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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
10
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pubmed:dateCreated |
2001-5-18
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pubmed:abstractText |
Extracellular cleavage of virus envelope fusion glycoproteins by host cellular proteases is a prerequisite for the infectivity of mammalian and nonpathogenic avian influenza viruses, and Sendai virus. Here we report a protease present in the airway that, like tryptase Clara, can process influenza A virus haemagglutinin and Sendai virus envelope fusion glycoprotein. This protease was extracted from the membrane fraction of rat lungs, purified and then identified as a mini-plasmin. Mini-plasmin was distributed predominantly in the epithelial cells of the upward divisions of bronchioles and potentiated the replication of broad-spectrum influenza A viruses and Sendai virus, even that of the plasmin-insensitive influenza A virus strain. In comparison with plasmin, its increased hydrophobicity, leading to its higher local concentrations on membranes, and decreased molecular mass may enable mini-plasmin to gain ready access to the cleavage sites of various haemagglutinins and fusion glycoproteins after expression of these viral proteins on the cell surface. These findings suggest that mini-plasmin in the airway may play a pivotal role in the spread of viruses and their pathogenicity.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0014-2956
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
268
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2847-55
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:11358500-Amino Acid Sequence,
pubmed-meshheading:11358500-Animals,
pubmed-meshheading:11358500-Blotting, Western,
pubmed-meshheading:11358500-Bronchi,
pubmed-meshheading:11358500-Cell Membrane,
pubmed-meshheading:11358500-Dose-Response Relationship, Drug,
pubmed-meshheading:11358500-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:11358500-Epithelial Cells,
pubmed-meshheading:11358500-Fibrinolysin,
pubmed-meshheading:11358500-Humans,
pubmed-meshheading:11358500-Immunohistochemistry,
pubmed-meshheading:11358500-Infection,
pubmed-meshheading:11358500-Influenza A virus,
pubmed-meshheading:11358500-Isoflurophate,
pubmed-meshheading:11358500-Lung,
pubmed-meshheading:11358500-Male,
pubmed-meshheading:11358500-Molecular Sequence Data,
pubmed-meshheading:11358500-Peptide Fragments,
pubmed-meshheading:11358500-Rats,
pubmed-meshheading:11358500-Rats, Wistar,
pubmed-meshheading:11358500-Respirovirus,
pubmed-meshheading:11358500-Sequence Analysis, Protein,
pubmed-meshheading:11358500-Sequence Homology, Amino Acid,
pubmed-meshheading:11358500-Substrate Specificity,
pubmed-meshheading:11358500-Viral Envelope Proteins
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pubmed:year |
2001
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pubmed:articleTitle |
Mini-plasmin found in the epithelial cells of bronchioles triggers infection by broad-spectrum influenza A viruses and Sendai virus.
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pubmed:affiliation |
Division of Enzyme Chemistry, Institute for Enzyme Research, University of Tokushima, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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