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http://purl.uniprot.org/citations/20800577http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20800577http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20800577http://www.w3.org/2000/01/rdf-schema#comment"A variety of Mycobacterium tuberculosis cell wall components induce expression of matrix metalloproteinase 9 (MMP-9) by monocytic cells and levels of MMP-9 in vivo positively correlate with severity of disease. Toll-like receptor (TLR)2 mediates cellular responses to acylated molecules but can also mediate responsiveness to diverse molecular structures, including non-acylated native viral and bacterial proteins. MPT/B-83 is a cell-associated lipoglycoprotein common to M. tuberculosis and M. bovis and an important antigen during infection of cattle. Since MPB83 is acylated and glycosylated, we investigated whether MPB83 would induce MMP-9 expression via interaction with TLR2, and assessed the contribution of the lipid, glycan and polypeptide components to its activity. Acylated peptide derived from MPB83 stimulated MMP-9 expression by human macrophage cells via interaction with both TLR2 and TLR1, but not TLR4. Lesser induction was found with secreted (non-acylated, but glycosylated) MPB83 protein purified from culture of M. bovis. Stimulation of cells with MPB83 induced TNF-α production which acted to upregulate MMP-9 expression. Surprisingly, recombinant MPB83 protein devoid of any post-translational modification also induced MMP-9 expression. Direct interaction of RecMPB83 with TLR2 was demonstrated by surface plasmon-resonance. MPB83 may act as a virulence factor through TLR2 mediated induction of MMP-9."xsd:string
http://purl.uniprot.org/citations/20800577http://purl.org/dc/terms/identifier"doi:10.1016/j.bbrc.2010.08.085"xsd:string
http://purl.uniprot.org/citations/20800577http://purl.org/dc/terms/identifier"doi:10.1016/j.bbrc.2010.08.085"xsd:string
http://purl.uniprot.org/citations/20800577http://purl.uniprot.org/core/author"Singh M."xsd:string
http://purl.uniprot.org/citations/20800577http://purl.uniprot.org/core/author"Singh M."xsd:string
http://purl.uniprot.org/citations/20800577http://purl.uniprot.org/core/author"Spallek R."xsd:string
http://purl.uniprot.org/citations/20800577http://purl.uniprot.org/core/author"Spallek R."xsd:string
http://purl.uniprot.org/citations/20800577http://purl.uniprot.org/core/author"Guerardel Y."xsd:string
http://purl.uniprot.org/citations/20800577http://purl.uniprot.org/core/author"Guerardel Y."xsd:string
http://purl.uniprot.org/citations/20800577http://purl.uniprot.org/core/author"Coddeville B."xsd:string
http://purl.uniprot.org/citations/20800577http://purl.uniprot.org/core/author"Coddeville B."xsd:string
http://purl.uniprot.org/citations/20800577http://purl.uniprot.org/core/author"Chambers M.A."xsd:string
http://purl.uniprot.org/citations/20800577http://purl.uniprot.org/core/author"Chambers M.A."xsd:string
http://purl.uniprot.org/citations/20800577http://purl.uniprot.org/core/author"Elass E."xsd:string
http://purl.uniprot.org/citations/20800577http://purl.uniprot.org/core/author"Elass E."xsd:string
http://purl.uniprot.org/citations/20800577http://purl.uniprot.org/core/author"Whelan A.O."xsd:string
http://purl.uniprot.org/citations/20800577http://purl.uniprot.org/core/author"Whelan A.O."xsd:string
http://purl.uniprot.org/citations/20800577http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20800577http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20800577http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/20800577http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/20800577http://purl.uniprot.org/core/pages"403-408"xsd:string
http://purl.uniprot.org/citations/20800577http://purl.uniprot.org/core/pages"403-408"xsd:string