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SUMMARY:Bigger Picture Talks at CEB with Professor Susan Daniel: Regulatio
 n of the coronavirus fusion peptide interaction with the host membrane and
  its impact on viral infectivity - Professor Susan Daniel\, Cornell Univer
 sity
DTSTART:20220420T150000Z
DTEND:20220420T160000Z
UID:TALK172310@talks.cam.ac.uk
CONTACT:Communications\, CEB
DESCRIPTION:Our departmental seminar series\, Bigger Picture Talks\, runs 
 throughout the academic year\, inviting thought-leaders from across the wo
 rld driving significant advances in our impact areas of energy\, health an
 d sustainability to share and discuss their work with us. This is a fantas
 tic opportunity for us to hear from other leading researchers\, develop ne
 w connections and collaborations\, and discuss some of the wider questions
  in our field. We hope they will inspire new ideas for us all to take into
  our own research.\n\nWe are running this event in a hybrid format. To *re
 gister to attend in person*\, please "register through Eventbrite":https:/
 /www.eventbrite.co.uk/e/bigger-picture-talks-at-ceb-professor-susan-daniel
 -tickets-311653432807\n\nTo *register to attend online*\, please register 
 via our "Zoom webinar registration page":https://ceb-cam-ac-uk.zoom.us/web
 inar/register/WN_k-VUt2SgSoOdT1VUk5pQGQ\n\nProfessor Susan Daniel\, Fred H
 . Rhodes Professor at Cornell University presents her work exploring the r
 eplication cycle of the SARS-CoV-2 virus.\n\n*Abstract*\n\nThe coronavirus
  disease 2019 (COVID-19) necessitates develop of effective therapies again
 st the causative agent\, SARS-CoV-2\, and other pathogenic coronaviruses (
 CoV) that have yet to emerge. Focusing on the CoV replication cycle\, spec
 ifically the entry steps involving membrane fusion\, is an astute choice b
 ecause of the conservation of the fusion machinery and mechanism across th
 e CoV family. For coronavirus\, entry into a host cell is mediated by a si
 ngle glycoprotein protruding from its membrane envelope\, called spike (S)
 . Within S\, the region that directly interacts with the membrane is calle
 d the fusion peptide\, FP. It is the physico-chemical interactions of the 
 FP with the host membrane that anchors it\, enabling the necessary deforma
 tions of the membrane leading to delivery of the viral genome into the cel
 l when a fusion pore opens. Thermodynamic\, kinetic\, and intermolecular i
 nteractions are useful to understand molecular level FP interactions with 
 the host membrane. This knowledge can be leveraged to stop the spread of i
 nfection. Here\, we examine the impact of calcium ions on CoV entry. Using
  cell infectivity\, biophysical assays\, and spectroscopic methods\, we fo
 und that calcium ions stabilize the FP structure during conformational cha
 nge that then allows its insertion into the host membrane\, resulting in i
 ncreased lipid ordering in the membrane. This lipid ordering precedes memb
 rane fusion and correlates with increased fusion activity and higher level
 s of infection when calcium in present. As such\, depletion of calcium ion
 s leads to structure and activity changes in the fusion peptide that corre
 late well with in vitro experiments using calcium-chelating agents to bloc
 k cell infection. In a final set of experiments\, we show calcium channel 
 blockers can block virus infection in lung cells.
LOCATION:Department of Chemical Engineering and Biotechnology\, West Cambr
 idge Site\, LT1\; and online
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