Inhibition of K88-mediated adhesion of Escherichia coli to mammalian receptors by antibiotics that affect bacterial protein synthesis

1986 ◽  
Vol 18 (4) ◽  
pp. 441-451 ◽  
Author(s):  
Ian Chopra ◽  
Keith Hacker
Keyword(s):  
Escherichia Coli ◽  
Protein Synthesis ◽  
Bacterial Protein ◽  
Bacterial Protein Synthesis

scholarly journals Histidine-Triad Hydrolases Provide Resistance to Peptide-Nucleotide Antibiotics

mBio ◽  
2020 ◽  
Vol 11 (2) ◽  
Author(s):  
Eldar Yagmurov ◽  
Darya Tsibulskaya ◽  
Alexey Livenskyi ◽  
Marina Serebryakova ◽  
Yury I. Wolf ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Protein Synthesis ◽  
Antibiotic Resistance ◽  
Potent Inhibitor ◽  
Trna Synthetase ◽  
Bacterial Protein ◽  
Mechanisms Of Resistance ◽  
Content Type ◽  
Bacterial Protein Synthesis ◽  
Related Compounds

ABSTRACT The Escherichia coli microcin C (McC) and related compounds are potent Trojan horse peptide-nucleotide antibiotics. The peptide part facilitates transport into sensitive cells. Inside the cell, the peptide part is degraded by nonspecific peptidases releasing an aspartamide-adenylate containing a phosphoramide bond. This nonhydrolyzable compound inhibits aspartyl-tRNA synthetase. In addition to the efficient export of McC outside the producing cells, special mechanisms have evolved to avoid self-toxicity caused by the degradation of the peptide part inside the producers. Here, we report that histidine-triad (HIT) hydrolases encoded in biosynthetic clusters of some McC homologs or by standalone genes confer resistance to McC-like compounds by hydrolyzing the phosphoramide bond in toxic aspartamide-adenosine, rendering them inactive. IMPORTANCE Uncovering the mechanisms of resistance is a required step for countering the looming antibiotic resistance crisis. In this communication, we show how universally conserved histidine-triad hydrolases provide resistance to microcin C, a potent inhibitor of bacterial protein synthesis.

scholarly journals Histidine-Triad Hydrolases Provide Resistance to Peptide-Nucleotide Antibiotics

2020 ◽  
Author(s):  
Eldar Yagmurov ◽  
Darya Tsibulskaya ◽  
Alexey Livenskyi ◽  
Marina Serebryakova ◽  
Yury I. Wolf ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Protein Synthesis ◽  
Antibiotic Resistance ◽  
Potent Inhibitor ◽  
Trna Synthetase ◽  
Trojan Horse ◽  
Bacterial Protein ◽  
Mechanisms Of Resistance ◽  
Bacterial Protein Synthesis ◽  
Related Compounds

ABSTRACTThe Escherichia coli microcin C (McC) and related compounds are potent Trojan-horse peptide-nucleotide antibiotics. The peptide part facilitates transport into sensitive cells. Inside the cell, the peptide part is degraded by non-specific peptidases releasing an aspartamide-adenylate containing a phosphoramide bond. This non-hydrolyzable compound inhibits aspartyl-tRNA synthetase. In addition to the efficient export of McC outside of the producing cells, special mechanisms evolved to avoid self-toxicity caused by the degradation of the peptide part inside the producers. Here, we report that histidine triad (HIT) hydrolases encoded in biosynthetic clusters of some McC homologs or by stand-alone genes confer resistance to McC–like compounds by hydrolyzing the phosphoramide bond in toxic aspartamide-adenosine, rendering them inactive.IMPORTANCEUncovering the mechanisms of resistance is a required step for countering the looming antibiotic resistance crisis. In this communication, we show how universally conserved histidine triad hydrolases provide resistance to microcin C – a potent inhibitor of bacterial protein synthesis.

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