HIGHLIGHTS
- who: Clostridium perfringens and collaborators from the (UNIVERSITY) have published the article: Cryo-EM structure of the octameric pore of Clostridium perfringens b -toxin, in the Journal: (JOURNAL)
- what: The authors show that CPB forms homo-octameric pores like the heterooligomeric pores of the bi-component leukocidins with important differences in the receptor binding region and the N-terminal latch domain. The authors propose that CPB together with the newly identified Epx toxins is a member a new subclass of the hemolysin-like family. The authors show that the b-barrel protrusion domain can be . . .
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