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10.1002/bit.26029 http://scihub22266oqcxt.onion/10.1002/bit.26029 C5367918!5367918 !27260850     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=27260850 &cmd=llinks): Failed to open stream: HTTP request failed! 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Newly identified bacteriolytic enzymes that target a wide range of clinical isolates of Clostridium difficile |pdf=|usr=}}{{27260850 }} gab.com Text Newly identified bacteriolytic enzymes that target a wide range of clinical isolates of Clostridium difficile JO: Biotechnol Bioeng http://www.kidney.de/pget.php?&tw=1&pmid=27260850 #FOAvip Clostridium difficile has emerged as a major cause of infectious diarrhea in hospitalized patients, with increasing mortality rate and annual healthcare costs exceeding $3 billion. Since C. difficile infections are associated with the use of antibiotics, there is an urgent need to develop treatments that can inactivate the bacterium selectively without affecting commensal microflora. Lytic enzymes from bacteria and bacteriophages show promise as highly selective and effective antimicrobial agents. These enzymes often have a modular structure, consisting of a catalytic domain and a binding domain. In the current work, using consensus catalytic domain and cell-wall binding domain sequences as probes, we analyzed in silico the genome of C. difficile, as well as phages infecting C. difficile. We identified two genes encoding cell lytic enzymes with possible activity against C. difficile. We cloned the genes in a suitable expression vector, expressed and purified the protein products, and tested enzyme activity in vitro. These newly identified enzymes were found to be active against C. difficile cells in a dose-dependent manner. We achieved a more than 4-log reduction in the number of viable bacteria within 5?h of application. Moreover, we found that the enzymes were active against a wide range of C. difficile clinical isolates. We also characterized the biocatalytic mechanism by identifying the specific bonds cleaved by these enzymes within the cell wall peptidoglycan. These results suggest a new approach to combating the growing healthcare problem associated with C. difficile infections. Biotechnol. Bioeng. 2016;113: 2568-2576. © 2016 Wiley Periodicals, Inc. Twit Text FOAVip Newly identified bacteriolytic enzymes that target a wide range of clinical isolates of Clostridium difficile ????Biotechnol Bioeng http://www.kidney.de/pget.php?&tw=1&pmid=27260850 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27260850 #FOAvip English Wikipedia <ref>{{Cite pmid|27260850 }}</ref> Newly identified bacteriolytic enzymes that target a wide range of clinical isolates of Clostridium difficile #MMPMID27260850 Mehta KK ; Paskaleva EE ; Wu X ; Grover N ; Mundra RV ; Chen K ; Zhang Y ; Yang Z ; Feng H ; Dordick JS ; Kane RS Biotechnol Bioeng 2016[Dec]; 113 (12 ): 2568-2576 PMID27260850 show ga Clostridium difficile has emerged as a major cause of infectious diarrhea in hospitalized patients, with increasing mortality rate and annual healthcare costs exceeding $3 billion. Since C. difficile infections are associated with the use of antibiotics, there is an urgent need to develop treatments that can inactivate the bacterium selectively without affecting commensal microflora. Lytic enzymes from bacteria and bacteriophages show promise as highly selective and effective antimicrobial agents. These enzymes often have a modular structure, consisting of a catalytic domain and a binding domain. In the current work, using consensus catalytic domain and cell-wall binding domain sequences as probes, we analyzed in silico the genome of C. difficile, as well as phages infecting C. difficile. We identified two genes encoding cell lytic enzymes with possible activity against C. difficile. We cloned the genes in a suitable expression vector, expressed and purified the protein products, and tested enzyme activity in vitro. These newly identified enzymes were found to be active against C. difficile cells in a dose-dependent manner. We achieved a more than 4-log reduction in the number of viable bacteria within 5?h of application. Moreover, we found that the enzymes were active against a wide range of C. difficile clinical isolates. We also characterized the biocatalytic mechanism by identifying the specific bonds cleaved by these enzymes within the cell wall peptidoglycan. These results suggest a new approach to combating the growing healthcare problem associated with C. difficile infections. Biotechnol. Bioeng. 2016;113: 2568-2576. © 2016 Wiley Periodicals, Inc. |Anti-Bacterial Agents/*administration & dosage/*chemistry [MESH] |Apoptosis/drug effects/physiology [MESH] |Bacteriolysis/*drug effects/physiology [MESH] |Cell Survival/drug effects/physiology [MESH] |Clostridioides difficile/cytology/*drug effects/*physiology [MESH] |Drug Discovery [MESH]Newly identified bacteriolytic enzymes that target a wide range of cli(epmc).pdf DeepDyve Pubget Overpricing