Pore-forming protein toxins: from structure to function

Enhanced SnapShot: Pore-Forming Toxins

Structure and Function of Pore-Forming b-Barrels from Bacteria

Crystallographic studies of the past ten years have revealed that many outer membrane proteins and bacterial toxins are constructed on the b-barrel motif. Two structural classes can be identified. The first class, represented by the porins, includes monomeric or multimeric proteins where each b-barrel is formed from a single polypeptide. The second class features proteins where the b-barrel is ...

Structure and function of pore-forming beta-barrels from bacteria.

Crystallographic studies of the past ten years have revealed that many outer membrane proteins and bacterial toxins are constructed on the beta-barrel motif. Two structural classes can be identified. The first class, represented by the porins, includes monomeric or multimeric proteins where each beta-barrel is formed from a single polypeptide. The second class features proteins where the beta-b...

Global Functional Analyses of Cellular Responses to Pore-Forming Toxins

Here we present the first global functional analysis of cellular responses to pore-forming toxins (PFTs). PFTs are uniquely important bacterial virulence factors, comprising the single largest class of bacterial protein toxins and being important for the pathogenesis in humans of many Gram positive and Gram negative bacteria. Their mode of action is deceptively simple, poking holes in the plasm...

1678 Pore - Forming Protein from E

Entamoeba histolytica, an enter ic h u m a n paras i te , produces extensive tissue des t ruc t ion in the course of the infection. Pr ior studies from this l abo ra to ry have discussed the isolation o f the p l a sma m e m b r a n e of this paras i te and charac te r ized cer ta in o f its intr insic po lypept ides and externa l ly disposed ant igens (1, 2). More recent interests have focused...