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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2-3
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pubmed:dateCreated |
1997-2-5
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pubmed:databankReference |
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pubmed:abstractText |
Mycobacterium avium is a causative agent of mycobacterioses in systemically immunocompromised individuals, whereas Mycobacterium intracellulare is responsible for causing infections in relatively immunocompetent hosts. In an attempt to identify components that could be involved in virulence, we characterised the 38 kDa-encoding gene of M intracellulare that is absent in M. avium. This antigen cross reacts immunologically with a major 38 kDa antigen of M. tuberculosis, and both antigens are homologues of the phosphate transport subunit S (PstS) of the pst complex of Escherichia coli. Unlike the M. tuberculosis complex the M. intracellulare coding gene was found to be duplicated. We also identified and characterised other pst genes that may constitute an operon. Considering that multiple isoforms of PstS are present in mycobacteria the possible role of pstS1 genes for pathogenesis is discussed.
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Ag38 antigen, Mycobacterium...,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Immunodominant Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Periplasmic Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphate-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/PstS protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0378-1097
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
144
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
235-40
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8900068-Amino Acid Sequence,
pubmed-meshheading:8900068-Antigens, Bacterial,
pubmed-meshheading:8900068-Carrier Proteins,
pubmed-meshheading:8900068-Cross Reactions,
pubmed-meshheading:8900068-Escherichia coli Proteins,
pubmed-meshheading:8900068-Genes, Bacterial,
pubmed-meshheading:8900068-Humans,
pubmed-meshheading:8900068-Immunodominant Epitopes,
pubmed-meshheading:8900068-Lipoproteins,
pubmed-meshheading:8900068-Membrane Proteins,
pubmed-meshheading:8900068-Molecular Sequence Data,
pubmed-meshheading:8900068-Multigene Family,
pubmed-meshheading:8900068-Mycobacterium avium Complex,
pubmed-meshheading:8900068-Mycobacterium tuberculosis,
pubmed-meshheading:8900068-Operon,
pubmed-meshheading:8900068-Periplasmic Binding Proteins,
pubmed-meshheading:8900068-Phosphate-Binding Proteins,
pubmed-meshheading:8900068-Recombinant Fusion Proteins,
pubmed-meshheading:8900068-Sequence Alignment,
pubmed-meshheading:8900068-Sequence Homology, Amino Acid,
pubmed-meshheading:8900068-Species Specificity
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pubmed:year |
1996
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pubmed:articleTitle |
Duplication of genes encoding the immunodominant 38 kDa antigen in Mycobacterium intracellulare.
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pubmed:affiliation |
M.R.C. Tuberculosis and Related Infections, Unit, Hammersmith Hospital,London, UK. h.thangar@rpms.ac.uk
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pubmed:publicationType |
Journal Article,
Comparative Study
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