Anthrax toxin-mediated delivery of cholera toxin-A subunit into the cytosol of mammalian cells

2000 ◽  
Vol 32 (1) ◽  
pp. 69 ◽  
Author(s):  
Manju Sharma ◽  
Hemant Khanna ◽  
Naveen Arora ◽  
Yogendra Singh
Keyword(s):  
Cholera Toxin ◽  
Mammalian Cells ◽  
Anthrax Toxin ◽  
Toxin A ◽  
A Subunit

scholarly journals Expression and mutagenesis of recombinant cholera toxin A subunit

1994 ◽  
Vol 17 (5) ◽  
pp. 339-346 ◽  
Author(s):  
Kirsten L. Vadheim ◽  
Yogendra Singh ◽  
Jerry M. Keith
Keyword(s):  
Cholera Toxin ◽  
Toxin A ◽  
A Subunit

Intracellular Signal Triggered by Cholera Toxin inSaccharomyces boulardii and Saccharomyces cerevisiae

1998 ◽  
Vol 64 (2) ◽  
pp. 564-568 ◽  
Author(s):  
Rogelio L. Brandão ◽  
Ieso M. Castro ◽  
Eduardo A. Bambirra ◽  
Sheila C. Amaral ◽  
Luciano G. Fietto ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cholera Toxin ◽  
Mammalian Cells ◽  
Specific Binding ◽  
Saccharomyces Boulardii ◽  
Yeast Cells ◽  
B Subunit ◽  
Nonfermentable Carbon Source ◽  
A Subunit ◽  
Yeast Surface

ABSTRACT As is the case for Saccharomyces boulardii, Saccharomyces cerevisiae W303 protects Fisher rats against cholera toxin (CT). The addition of glucose or dinitrophenol to cells of S. boulardii grown on a nonfermentable carbon source activated trehalase in a manner similar to that observed for S. cerevisiae. The addition of CT to the same cells also resulted in trehalase activation. Experiments performed separately on the A and B subunits of CT showed that both are necessary for activation. Similarly, the addition of CT but not of its separate subunits led to a cyclic AMP (cAMP) signal in both S. boulardii and S. cerevisiae. These data suggest that trehalase stimulation by CT probably occurred through the cAMP-mediated protein phosphorylation cascade. The requirement of CT subunit B for both the cAMP signal and trehalase activation indicates the presence of a specific receptor on the yeasts able to bind to the toxin, a situation similar to that observed for mammalian cells. This hypothesis was reinforced by experiments with 125I-labeled CT showing specific binding of the toxin to yeast cells. The adhesion of CT to a receptor on the yeast surface through the B subunit and internalization of the A subunit (necessary for the cAMP signal and trehalase activation) could be one more mechanism explaining protection against the toxin observed for rats treated with yeasts.

scholarly journals Sleep-inducing effect of substance P-cholera toxin A subunit in mice

2017 ◽  
Vol 659 ◽  
pp. 44-47 ◽  
Author(s):  
Mark R. Zielinski ◽  
Dmitry Gerashchenko
Keyword(s):  
Substance P ◽  
Cholera Toxin ◽  
Toxin A ◽  
A Subunit

scholarly journals Engineering of cholera toxin A-subunit for carriage of epitopes at its amino end

FEBS Letters ◽  
1997 ◽  
Vol 401 (1) ◽  
pp. 95-97 ◽  
Author(s):  
J Sanchez ◽  
R Argotte ◽  
A Buelna
Keyword(s):  
Cholera Toxin ◽  
Toxin A ◽  
A Subunit

scholarly journals KDEL Receptor (Erd2p)-mediated Retrograde Transport of the Cholera Toxin A Subunit from the Golgi Involves COPI, p23, and the COOH Terminus of Erd2p

1998 ◽  
Vol 143 (3) ◽  
pp. 601-612 ◽  
Author(s):  
Irina Majoul ◽  
Kai Sohn ◽  
Felix Theodor Wieland ◽  
Rainer Pepperkok ◽  
Mariagrazia Pizza ◽  
...  
Keyword(s):  
Coat Protein ◽  
Cholera Toxin ◽  
Retrograde Transport ◽  
Vero Cells ◽  
Toxin A ◽  
P24 Protein ◽  
A Subunit ◽  
Intermediate Compartment ◽  
Camp Levels ◽  
Kdel Receptor

A cholera toxin mutant (CTX–K63) unable to raise cAMP levels was used to study in Vero cells the retrograde transport of the toxin A subunit (CTX-A–K63), which possesses a COOH-terminal KDEL retrieval signal. Microinjected GTP-γ-S inhibits the internalization as well as Golgi–ER transport of CTX-A–K63. The appearance of CTX-A–K63 in the Golgi induces a marked dispersion of Erd2p and p53 but not of the Golgi marker giantin. Erd2p is translocated under these conditions most likely to the intermediate compartment as indicated by an increased colocalization of Erd2p with mSEC13, a member of the mammalian coat protein II complex. IgGs as well as Fab fragments directed against Erd2p, β-COP, or p23, a new member of the p24 protein family, inhibit or block retrograde transport of CTX-A–K63 from the Golgi without affecting its internalization or its transport to the Golgi. Anti-Erd2p antibodies do not affect the binding of CTX-A to Erd2p, but inhibit the CTX-K63–induced translocation of Erd2p and p53.

scholarly journals Nasally administered cholera toxin A-subunit acts as a mucosal adjuvant

2003 ◽  
Vol 45 (1) ◽  
pp. 25-31 ◽  
Author(s):  
Emilio A. Campos ◽  
Jun Namikoshi ◽  
Satomi Maeba ◽  
Masafumi Yamamoto ◽  
Masahiko Fukumoto ◽  
...  
Keyword(s):  
Cholera Toxin ◽  
Toxin A ◽  
Mucosal Adjuvant ◽  
A Subunit
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