Source:http://linkedlifedata.com/resource/pubmed/id/17208488
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
|
| pubmed:dateCreated |
2007-2-16
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| pubmed:databankReference | |
| pubmed:abstractText |
Mycobacterium tuberculosis produces heparin-binding hemagglutinin (TB-HBHA), an adhesin involved in binding to non-professional phagocytes and in extrapulmonary dissemination. TB-HBHA binds sulphated glycoconjugates through its C-terminal lysine-rich domain and can be purified by heparin-Sepharose chromatography. Homologues of HBHA are found in other pathogenic mycobacteria, but previous investigations failed to demonstrate them in non-pathogenic Mycobacterium smegmatis. We identified a gene encoding a HBHA-like protein, named MS-HBHA, from the complete M. smegmatis genome. The deduced MS-HBHA amino acid sequence revealed 68% identity with that of TB-HBHA and contains lysine-rich repeats in its C-terminal domain. However, in contrast to TB-HBHA, the lysine-rich domain of MS-HBHA is preceded by a stretch of acidic residues. This difference likely explains the low affinity for heparin displayed by MS-HBHA compared to TB-HBHA. Isolation by heparin-Sepharose chromatography procedure and mass spectrometry analysis indicated that MS-HBHA, similar to TB-HBHA contains several methylated lysine residues in its C-terminal domain. Although MS-HBHA is associated with M. smegmatis cell wall fractions, it does not seem to play a role in epithelial adherence and its function remains unknown. We therefore conclude that TB-HBHA may have evolved as an adhesin in pathogenic mycobacteria from a homolog that serves a different function in a saprophytic mycobacterium.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adhesins, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/Lectins,
http://linkedlifedata.com/resource/pubmed/chemical/heparin-binding hemagglutinin
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| pubmed:status |
MEDLINE
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| pubmed:month |
Feb
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| pubmed:issn |
1286-4579
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| pubmed:author |
pubmed-author:Angela de Melo MarquesMariaM,
pubmed-author:BietFranckF,
pubmed-author:BrennanPatrick JPJ,
pubmed-author:DrobecqHervéH,
pubmed-author:GrayonMaggyM,
pubmed-author:LochtCamilleC,
pubmed-author:MenozziFranco DanteFD,
pubmed-author:RazeDominiqueD,
pubmed-author:Vidal PessolaniMaria CristinaMC,
pubmed-author:Xavier da SilveiraErika KoppEK
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| pubmed:issnType |
Print
|
| pubmed:volume |
9
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| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
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| pubmed:pagination |
175-82
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| pubmed:meshHeading |
pubmed-meshheading:17208488-Adhesins, Bacterial,
pubmed-meshheading:17208488-Amino Acid Sequence,
pubmed-meshheading:17208488-Bacterial Adhesion,
pubmed-meshheading:17208488-Bacterial Proteins,
pubmed-meshheading:17208488-Cell Fractionation,
pubmed-meshheading:17208488-Cell Line,
pubmed-meshheading:17208488-Cell Wall,
pubmed-meshheading:17208488-DNA, Bacterial,
pubmed-meshheading:17208488-Epithelial Cells,
pubmed-meshheading:17208488-Genome, Bacterial,
pubmed-meshheading:17208488-Humans,
pubmed-meshheading:17208488-Lectins,
pubmed-meshheading:17208488-Mass Spectrometry,
pubmed-meshheading:17208488-Molecular Sequence Data,
pubmed-meshheading:17208488-Mycobacterium smegmatis,
pubmed-meshheading:17208488-Protein Structure, Tertiary,
pubmed-meshheading:17208488-Repetitive Sequences, Amino Acid,
pubmed-meshheading:17208488-Sequence Analysis, DNA,
pubmed-meshheading:17208488-Sequence Homology, Amino Acid
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| pubmed:year |
2007
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| pubmed:articleTitle |
Mycobacterium smegmatis produces an HBHA homologue which is not involved in epithelial adherence.
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| pubmed:affiliation |
UR1282, Infectiologie Animale, Santé Publique (IASP-311), INRA Centre de Tours, F-37380 Nouzilly France. franck.biet@tours.inra.fr
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| pubmed:publicationType |
Journal Article
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