Characterization of the multidrug efflux transporter styMdtM from Salmonella enterica serovar Typhi

2021 ◽  
Author(s):  
Aqsa Shaheen ◽  
Fouzia Ismat ◽  
Mazhar Iqbal ◽  
Abdul Haque ◽  
Zaheer Ul‐Haq ◽  
...  
Keyword(s):  
Salmonella Enterica ◽  
Efflux Transporter ◽  
Multidrug Efflux ◽  
Salmonella Enterica Serovar Typhi

scholarly journals Typhoid Fever due to Extended Spectrum β-Lactamase-Producing Salmonella enterica Serovar Typhi: A Case Report and Literature Review

2018 ◽  
Vol 2018 ◽  
pp. 1-5 ◽  
Author(s):  
Abdul Azeez Ahamed Riyaaz ◽  
Vindya Perera ◽  
Sabaratnam Sivakumaran ◽  
Nelun de Silva
Keyword(s):  
Case Report ◽  
Sri Lanka ◽  
Typhoid Fever ◽  
Salmonella Enterica ◽  
Salmonella Enterica Serovar Typhi ◽  
Extended Spectrum ◽  
Cephalosporin Resistance ◽  
Resistant Strains ◽  
Derivatives Of

Emergence of cephalosporin-resistant strains of Salmonella enterica serovar Typhi is a cause of concern in the management of enteric fever. Cephalosporin resistance in Salmonella species is mainly due to the production of extended-spectrum β-lactamases (ESBLs). The majority of ESBLs in Salmonella enterica serovar Typhi are derivatives of the TEM, SHV, and CTX-M β-lactamase families. Of these, CTX-M appears to be predominant. This paper discusses the detection and molecular characterization of an ESBL-producing Salmonella enterica serovar Typhi strain isolated from a patient who was admitted to a private hospital in Sri Lanka. The three main types of β-lactamases such as TEM, SHV, and CTX-M were identified in this isolate. This case report from Sri Lanka contributes to the knowledge of the increasingly reported cases of typhoid fever due to Salmonella enterica serovar Typhi resistant to β-lactamase by ESBL production.

Functional Characterization of the Heterooligomeric EbrAB Multidrug Efflux Transporter ofBacillus subtilis†

Biochemistry ◽  
2007 ◽  
Vol 46 (17) ◽  
pp. 5218-5225 ◽  
Author(s):  
Zhongge Zhang ◽  
Che Ma ◽  
Owen Pornillos ◽  
Xia Xiu ◽  
Geoffrey Chang ◽  
...  
Keyword(s):  
Functional Characterization ◽  
Efflux Transporter ◽  
Multidrug Efflux ◽  
Ofbacillus Subtilis

scholarly journals Genetic and Biochemical Characterization of Salmonella enterica Serovar Typhi Deoxyribokinase

2000 ◽  
Vol 182 (4) ◽  
pp. 869-873 ◽  
Author(s):  
Lise Tourneux ◽  
Nadia Bucurenci ◽  
Cosmin Saveanu ◽  
Pierre Alexandre Kaminski ◽  
Madeleine Bouzon ◽  
...  
Keyword(s):  
Salmonella Enterica ◽  
Biochemical Characterization ◽  
Site Directed Mutagenesis ◽  
Gene Encoding ◽  
E Coli ◽  
Salmonella Enterica Serovar Typhi ◽  
Acid Protein ◽  
Serovar Typhimurium ◽  
Amino Acid Protein

ABSTRACT We identified in the genome of Salmonella entericaserovar Typhi the gene encoding deoxyribokinase, deoK. Two other genes, vicinal to deoK, were determined to encode the putative deoxyribose transporter (deoP) and a repressor protein (deoQ). This locus, located between theuhpA and ilvN genes, is absent inEscherichia coli. The deoK gene inserted on a plasmid provides a selectable marker in E. coli for growth on deoxyribose-containing medium. Deoxyribokinase is a 306-amino-acid protein which exhibits about 35% identity with ribokinase from serovar Typhi, S. enterica serovar Typhimurium, or E. coli. The catalytic properties of the recombinant deoxyribokinase overproduced in E. colicorrespond to those previously described for the enzyme isolated from serovar Typhimurium. From a sequence comparison between serovar Typhi deoxyribokinase and E. coliribokinase, whose crystal structure was recently solved, we deduced that a key residue differentiating ribose and deoxyribose is Met10, which in ribokinase is replaced by Asn14. Replacement by site-directed mutagenesis of Met10 with Asn decreased theV max of deoxyribokinase by a factor of 2.5 and increased the K m for deoxyribose by a factor of 70, compared to the parent enzyme.

scholarly journals Characterization of the Multiple Transferable Resistance Repressor, MtrR, from Neisseria gonorrhoeae

2005 ◽  
Vol 187 (14) ◽  
pp. 5008-5012 ◽  
Author(s):  
Katherine M. Hoffmann ◽  
Daniel Williams ◽  
William M. Shafer ◽  
Richard G. Brennan
Keyword(s):  
Dna Binding ◽  
Neisseria Gonorrhoeae ◽  
Random Coil ◽  
Efflux Transporter ◽  
Multidrug Efflux ◽  
Sheet Structure ◽  
Β Sheet

ABSTRACT MtrR represses expression of the Neisseria gonorrhoeae mtrCDE multidrug efflux transporter genes. MtrR displays salt-dependent DNA binding, a stoichiometry of two dimers per DNA site, and, for a protein that was expected to be essentially all helical, a high percentage of random coil and possibly β-sheet structure.

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