO, Hong L, Zhou Y, Li Z, et al. Development of a COVID-19 vaccine based on the receptor binding domain displayed on virus-like particles. bioRxiv. 2020;1–6.
Saitou N, Nei M. The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol Biol Evol. 1987;4(4): 406–25.
Kumar S, Stecher G, Li M, Knyaz C,Tamura K. MEGA X: Molecular Evolutionary Genetics Analysis across Computing Platforms F. U. Battistuzzi, ed. Mol Biol Evol. 2018;35(6): 1547–49.
Gunadi, Wibawa H, Marcellus, Hakim MS, Daniwijaya EW, Rizki LP, et al. Full-length genome characterization and phylogenetic analysis of SARS-CoV-2 virus strains from Yogyakarta and Central Java, Indonesia. PeerJ. 2020;8:e10575.
Higgins D, Thompson J, Gibson D, Tompson JD, Higgins DG, Gibson TJ. CLUSTAL W: improving the sensitivity of progressive multiple sequence aligment through sequence weighting, position-specific gap penalties and weight matrix choice, Nucleic Acid Res. 1994;22:4673–80.
Walls AC, Park YJ, Tortorici MA, Wall A, McGuire AT, Veesler D. Structure, function, and antigenicity of the SARS-CoV-2 Spike glycoprotein. Cell. 2020;181(2):281–92.
Yuan M, Wu NC, Zhu X, Lee CCD, So RTY, Lv H, et al. A highly conserved cryptic epitope in the receptor binding domains of SARS-CoV-2 and SARS-CoV. Science. 2020;368(6491):630–3.
Chaturvedi P, Han Y, Král P, Vuković L. Adaptive evolution of peptide inhibitors for mutating SARS-CoV-2. [published online ahead of print, 2020 Oct 8]. Adv Theory Simul. 2020;2000156.
Korber B, Fischer W, Gnanakaran SG, Yoon H, Theiler J, Abfalterer W, et al. Spike mutation pipeline reveals the emergence of a more transmissible form of SARS-CoV-2. bioRxiv. 2020;069054.
Isabel S, Graña-Miraglia L, Gutierrez JM, Bundalovic-Torma C, Groves HE, Isabel MR, et al. Evolutionary and structural analyses of SARS-CoV-2 D614G spike protein mutation now documented worldwide. Sci Rep. 2020;10(1):14031.
Lan J, Ge J, Yu J, Shan S, Zhou H, Fan S, et al. Structure of the SARS-CoV-2 Spike receptor-binding domain bound to the ACE2 receptor. Nature. 2020;581(7807):215–20.
Hu J, He CL, Gao QZ, Zhang GJ, Cao XX, Long QX, et al. The D614G mutation of SARS-CoV-2 spike protein enhances viral infectivity. bioRxiv. 2020;161323.
Zhang L, Jackson CB, Mou H, Ojha A, Rangarajan ES, Izard T, et al The D614G mutation in the SARS-CoV-2 spike protein reduces S1 shedding and increases infectivity. bioRxiv. 2020;2020.06.12.148726.
Hou YJ, Chiba S, Halfmann P, Ehre C, Kuroda M, Dinnon KH, et al. SARS-CoV-2 D614G variant exhibits enhanced replication ex vivo and earlier transmission in vivo. Preprint. bioRxiv. 2020;2020.09.28.317685.
Plante JA, Liu Y, Liu J, Xia H, Johnson BA, Lokugamage KG, et al. Spike mutation D614G alters SARS-CoV-2 fitness and neutralization susceptibility. Preprint. bioRxiv. 2020;2020.09.01.278689. Published 2020 Sep 2.
Ansori ANM, Kharisma VD, Muttaqin SS, Antonius Y, Parikesit AA. Genetic Variant of SARS-CoV-2 Isolates in Indonesia: Spike Glycoprotein Gene. J Pure Appl Microbiol. 2020;14(suppl 1):971–8.
Planas D, Bruel T, Grzelak L, Guivel-Benhassine F, Staropoli I, Porrot F, et al. Sensitivity of infectious SARS-CoV-2 B.1.1.7 and B.1.351 variants to neutralizing antibodies. [published online ahead of print, 2021 Mar 26]. Nat Med. 2021;10.1038/s41591-021-01318-5.
DOI: https://doi.org/10.15395/mkb.v53n1.2230
Article Metrics
Abstract view : 1171 timesPDF - 701 times
This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License.
MKB is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License
View My Stats