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- W2411242518 abstract "Anthrax toxin is a three-protein virulence factor that utilizes transmembrane protein translocation as its mechanism to intoxicate cells during anthrax pathogenesis. The protective antigen (PA) assembles into a prepore state on the host cell surface. Upon endocytosis, acidic endosomal pH conditions drive PA to form a transmembrane channel, through which the lethal factor and edema factor are translocated into the host cytosol. Translocation is catalyzed by two key nonspecific polypeptide binding sites - the α-clamp and Φ-clamp. However, since the exact molecular mechanism of protein translocation has not been elucidated and electron microscopy structure revealed that the Φ clamp is narrow, we are testing the hypothesis that the clamp changes state to a more open state to accommodate large sterically bulky peptide sequences. A 10-residue, sterically bulky peptide, ‘KKKKKWWSWW’, was used to functionally probe polypeptide-clamp dynamics within wild-type (WT) and mutant PA channels. The peptide was synthesized with all L-stereoisomers (L-Trp), all D-stereoisomers (D-Trp) and alternating D- and L-stereoisomers (DL-Trp). Ensemble and single-channel assays were performed using planar lipid bilayer electrophysiology. Overall DL-Trp translocated less efficiently than D-Trp and L-Trp. In single-channel experiments, sub-conducting intermediates were observed for each peptide isomer. These intermediates were populated on pathway with the translocation process. A series of different intermediates was observed during an individual translocation event through the Φ-clamp mutant (F427A) channel. The absence of the bulky Phe residues in F427A mutant allows easier translocation of the peptides. Moreover, PA F427A rarely achieves a complete closed state, as seen from the incomplete blockade of conductance. This study shows that this model can thus be used as a system to determine the stereospecificities of the channels and can be used as to probe the dynamics of protein translocation." @default.
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- W2411242518 date "2016-02-01" @default.
- W2411242518 modified "2023-09-26" @default.
- W2411242518 title "Characterization of PA Channels in Anthrax Toxin using Trp Peptides" @default.
- W2411242518 doi "https://doi.org/10.1016/j.bpj.2015.11.2241" @default.
- W2411242518 hasPublicationYear "2016" @default.
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