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10.1073/pnas.1507082112 http://scihub22266oqcxt.onion/10.1073/pnas.1507082112 C4475985!4475985 !25944934     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=25944934 &cmd=llinks): Failed to open stream: HTTP request failed! 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Destructin-1 is a collagen-degrading endopeptidase secreted by Pseudogymnoascus destructans, the causative agent of white-nose syndrome |pdf=|usr=}}{{25944934 }} gab.com Text Destructin-1 is a collagen-degrading endopeptidase secreted by Pseudogymnoascus destructans, the causative agent of white-nose syndrome JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=25944934 #FOAvip Pseudogymnoascus destructans is the causative agent of white-nose syndrome, a disease that has caused the deaths of millions of bats in North America. This psychrophilic fungus proliferates at low temperatures and targets hibernating bats, resulting in their premature arousal from stupor with catastrophic consequences. Despite the impact of white-nose syndrome, little is known about the fungus itself or how it infects its mammalian host. P. destructans is not amenable to genetic manipulation, and therefore understanding the proteins involved in infection requires alternative approaches. Here, we identify hydrolytic enzymes secreted by P. destructans, and use a novel and unbiased substrate profiling technique to define active peptidases. These experiments revealed that endopeptidases are the major proteolytic activities secreted by P. destructans, and that collagen, the major structural protein in mammals, is actively degraded by the secretome. A serine endopeptidase, hereby-named Destructin-1, was subsequently identified, and a recombinant form overexpressed and purified. Biochemical analysis of Destructin-1 showed that it mediated collagen degradation, and a potent inhibitor of peptidase activity was identified. Treatment of P. destructans-conditioned media with this antagonist blocked collagen degradation and facilitated the detection of additional secreted proteolytic activities, including aminopeptidases and carboxypeptidases. These results provide molecular insights into the secretome of P. destructans, and identify serine endopeptidases that have the clear potential to facilitate tissue invasion and pathogenesis in the mammalian host. Twit Text FOAVip Destructin-1 is a collagen-degrading endopeptidase secreted by Pseudogymnoascus destructans, the causative agent of white-nose syndrome ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=25944934 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25944934 #FOAvip English Wikipedia <ref>{{Cite pmid|25944934 }}</ref> Destructin-1 is a collagen-degrading endopeptidase secreted by Pseudogymnoascus destructans, the causative agent of white-nose syndrome #MMPMID25944934 O'Donoghue AJ ; Knudsen GM ; Beekman C ; Perry JA ; Johnson AD ; DeRisi JL ; Craik CS ; Bennett RJ Proc Natl Acad Sci U S A 2015[Jun]; 112 (24 ): 7478-83 PMID25944934 show ga Pseudogymnoascus destructans is the causative agent of white-nose syndrome, a disease that has caused the deaths of millions of bats in North America. This psychrophilic fungus proliferates at low temperatures and targets hibernating bats, resulting in their premature arousal from stupor with catastrophic consequences. Despite the impact of white-nose syndrome, little is known about the fungus itself or how it infects its mammalian host. P. destructans is not amenable to genetic manipulation, and therefore understanding the proteins involved in infection requires alternative approaches. Here, we identify hydrolytic enzymes secreted by P. destructans, and use a novel and unbiased substrate profiling technique to define active peptidases. These experiments revealed that endopeptidases are the major proteolytic activities secreted by P. destructans, and that collagen, the major structural protein in mammals, is actively degraded by the secretome. A serine endopeptidase, hereby-named Destructin-1, was subsequently identified, and a recombinant form overexpressed and purified. Biochemical analysis of Destructin-1 showed that it mediated collagen degradation, and a potent inhibitor of peptidase activity was identified. Treatment of P. destructans-conditioned media with this antagonist blocked collagen degradation and facilitated the detection of additional secreted proteolytic activities, including aminopeptidases and carboxypeptidases. These results provide molecular insights into the secretome of P. destructans, and identify serine endopeptidases that have the clear potential to facilitate tissue invasion and pathogenesis in the mammalian host. |Amino Acid Sequence [MESH] |Animals [MESH] |Ascomycota/*enzymology/genetics/*pathogenicity [MESH] |Base Sequence [MESH] |Catalytic Domain [MESH] |Chiroptera/*microbiology [MESH] |Collagenases/chemistry/genetics/*metabolism [MESH] |DNA, Fungal/genetics [MESH] |Fungal Proteins/chemistry/genetics/*metabolism [MESH] |Models, Molecular [MESH] |Molecular Sequence Data [MESH] |Mycoses/microbiology/*veterinary [MESH] |Proteolysis [MESH] |Recombinant Proteins/chemistry/genetics/metabolism [MESH] |Sequence Homology, Amino Acid [MESH]Destructin-1 is a collagen-degrading endopeptidase secreted by Pseudog(epmc).pdf DeepDyve Pubget Overpricing