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10.1038/srep32948 http://scihub22266oqcxt.onion/10.1038/srep32948 C5021996!5021996 !27624595     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=27624595 &cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215 Deprecated: Implicit conversion from float 221.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 221.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\27624595 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Sci+Rep 2016 ; 6 (ä): 32948 Nephropedia Template TP {{tp|p=27624595 |t=2016. Imaging the antimicrobial mechanism(s) of cathelicidin-2 |pdf=|usr=}}{{27624595 }} gab.com Text Imaging the antimicrobial mechanism(s) of cathelicidin-2 JO: Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=27624595 #FOAvip Host defence peptides (HDPs) have the potential to become alternatives to conventional antibiotics in human and veterinary medicine. The HDP chicken cathelicidin-2 (CATH-2) has immunomodulatory and direct killing activities at micromolar concentrations. In this study the mechanism of action of CATH-2 against Escherichia coli (E. coli) was investigated in great detail using a unique combination of imaging and biophysical techniques. Live-imaging with confocal fluorescence microscopy demonstrated that FITC-labelled CATH-2 mainly localized at the membrane of E. coli. Upon binding, the bacterial membrane was readily permeabilized as was shown by propidium iodide influx into the cell. Concentration- and time-dependent effects of the peptide on E. coli cells were examined by transmission electron microscopy (TEM). CATH-2 treatment was found to induce dose-dependent morphological changes in E. coli. At sub-minimal inhibitory concentrations (sub-MIC), intracellular granulation, enhanced vesicle release and wrinkled membranes were observed, while membrane breakage and cell lysis occurred at MIC values. These effects were visible within 1-5?minute of peptide exposure. Immuno-gold TEM showed CATH-2 binding to bacterial membranes. At sub-MIC values the peptide rapidly localized intracellularly without visible membrane permeabilization. It is concluded that CATH-2 has detrimental effects on E. coli at concentrations that do not immediately kill the bacteria. Twit Text FOAVip Imaging the antimicrobial mechanism(s) of cathelicidin-2 ????Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=27624595 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27624595 #FOAvip English Wikipedia <ref>{{Cite pmid|27624595 }}</ref> Imaging the antimicrobial mechanism(s) of cathelicidin-2 #MMPMID27624595 Schneider VA ; Coorens M ; Ordonez SR ; Tjeerdsma-van Bokhoven JL ; Posthuma G ; van Dijk A ; Haagsman HP ; Veldhuizen EJ Sci Rep 2016[Sep]; 6 (ä): 32948 PMID27624595 show ga Host defence peptides (HDPs) have the potential to become alternatives to conventional antibiotics in human and veterinary medicine. The HDP chicken cathelicidin-2 (CATH-2) has immunomodulatory and direct killing activities at micromolar concentrations. In this study the mechanism of action of CATH-2 against Escherichia coli (E. coli) was investigated in great detail using a unique combination of imaging and biophysical techniques. Live-imaging with confocal fluorescence microscopy demonstrated that FITC-labelled CATH-2 mainly localized at the membrane of E. coli. Upon binding, the bacterial membrane was readily permeabilized as was shown by propidium iodide influx into the cell. Concentration- and time-dependent effects of the peptide on E. coli cells were examined by transmission electron microscopy (TEM). CATH-2 treatment was found to induce dose-dependent morphological changes in E. coli. At sub-minimal inhibitory concentrations (sub-MIC), intracellular granulation, enhanced vesicle release and wrinkled membranes were observed, while membrane breakage and cell lysis occurred at MIC values. These effects were visible within 1-5?minute of peptide exposure. Immuno-gold TEM showed CATH-2 binding to bacterial membranes. At sub-MIC values the peptide rapidly localized intracellularly without visible membrane permeabilization. It is concluded that CATH-2 has detrimental effects on E. coli at concentrations that do not immediately kill the bacteria. |Animals [MESH] |Antimicrobial Cationic Peptides/chemistry/*pharmacology [MESH] |Chickens [MESH] |Dose-Response Relationship, Drug [MESH] |Escherichia coli/*drug effects/ultrastructure [MESH] |Fluorescein-5-isothiocyanate/chemistry/*metabolism [MESH] |Microbial Sensitivity Tests [MESH] |Microscopy, Confocal [MESH] |Microscopy, Fluorescence [MESH]Imaging the antimicrobial mechanism(s) of cathelicidin-2 (epmc).pdf DeepDyve Pubget Overpricing