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10.1016/j.bbrep.2020.100896 http://scihub22266oqcxt.onion/10.1016/j.bbrep.2020.100896 33506114!7815659!33506114     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Biochem+Biophys+Rep 2021 ; 25 (ä): 100896 Nephropedia Template TP {{tp|p=33506114|t=2021. Mutational sensitivity of D614G in spike protein of SARS-CoV-2 in Jordan |pdf=|usr=}}{{33506114}} gab.com Text Mutational sensitivity of D614G in spike protein of SARS-CoV-2 in Jordan JO: Biochem Biophys Rep http://www.kidney.de/pget.php?&tw=1&pmid=33506114 #FOAvip BACKGROUND: Spike protein is the surface glycoprotein of the severe acute respiratory syndrome-coronavirus-2 (SARS-CoV-2) necessary for the entry of the virus via the transmembrane receptors of the human respiratory cells causing COVID-19 disease. AIM: Here, we aimed to predict the three-dimensional monomer structure of spike protein of SARS-CoV-2 from 20 Jordanian nasopharyngeal samples and to determine the percentage of single amino acid variants (SAV) in the spike protein of SARS-CoV-2. METHODS: The output of the Protein Homology/analogY Recognition Engine V 2.0 (Phyre2) found four single amino acid variants in the spike gene. RESULTS: The first variant represented by 5% of samples that showed tyrosine deletion at Y144 located in the N terminal domain. The second and the dominant variant, represented by 62%, showed aspartate a coil amino acid substitution to glycine an extracellular amino acid at D614G located in the spike recognition binding site. The third variant, represented by 5%, showed aspartate substitution to tyrosine at D1139Y, and the fourth variant, represented by 5% glycine substitution to serine at G1167S. CONCLUSION: Our results have shown low mutational sensitivity in all variants except to D614G the one with the most likely neutral mutational sensitivity that all variants might not explicitly affect the function of spike glycoprotein. However, D614G might change the viral conformational plasticity and hence a potential viral fitness gain but one must be cautious about drawing any concrete conclusions about the severity of symptoms and viral transmission from genomic data only. GENERAL SIGNIFICANCE: Studying mutations such as D614G in deep is essential to control the pandemic in terms of immune systems, antibodies, or even vaccines. Twit Text FOAVip Mutational sensitivity of D614G in spike protein of SARS-CoV-2 in Jordan ????Biochem Biophys Rep http://www.kidney.de/pget.php?&tw=1&pmid=33506114 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33506114 #FOAvip English Wikipedia <ref>{{Cite pmid|33506114}}</ref> Mutational sensitivity of D614G in spike protein of SARS-CoV-2 in Jordan #MMPMID33506114 Al-Zyoud W; Haddad H Biochem Biophys Rep 2021[Mar]; 25 (ä): 100896 PMID33506114show ga BACKGROUND: Spike protein is the surface glycoprotein of the severe acute respiratory syndrome-coronavirus-2 (SARS-CoV-2) necessary for the entry of the virus via the transmembrane receptors of the human respiratory cells causing COVID-19 disease. AIM: Here, we aimed to predict the three-dimensional monomer structure of spike protein of SARS-CoV-2 from 20 Jordanian nasopharyngeal samples and to determine the percentage of single amino acid variants (SAV) in the spike protein of SARS-CoV-2. METHODS: The output of the Protein Homology/analogY Recognition Engine V 2.0 (Phyre2) found four single amino acid variants in the spike gene. RESULTS: The first variant represented by 5% of samples that showed tyrosine deletion at Y144 located in the N terminal domain. The second and the dominant variant, represented by 62%, showed aspartate a coil amino acid substitution to glycine an extracellular amino acid at D614G located in the spike recognition binding site. The third variant, represented by 5%, showed aspartate substitution to tyrosine at D1139Y, and the fourth variant, represented by 5% glycine substitution to serine at G1167S. CONCLUSION: Our results have shown low mutational sensitivity in all variants except to D614G the one with the most likely neutral mutational sensitivity that all variants might not explicitly affect the function of spike glycoprotein. However, D614G might change the viral conformational plasticity and hence a potential viral fitness gain but one must be cautious about drawing any concrete conclusions about the severity of symptoms and viral transmission from genomic data only. GENERAL SIGNIFICANCE: Studying mutations such as D614G in deep is essential to control the pandemic in terms of immune systems, antibodies, or even vaccines. äMutational sensitivity of D614G in spike protein of SARS-CoV-2 in Jord(epmc).pdf DeepDyve Pubget Overpricing