Determination of the Complete Amino Acid Sequence of Recombinant Human γ-Interferon Produced in Escherichia coli

1986 ◽  
Vol 6 (4) ◽  
pp. 331-336 ◽  
Author(s):  
SHOJIRO YAMAZAKI ◽  
TSUNEO SHIMAZU ◽  
SHIGENOBU KIMURA ◽  
HIROHIKO SHIMIZU
1975 ◽  
Vol 356 (2) ◽  
pp. 1955-1976 ◽  
Author(s):  
Joël Vandekerckhove ◽  
Wilfried Rombauts ◽  
Ben Peeters ◽  
Brigitte Wittmann-Liebold

1985 ◽  
Vol 149 (2) ◽  
pp. 283-285
Author(s):  
Thomas Marti ◽  
Johann Schaller ◽  
Egon E. Rickli

1980 ◽  
Vol 1 (3) ◽  
pp. 248-264 ◽  
Author(s):  
HISATAKA KASAI ◽  
YUKIO KATO ◽  
TOSHIAKI ISOBE ◽  
HIROSHI KAWASAKI ◽  
TSUNEO OKUYAMA

FEBS Letters ◽  
1988 ◽  
Vol 240 (1-2) ◽  
pp. 127-132 ◽  
Author(s):  
André B.P. Van Kuilenburg ◽  
Anton O. Muijsers ◽  
Hans Demol ◽  
Henk L. Dekker ◽  
Jozef J. Van Beeumen

2019 ◽  
Vol 63 (12) ◽  
Author(s):  
Linda Mueller ◽  
Amandine Masseron ◽  
Guy Prod’Hom ◽  
Tatiana Galperine ◽  
Gilbert Greub ◽  
...  

ABSTRACT A novel KPC variant, KPC-41, was identified in a Klebsiella pneumoniae clinical isolate from Switzerland. This β-lactamase possessed a 3-amino-acid insertion (Pro-Asn-Lys) located between amino acids 269 and 270 compared to the KPC-3 amino acid sequence. Cloning and expression of the blaKPC-41 gene in Escherichia coli, followed by determination of MIC values and kinetic parameters, showed that KPC-41, compared to those of KPC-3, has an increased affinity to ceftazidime and a decreased sensitivity to avibactam, leading to resistance to ceftazidime-avibactam once produced in K. pneumoniae. Furthermore, KPC-41 exhibited a drastic decrease of its carbapenemase activity. This report highlights that a diversity of KPC variants conferring resistance to ceftazidime-avibactam already circulate in Europe.


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