Mutational sensitivity of D614G in spike protein of SARS-CoV-2 in Jordan

Biochemistry and Biophysics Reports - Tập 25 - Trang 100896 - 2021
Walid Al-Zyoud1, Hazem Haddad2
1Department of Biomedical Engineering, School of Applied Medical Sciences, German Jordanian University, Amman, Jordan
2Princess Haya Biotechnology Centre, Jordan University of Science and Technology, Irbid, Jordan

Tài liệu tham khảo

Wu, 2020, A new coronavirus associated with human respiratory disease in China, Nature, 579, 265, 10.1038/s41586-020-2008-3 Liu, 2020, COVID-19: the first documented coronavirus pandemic in history, Biomed. J., 43(4), 328, 10.1016/j.bj.2020.04.007 Lu, 2020, Genomic characterisation and epidemiology of 2019 novel coronavirus: implications for virus origins and receptor binding, Lancet, 395, 565, 10.1016/S0140-6736(20)30251-8 Wrapp, 2020, Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation. - PubMed - NCBI, Science, 13;367(6483), 1260, 10.1126/science.abb2507 Lan, 2020, Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor, Nature, 1 Zhang, 2020, Angiotensin-converting enzyme 2 (ACE2) as a SARS-CoV-2 receptor: molecular mechanisms and potential therapeutic target, Intensive Care Med., 46, 586, 10.1007/s00134-020-05985-9 Glowacka, 2011, Evidence that TMPRSS2 activates the severe acute respiratory syndrome coronavirus spike protein for membrane fusion and reduces viral control by the humoral immune response, J. Virol., 85, 4122, 10.1128/JVI.02232-10 Xia, 2020, Inhibition of SARS-CoV-2 (previously 2019-nCoV) infection by a highly potent pan-coronavirus fusion inhibitor targeting its spike protein that harbors a high capacity to mediate membrane fusion, Cell Res., 30, 343, 10.1038/s41422-020-0305-x Henderson R, Edwards RJ, Mansouri K, Janowska K, Stalls V, Gobeil SMC, et al. Controlling the SARS-CoV-2 Spike Glycoprotein Conformation. [cited 2020 Aug 29]. Grubaugh, 2020, Making sense of mutation: what D614G means for the COVID-19 pandemic remains unclear, Cell, 182, 794, 10.1016/j.cell.2020.06.040 Korber, 2020, Tracking changes in SARS-CoV-2 spike: evidence that D614G increases infectivity of the COVID-19 virus, Cell, 182, 812, 10.1016/j.cell.2020.06.043 Abio Madeira, 2019, vol. 47 Waterhouse, 2009, Jalview Version 2-A multiple sequence alignment editor and analysis workbench, Bioinformatics, 25, 1189, 10.1093/bioinformatics/btp033 Jones, 1999, Protein secondary structure prediction based on position-specific scoring matrices, J. Mol. Biol., 292, 195, 10.1006/jmbi.1999.3091 Moult, 2014, Critical assessment of methods of protein structure prediction (CASP) - round x, Proteins Struct Funct Bioinforma, 82, 1, 10.1002/prot.24452 Angyal A, Brown RL, Carrilero L, Green LR, Groves DC, Johnson KJ, et al. Spike Mutation Pipeline Reveals the Emergence of a More Transmissible Form of SARS-CoV-2 on Behalf of the Sheffield COVID-19 Genomics Group#, LaBranche CC2, and Montefiori DC2. Yates, 2014, SuSPect: enhanced prediction of single amino acid variant (SAV) phenotype using network features, J. Mol. Biol., 426, 2692, 10.1016/j.jmb.2014.04.026 Kelley, 2015, The Phyre2 web portal for protein modeling, prediction and analysis, Nat. Protoc., 10, 845, 10.1038/nprot.2015.053 Walls, 2020, Structure, function, and antigenicity of the SARS-CoV-2 spike glycoprotein, Cell, 181, 281, 10.1016/j.cell.2020.02.058 Isabel, 2020, Evolutionary and structural analyses of SARS-CoV-2 D614G spike protein mutation now documented worldwide, Sci. Rep., 10, 14031, 10.1038/s41598-020-70827-z Haddad, 2020, miRNA target prediction might explain the reduced transmission of SARS-CoV-2 in Jordan, Middle East, Non-coding RNA Res., 5, 135, 10.1016/j.ncrna.2020.08.002