Site-directed mutagenesis and function analysis of glgC gene from Escherichia coli

2008 ◽  
Vol 30 (10) ◽  
pp. 1372-1378
Author(s):  
Shuang ZHOU
Keyword(s):  
Escherichia Coli ◽  
Function Analysis ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
And Function

scholarly journals Structure and function analysis of Polygonatum cyrtonema lectin by site-directed mutagenesis

2017 ◽  
Vol 49 (12) ◽  
pp. 1099-1111 ◽  
Author(s):  
Yuyu Chen ◽  
Kaimin Lu ◽  
Jianzong Li ◽  
Danfeng Liang ◽  
Hao luo ◽  
...  
Keyword(s):  
Function Analysis ◽  
Structure And Function ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
And Function

scholarly journals Primary Structure and Function Analysis of theAbrus precatoriusAgglutinin A Chain by Site-directed Mutagenesis

2000 ◽  
Vol 275 (3) ◽  
pp. 1897-1901 ◽  
Author(s):  
Chao-Lin Liu ◽  
Chia-Chu Tsai ◽  
Su-Chang Lin ◽  
Li-In Wang ◽  
Chong-Ing Hsu ◽  
...  
Keyword(s):  
Primary Structure ◽  
Function Analysis ◽  
Structure And Function ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
A Chain ◽  
And Function

scholarly journals Overexpression, site-directed mutagenesis, and mechanism of Escherichia coli acid phosphatase

1992 ◽  
Vol 267 (32) ◽  
pp. 22830-22836 ◽  
Author(s):  
K Ostanin ◽  
E.H. Harms ◽  
P.E. Stevis ◽  
R Kuciel ◽  
M.M. Zhou ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Acid Phosphatase ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis

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.

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