scholarly journals Retargeting the Clostridium botulinum C2 toxin to the neuronal cytosol

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Benjamin J. Pavlik ◽  
Elizabeth J. Hruska ◽  
Kevin E. Van Cott ◽  
Paul H. Blum
Keyword(s):  
Clostridium Botulinum ◽  
Clostridium Botulinum C2 Toxin ◽  
C2 Toxin

Clostridium botulinum C2 toxin: binding studies with fluorescence-activated cytometry

Toxicon ◽  
2002 ◽  
Vol 40 (8) ◽  
pp. 1135-1140 ◽  
Author(s):  
Bradley G. Stiles ◽  
Dagmar Blöcker ◽  
Martha L. Hale ◽  
Mary Ann Guetthoff ◽  
Holger Barth
Keyword(s):  
Clostridium Botulinum ◽  
Binding Studies ◽  
Toxin Binding ◽  
Clostridium Botulinum C2 Toxin ◽  
C2 Toxin

Intracellular trafficking of Clostridium botulinum C2 toxin

Toxicon ◽  
2014 ◽  
Vol 82 ◽  
pp. 76-82 ◽  
Author(s):  
Masahiro Nagahama ◽  
Chihiro Takahashi ◽  
Kouhei Aoyanagi ◽  
Ryo Tashiro ◽  
Keiko Kobayashi ◽  
...  
Keyword(s):  
Intracellular Trafficking ◽  
Clostridium Botulinum ◽  
Clostridium Botulinum C2 Toxin ◽  
C2 Toxin

scholarly journals Binding and Internalization of Clostridium botulinum C2 Toxin

2009 ◽  
Vol 77 (11) ◽  
pp. 5139-5148 ◽  
Author(s):  
Masahiro Nagahama ◽  
Tohko Hagiyama ◽  
Takashi Kojima ◽  
Kouhei Aoyanagi ◽  
Chihiro Takahashi ◽  
...  
Keyword(s):  
Clostridium Botulinum ◽  
Mdck Cells ◽  
Binary Toxin ◽  
Akt Inhibitor ◽  
Surface Plasmon Resonance Analysis ◽  
Akt Phosphorylation ◽  
Resonance Analysis ◽  
Clostridium Botulinum C2 Toxin ◽  
C2 Toxin ◽  
Binding Component

ABSTRACT Clostridium botulinum C2 toxin is a binary toxin composed of an enzymatic component (C2I) and a binding component (C2II). The activated binding component (C2IIa) forms heptamers, and the oligomer with C2I is taken up by receptor-mediated endocytosis. We investigated the binding and internalization of C2IIa in cells. The C2IIa monomer formed oligomers on lipid rafts in membranes of MDCK cells. Methyl-beta-cyclodextrin inhibited the binding of C2IIa and the rounding of the cells induced by C2I plus C2IIa. C2I was localized to the rafts in the presence, but not the absence, of C2IIa. Surface plasmon resonance analysis revealed that C2I bound to the oligomer of C2IIa, but not the monomer of C2IIa. C2I and C2IIa were rapidly internalized in the cells. LY294002, a phosphatidylinositol 3-kinase (PI3K) inhibitor, inhibited the internalization of C2IIa in the cells and the rounding activity in the presence of C2I plus C2IIa. Incubation of the cells with C2I plus C2IIa resulted in the activation of PI3K and in phosphorylation of phosphoinositide-dependent kinase 1 and protein kinase B/Akt (Akt), but that with C2IIa alone did not. Akt inhibitor X, an Akt phosphorylation inhibitor, inhibited the rounding activity but not the internalization of C2IIa. The results suggest that the binding of C2I to the oligomer of C2IIa on rafts triggers the activation of the PI3K-Akt signaling pathway and, in turn, the initiation of endocytosis.

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