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Dimerisation and structural integrity of Heparin Binding Hemagglutinin A from Mycobacterium tuberculosis:Implicatios for bacterial agglutination
- Publication Year :
- 2010
-
Abstract
- Heparin Binding Hemagglutinin A (HBHA) is hitherto the sole virulence factor associated with tuberculosis dissemination from the lungs, the site of primary infection, to epithelial cells. We have previously reported the solution structure of HBHA, a dimeric and elongated molecule. Since oligomerisation of HBHA is associated with its ability to induce bacterial agglutination, we investigated this process using experimental and modelling techniques. We here identified a short segment of HBHA whose presence is mandatory for the stability of folded conformation, whose denaturation is a reversible two-state process. Our data suggest that agglutination-driven cell–cell interactions do not occur via association of HBHA monomers, nor via association of HBHA dimers and open the scenario to a possible trans-dimerisation process.
- Subjects :
- Agglutination
Tuberculosi
Dimerisation
Coiled coil
Stability
Subjects
Details
- Language :
- English
- Database :
- OpenAIRE
- Accession number :
- edsair.od......3730..fc19b3e7857d218cb442c49fc6e834d2