Use of nonthermal technologies in the production of functional beverages from vegetable ingredients to preserve heat‐labile phytochemicals

2017 ◽  
Vol 42 (2) ◽  
pp. e13506 ◽  
Author(s):  
J. Abraham Domínguez Avila ◽  
Abraham Wall Medrano ◽  
Cinthya A. Ruiz Pardo ◽  
Efigenia Montalvo González ◽  
Gustavo A. González Aguilar
Keyword(s):  
Heat Labile ◽  
Functional Beverages

Specificity of receptor-mediated signal transduction by E. coli type its heat-labile toxin

2001 ◽  
Vol 120 (5) ◽  
pp. A700-A700
Author(s):  
S WIMERMACKIN ◽  
R HOLMES ◽  
A WOLF ◽  
W LENCER ◽  
M JOBLING
Keyword(s):  
Signal Transduction ◽  
E Coli ◽  
Heat Labile

Construction of plasmids useful for production of the B subunit of cholera toxin fromVibrio cholerae or a heat-labile enterotoxin from enterotoxigenicEscherichia coli

1994 ◽  
Vol 10 (4) ◽  
pp. 393-398 ◽  
Author(s):  
Takao Tsuji ◽  
Michio Kato ◽  
Yutaka Kato ◽  
Hidetsugu Kawase ◽  
Seizi Imamura ◽  
...  
Keyword(s):  
Cholera Toxin ◽  
B Subunit ◽  
Heat Labile

scholarly journals A genetically detoxified derivative of heat-labile Escherichia coli enterotoxin induces neutralizing antibodies against the A subunit.

1994 ◽  
Vol 180 (6) ◽  
pp. 2147-2153 ◽  
Author(s):  
M Pizza ◽  
M R Fontana ◽  
M M Giuliani ◽  
M Domenighini ◽  
C Magagnoli ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Cholera Toxin ◽  
Neutralizing Antibodies ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
E Coli ◽  
Heat Labile ◽  
A Subunit ◽  
Adp Ribosyltransferase ◽  
Derivatives Of

Escherichia coli enterotoxin (LT) and the homologous cholera toxin (CT) are A-B toxins that cause travelers' diarrhea and cholera, respectively. So far, experimental live and killed vaccines against these diseases have been developed using only the nontoxic B portion of these toxins. The enzymatically active A subunit has not been used because it is responsible for the toxicity and it is reported to induce a negligible titer of toxin neutralizing antibodies. We used site-directed mutagenesis to inactivate the ADP-ribosyltransferase activity of the A subunit and obtained nontoxic derivatives of LT that elicited a good titer of neutralizing antibodies recognizing the A subunit. These LT mutants and equivalent mutants of CT may be used to improve live and killed vaccines against cholera and enterotoxinogenic E. coli.

Amplification of immune responses against a DNA-delivered idiotypic lymphoma antigen by fusion to the B subunit of E. coli heat labile toxin

Vaccine ◽  
2009 ◽  
Vol 27 (32) ◽  
pp. 4289-4296 ◽  
Author(s):  
Caleb G. Chen ◽  
Yen-Ta Lu ◽  
Marie Lin ◽  
Natalia Savelyeva ◽  
Freda K. Stevenson ◽  
...  
Keyword(s):  
Immune Responses ◽  
E Coli ◽  
B Subunit ◽  
Heat Labile

scholarly journals Assembly of the B subunit pentamer of Escherichia coli heat-labile enterotoxin. Kinetics and molecular basis of rate-limiting steps in vitro.

1996 ◽  
Vol 271 (43) ◽  
pp. 27188
Author(s):  
Lloyd W. Ruddock ◽  
Jeremy J.F. Coen ◽  
Caroline Cheesman ◽  
Robert B. Freedman ◽  
Timothy R. Hirst
Keyword(s):  
Escherichia Coli ◽  
Molecular Basis ◽  
B Subunit ◽  
Heat Labile ◽  
Rate Limiting

scholarly journals Crystal Structure of the B Subunit of Escherichia coli Heat-labile Enterotoxin Carrying Peptides with Anti-herpes Simplex Virus Type 1 Activity

1999 ◽  
Vol 274 (13) ◽  
pp. 8764-8769
Author(s):  
Dubravka Matković-Calogović ◽  
Arianna Loregian ◽  
Maria Rosa D'Acunto ◽  
Roberto Battistutta ◽  
Alessandro Tossi ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Escherichia Coli ◽  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
B Subunit ◽  
Heat Labile ◽  
Simplex Virus
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