Linked Life Data

18187354

Source:http://linkedlifedata.com/resource/pubmed/id/18187354

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pubmed-article:18187354pubmed:abstractTextKudoa paniformis and Kudoa thyrsites (Myxozoa: Myxosporea) infections are associated with severe proteolysis of host muscle tissue post-mortem. The present study was undertaken to identify and characterize the protease responsible for myoliquefaction and determine mechanisms controlling protease function in vivo. N-terminal sequence analysis of partially purified protease from hake muscle infected with K. paniformis and K. thyrsites revealed a 23 amino acid sequence that aligned with cysteine proteases. Enzyme inhibition assays confirmed the presence of an essential active site cysteine residue. Using the above K. paniformis amino acid sequence data, a corresponding cDNA sequence from K. thyrsites plasmodia was elucidated revealing a cathepsin L proenzyme (Kth-CL). The translated amino acid sequence lacked a signal sequence characteristic of lysosomal and secreted proteins suggesting a unique cytoplasmic location. Only the proenzyme form of Kth-CL was present in Atlantic salmon muscle anti-mortem but this form became processed in vivo when infected muscle was stored at 4 degrees C. The proenzyme of Kth-CL showed uninhibited activity at pH 6.0, negligible activity at pH 6.5 and no measurable activity at pH 7.0 whilst the processed protease showed stability and function over a broad pH range (pH 4.5-8.8). The pH dependent processing and function of Kth-CL was consistent with histidine residues in the proregion playing a critical role in the regulation of Kth-CL.lld:pubmed
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pubmed-article:18187354pubmed:dateRevised2009-11-19lld:pubmed
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pubmed-article:18187354pubmed:articleTitleIdentification, characterization and deduced amino acid sequence of the dominant protease from Kudoa paniformis and K. thyrsites: a unique cytoplasmic cysteine protease.lld:pubmed
pubmed-article:18187354pubmed:affiliationBC Centre for Aquatic Health Sciences, 621 Island Hwy, PO Box 277, Campbell River, BC Canada V9W 5B1. val.funk@cahs-bc.calld:pubmed
pubmed-article:18187354pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:18187354pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed