BEGIN:VCALENDAR VERSION:2.0 METHOD:PUBLISH PRODID:-//Missouri State University/Calendar of Events//EN CALSCALE:GREGORIAN X-WR-TIMEZONE:America/Chicago BEGIN:VTIMEZONE TZID:America/Chicago BEGIN:DAYLIGHT TZOFFSETFROM:-0600 TZOFFSETTO:-0500 DTSTART:20070311T020000 RRULE:FREQ=YEARLY;BYMONTH=3;BYDAY=2SU TZNAME:CDT END:DAYLIGHT BEGIN:STANDARD TZOFFSETFROM:-0500 TZOFFSETTO:-0600 DTSTART:20071104T020000 RRULE:FREQ=YEARLY;BYMONTH=11;BYDAY=1SU TZNAME:CST END:STANDARD END:VTIMEZONE BEGIN:VEVENT UID:5bcfa835-35e9-41ab-b084-1dbc21038e97.213150@calendar.missouristate.edu CREATED:20210119T175756Z LAST-MODIFIED:20210119T175756Z LOCATION: SUMMARY:PAMS Seminar: "Virus-Receptor Interactions of Glycosylated SARS-Co V-2 Spike and Human ACE2 Receptor" by Dr. Oliver Grant DESCRIPTION:Dr. Oliver Grant\n\n\nComplex Carbohydrate Research CenterUniv ersity of Georgia\n\n\nNote: This seminar is at noon (brown bag seminar)! \n\n\nAbstract:Cellular infection by the 2019 severe acute respiratory sy ndrome coronavirus (SARS-CoV-2) is initiated by binding of the viral spik e glycoprotein (S) to its receptor\, the angiotensin-converting enzyme 2 (ACE2)\, which is present on the cellular membrane of human tissues and o rgans including the lung\, intestine and kidney. The SARS-CoV-2 S trimer contains 66 N-linked glycosylation sites\, which have been implicated in immune evasion and modulating receptor binding affinity. All sites are oc cupied by glycans when the spike protein is produced recombinantly in HEK -293 cells\, or isolated from virus-derived trimers\, or from trimers der ived from a viral vectored SARS-CoV-2 vaccine candidate. The human ACE2 ( hACE2) receptor contains 6 potential N-linked glycosylation sites that we re also found to be occupied under equivalent expression conditions. Rece ntly\, we combined a glycoproteomic analysis of the S glycoprotein and hA CE2 with molecular dynamics (MD) simulations to generate 3D models of gly cosylated hACE2 bound to the S glycoprotein trimer. An analysis of the MD simulations of these 3D structures led to the prediction that ACE2 glyca ns directly with the S glycoprotein. Thus differences in the occupancy or composition of glycans at these positions may modulate the strength of t he S protein - ACE2 interaction\, which may in turn impact infectivity\, disease severity and transmissibility.\n\n\n     Our results highlight ro les for glycans in sterically masking polypeptide epitopes and directly m odulating Spike-ACE2 interactions. Furthermore\, our results illustrate t he impact of viral evolution and divergence on Spike glycosylation\, as w ell as the influence of natural variants on ACE2 receptor glycosylation t hat\, taken together\, can facilitate immunogen design to achieve antibod y neutralization and inform therapeutic strategies to inhibit viral infec tion.\n\n\nThis seminar will be held exclusively on Zoom (955 5209 1021). Please visit the Physics Seminars page for a link. X-ALT-DESC;FMTTYPE=text/html:<html><head><title></title></head><body><p>Dr . Oliver Grant</p>\n<p>Complex Carbohydrate Research Center<br>University of Georgia</p>\n<p><strong>Note: This seminar is at noon (brown bag semi nar)!</strong></p>\n<p>Abstract:<br>Cellular infection by the 2019 severe acute respiratory syndrome coronavirus (SARS-CoV-2) is initiated by bind ing of the viral spike glycoprotein (S) to its receptor\, the angiotensin -converting enzyme 2 (ACE2)\, which is present on the cellular membrane o f human tissues and organs including the lung\, intestine and kidney. The SARS-CoV-2 S trimer contains 66 N-linked glycosylation sites\, which hav e been implicated in immune evasion and modulating receptor binding affin ity. All sites are occupied by glycans when the spike protein is produced recombinantly in HEK-293 cells\, or isolated from virus-derived trimers\ , or from trimers derived from a viral vectored SARS-CoV-2 vaccine candid ate. The human ACE2 (hACE2) receptor contains 6 potential N-linked glycos ylation sites that were also found to be occupied under equivalent expres sion conditions. Recently\, we combined a glycoproteomic analysis of the S glycoprotein and hACE2 with molecular dynamics (MD) simulations to gene rate 3D models of glycosylated hACE2 bound to the S glycoprotein trimer. An analysis of the MD simulations of these 3D structures led to the predi ction that ACE2 glycans directly with the S glycoprotein. Thus difference s in the occupancy or composition of glycans at these positions may modul ate the strength of the S protein - ACE2 interaction\, which may in turn impact infectivity\, disease severity and transmissibility.</p>\n<p>&nbsp \; &nbsp\; &nbsp\;Our results highlight roles for glycans in sterically m asking polypeptide epitopes and directly modulating Spike-ACE2 interactio ns. Furthermore\, our results illustrate the impact of viral evolution an d divergence on Spike glycosylation\, as well as the influence of natural variants on ACE2 receptor glycosylation that\, taken together\, can faci litate immunogen design to achieve antibody neutralization and inform the rapeutic strategies to inhibit viral infection.</p>\n<p>This seminar will be held exclusively on Zoom (955 5209 1021). Please visit the&nbsp\;<a h ref="https://physics.missouristate.edu/seminars.htm">Physics Seminars pag e</a> for a link.</p></body></html> DTSTART;TZID=America/Chicago:20210211T120000 DTEND;TZID=America/Chicago:20210211T130000 SEQUENCE:0 URL:https://physics.missouristate.edu/seminars.htm CATEGORIES:Public,Alumni,Current Students,Faculty,Future Students,Staff END:VEVENT END:VCALENDAR