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UID:914@biotech.technion.ac.il
DTSTART;TZID=Asia/Jerusalem:20200226T160000
DTEND;TZID=Asia/Jerusalem:20220202T164952
DTSTAMP:20220512T124721Z
URL:https://biotech.technion.ac.il/events/toward-hcv-vaccine-structural-st
 udies-of-hcv-e2-envelop-glycoprotein-that-facilitates-rational-design-of-h
 cv-vaccine-2/
SUMMARY:Toward HCV vaccine - Structural studies of HCV E2 envelop glycoprot
 ein that facilitates rational design of HCV vaccine
DESCRIPTION:A cross-genotype effective vaccine is obligated to achieve glob
 al elimination of hepatitis C virus (HCV). Recent studies underscore the i
 mportance of broadly neutralizing antibodies (bnAbs) in HCV clearance and 
 protection. Structural and functional studies of bnAbs in complexes with t
 heir antigen can provide critical information to guide prophylactic vaccin
 e design. For this purpose\, we determined the crystal structures of HCV E
 2 envelope glycoprotein in complex with a large panel of bnAbs. Structural
  analysis indicated that cross-neutralization of HCV by this group of bnAb
 s is mediated by their binding to highly conserved hydrophobic surface tha
 t overlaps with the CD81 receptor binding site. Structural based design of
  the E2 core fragment (E2c) resulted in improved antigens that demonstrate
  greater antigenicity and thermostability. Crystal structures of the optim
 ized E2c revealed how our designs stabilize E2 without altering key neutra
 lizing epitopes. Displaying of the optimized E2c on self-assembling nanopa
 rticles resulted in enhanced antigenicity and more effective elicitation o
 f nAbs response in mice immunization experiments\, assessing their potenti
 al as HCV vaccine candidates for eliciting a broadly neutralizing B-cell r
 esponse.
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