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UID:943@biology.technion.ac.il

DTSTART;TZID=Asia/Jerusalem:20210127T130000

DTEND;TZID=Asia/Jerusalem:20210127T140000

DTSTAMP:20210802T125903Z

URL:https://biology.technion.ac.il/en/seminars/phd-graduate-seminar-elena-
 matveev-2/

SUMMARY:PhD Graduate Seminar- Elena Matveev [No Categories]
DESCRIPTION:Location:   \n Affiliation: \n Host:\n Title:Structure-function
  analysis of EFF-1 mediated cell-cell fusion Cell-cellfusion is a univers
 al multi-step process essential for organogenesis and sexualreproduction. 
 EFF-1 protein and its paralog AFF-1 are necessary and sufficientfor fusion
  in the nematode Caenorhabditis elegans and in heterologoussystems. EFF-1 
 crystal structure showed that it is a homotrimer\, structurallysimilar to 
 viral class II fusion proteins (e.g. from Zika\, Semliki Forest andDengue 
 viruses). However\, the mechanisms of EFF-1 and AFF-1-mediated cell-cellfu
 sion remain elusive. Therefore\, to achieve better understanding of themec
 hanism of action\, the focus of my research was EFF-1 and AFF-1oligomeriza
 tion dynamics on the plasma membrane. My hypothesis was thattrimerization 
 is a step required for the fusogenic activity of the proteins. Totest this
  hypothesis\, I applied biochemical methods\, such as surfacebiotinylation
 \, and sucrose gradients as well as infections of AFF-1 andEFF-1-coated ps
 eudotyped viruses. I found that A. Wild type EFF-1 ismostly trimeric on th
 e surface of cells. B. The trimerization of EFF-1can be prevented in the p
 resence of two independent point mutations\, without areduction in protein
  activity. C. AFF-1 showed different oligomericstates on the plasma membra
 ne. Based on these results I suggest a new model inwhich the monomer\, and
  not the trimer\, constitutes the active form of theseeukaryotic fusogens.
  

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