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10.1371/journal.pcbi.1008790 http://scihub22266oqcxt.onion/10.1371/journal.pcbi.1008790 33793546!8016105!33793546     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=33793546&cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\33793546.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       PLoS+Comput+Biol 2021 ; 17 (4): e1008790 Nephropedia Template TP {{tp|p=33793546|t=2021. Computational epitope map of SARS-CoV-2 spike protein |pdf=|usr=}}{{33793546}} gab.com Text Computational epitope map of SARS-CoV-2 spike protein JO: PLoS Comput Biol http://www.kidney.de/pget.php?&tw=1&pmid=33793546 #FOAvip The primary immunological target of COVID-19 vaccines is the SARS-CoV-2 spike (S) protein. S is exposed on the viral surface and mediates viral entry into the host cell. To identify possible antibody binding sites, we performed multi-microsecond molecular dynamics simulations of a 4.1 million atom system containing a patch of viral membrane with four full-length, fully glycosylated and palmitoylated S proteins. By mapping steric accessibility, structural rigidity, sequence conservation, and generic antibody binding signatures, we recover known epitopes on S and reveal promising epitope candidates for structure-based vaccine design. We find that the extensive and inherently flexible glycan coat shields a surface area larger than expected from static structures, highlighting the importance of structural dynamics. The protective glycan shield and the high flexibility of its hinges give the stalk overall low epitope scores. Our computational epitope-mapping procedure is general and should thus prove useful for other viral envelope proteins whose structures have been characterized. Twit Text FOAVip Computational epitope map of SARS-CoV-2 spike protein ????PLoS Comput Biol http://www.kidney.de/pget.php?&tw=1&pmid=33793546 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33793546 #FOAvip English Wikipedia <ref>{{Cite pmid|33793546}}</ref> Computational epitope map of SARS-CoV-2 spike protein #MMPMID33793546 Sikora M; von Bulow S; Blanc FEC; Gecht M; Covino R; Hummer G PLoS Comput Biol 2021[Apr]; 17 (4): e1008790 PMID33793546show ga The primary immunological target of COVID-19 vaccines is the SARS-CoV-2 spike (S) protein. S is exposed on the viral surface and mediates viral entry into the host cell. To identify possible antibody binding sites, we performed multi-microsecond molecular dynamics simulations of a 4.1 million atom system containing a patch of viral membrane with four full-length, fully glycosylated and palmitoylated S proteins. By mapping steric accessibility, structural rigidity, sequence conservation, and generic antibody binding signatures, we recover known epitopes on S and reveal promising epitope candidates for structure-based vaccine design. We find that the extensive and inherently flexible glycan coat shields a surface area larger than expected from static structures, highlighting the importance of structural dynamics. The protective glycan shield and the high flexibility of its hinges give the stalk overall low epitope scores. Our computational epitope-mapping procedure is general and should thus prove useful for other viral envelope proteins whose structures have been characterized. |*Computational Biology[MESH] |Binding Sites, Antibody[MESH] |COVID-19 Vaccines/immunology[MESH] |COVID-19/virology[MESH] |Epitope Mapping/*methods[MESH] |Epitopes/*chemistry/immunology[MESH] |Immunogenicity, Vaccine[MESH] |Protein Conformation[MESH]Computational epitope map of SARS-CoV-2 spike protein (epmc).pdf DeepDyve Pubget Overpricing