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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
10
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pubmed:dateCreated |
1998-2-25
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pubmed:abstractText |
Renibacterium salmoninarum, the agent of bacterial kidney disease in salmonids, releases high concentrations of extracellular protein in tissues of infected fish. The extracellular protein consists almost entirely of a 57-kDa protein and derivatives of degradation and aggregation of the same molecule. The 57-kDa protein and its derivatives were fractionated into defined ranges of molecular mass. Separated fractions continued to produce degradation and aggregation products. One-dimensional electrophoretic separation of extracellular protein revealed a number of proteolytically active bands from > 100 to approximately 18 kDa associated with various 57-kDa protein derivatives in the different molecular mass fractions. Two-dimensional separation of extracellular protein showed that continued degradation and aggregation, similar both in location and behavior to some of the 57-kDa protein derivatives, was also displayed by the proteolytically active bands after their separation. Effects of reducing agents and sulfhydryl group proteinase inhibitors indicated a common mechanism for the proteolytically active polypeptides characteristic of a thiol proteinase. The results suggested that the 57-kDa protein and some of its derivatives undergo autolytic cleavage, releasing a proteolytically active polypeptide(s) of at least 18 kDa. Soluble polysaccharide-like material also was detected in extracellular products and tissue from infected fish. Antiserum to the polysaccharide-like material cross-reacted with O-polysaccharide of the fish pathogen Aeromonas salmonicida, suggesting some structural similarity between these polysaccharides. The polysaccharide and the proteolytic activity associated with the 57-kDa protein derivatives should be investigated with respect to the pathogenesis of R. salmoninarum infections.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/9480644-1777853,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9480644-1981894,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9480644-1987079,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9480644-2222123,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9480644-2323542,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9480644-2380689,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9480644-2482922,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9480644-2580026,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9480644-2653212,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9480644-3364716,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9480644-3524440,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9480644-4696702,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9480644-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9480644-7845226
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0099-2240
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
63
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3770-5
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:9480644-Aeromonas,
pubmed-meshheading:9480644-Animals,
pubmed-meshheading:9480644-Bacterial Proteins,
pubmed-meshheading:9480644-Cross Reactions,
pubmed-meshheading:9480644-Endopeptidases,
pubmed-meshheading:9480644-Extracellular Space,
pubmed-meshheading:9480644-Fish Diseases,
pubmed-meshheading:9480644-Gram-Positive Bacteria,
pubmed-meshheading:9480644-Gram-Positive Bacterial Infections,
pubmed-meshheading:9480644-Kidney Diseases,
pubmed-meshheading:9480644-Molecular Weight,
pubmed-meshheading:9480644-Polysaccharides, Bacterial,
pubmed-meshheading:9480644-Salmonidae,
pubmed-meshheading:9480644-Virulence
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pubmed:year |
1997
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pubmed:articleTitle |
Further characterization of Renibacterium salmoninarum extracellular products.
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pubmed:affiliation |
Department of Biology, University of New Brunswick, Fredericton, Canada.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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