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10.1016/j.jsb.2021.107713 http://scihub22266oqcxt.onion/10.1016/j.jsb.2021.107713 33662570!7919542!33662570     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       J+Struct+Biol 2021 ; 213 (2): 107713 Nephropedia Template TP {{tp|p=33662570|t=2021. Spike protein fusion loop controls SARS-CoV-2 fusogenicity and infectivity |pdf=|usr=}}{{33662570}} gab.com Text Spike protein fusion loop controls SARS-CoV-2 fusogenicity and infectivity JO: J Struct Biol http://www.kidney.de/pget.php?&tw=1&pmid=33662570 #FOAvip The high SARS-CoV-2 reproductive number driving the COVID-19 pandemic has been a mystery. Our recent in vitro, and in vivo coronaviral pathogenesis studies involving Mouse Hepatitis Virus (MHV-A59) suggest a crucial role for a small host membrane-virus contact initiator region of the Spike protein, called the fusion peptide that enhances the virus fusogenicity and infectivity. Here I study the Spike from five human beta-coronaviruses (HCoV) including the SARS-CoV-2, and MHV-A59 for comparison. The structural and dynamics analyses of the Spike show that its fusion loop spatially organizes three fusion peptides contiguous to each other to synergistically trigger the virus-host membrane fusion process. I propose a Contact Initiation Model based on the architecture of the Spike quaternary structure that explains the obligatory participation of the fusion loop in the initiation of the host membrane contact for the virus fusion process. Among all the HCoV Spikes in this study, SARS-CoV-2 has the most hydrophobic surface and the extent of hydrophobicity correlates with the reproductive number and infectivity of the other HCoV. Comparison between results from standard and replica exchange molecular dynamics reveal the unique physicochemical properties of the SARS-CoV-2 fusion peptides, accrued in part from the presence of consecutive prolines that impart backbone rigidity which aids the virus fusogenicity. The priming of the Spike by its cleavage and subsequent fusogenic conformational transition steered by the fusion loop may be critical for the SARS-CoV-2 spread. The importance of the fusion loop makes it an apt target for anti-virals and vaccine candidates. Twit Text FOAVip Spike protein fusion loop controls SARS-CoV-2 fusogenicity and infectivity ????J Struct Biol http://www.kidney.de/pget.php?&tw=1&pmid=33662570 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33662570 #FOAvip English Wikipedia <ref>{{Cite pmid|33662570}}</ref> Spike protein fusion loop controls SARS-CoV-2 fusogenicity and infectivity #MMPMID33662570 Pal D J Struct Biol 2021[Jun]; 213 (2): 107713 PMID33662570show ga The high SARS-CoV-2 reproductive number driving the COVID-19 pandemic has been a mystery. Our recent in vitro, and in vivo coronaviral pathogenesis studies involving Mouse Hepatitis Virus (MHV-A59) suggest a crucial role for a small host membrane-virus contact initiator region of the Spike protein, called the fusion peptide that enhances the virus fusogenicity and infectivity. Here I study the Spike from five human beta-coronaviruses (HCoV) including the SARS-CoV-2, and MHV-A59 for comparison. The structural and dynamics analyses of the Spike show that its fusion loop spatially organizes three fusion peptides contiguous to each other to synergistically trigger the virus-host membrane fusion process. I propose a Contact Initiation Model based on the architecture of the Spike quaternary structure that explains the obligatory participation of the fusion loop in the initiation of the host membrane contact for the virus fusion process. Among all the HCoV Spikes in this study, SARS-CoV-2 has the most hydrophobic surface and the extent of hydrophobicity correlates with the reproductive number and infectivity of the other HCoV. Comparison between results from standard and replica exchange molecular dynamics reveal the unique physicochemical properties of the SARS-CoV-2 fusion peptides, accrued in part from the presence of consecutive prolines that impart backbone rigidity which aids the virus fusogenicity. The priming of the Spike by its cleavage and subsequent fusogenic conformational transition steered by the fusion loop may be critical for the SARS-CoV-2 spread. The importance of the fusion loop makes it an apt target for anti-virals and vaccine candidates. |*Protein Domains[MESH] |*Protein Structure, Secondary[MESH] |Amino Acid Sequence[MESH] |COVID-19/epidemiology/*prevention & control/virology[MESH] |Humans[MESH] |Models, Molecular[MESH] |Pandemics[MESH] |Peptides/*chemistry/genetics/metabolism[MESH] |SARS-CoV-2/genetics/*metabolism/physiology[MESH] |Sequence Homology, Amino Acid[MESH] |Spike Glycoprotein, Coronavirus/*chemistry/genetics/metabolism[MESH] |Static Electricity[MESH] |Viral Envelope Proteins/chemistry/genetics/metabolism[MESH]Spike protein fusion loop controls SARS-CoV-2 fusogenicity and infecti(epmc).pdf DeepDyve Pubget Overpricing