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.
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Authors | Carla Esposito, Paola Carullo, Emilia Pedone, Giuseppe Graziano, Pompea Del Vecchio, Rita Berisio |
Journal | FEBS letters
(FEBS Lett)
Vol. 584
Issue 6
Pg. 1091-6
(Mar 19 2010)
ISSN: 1873-3468 [Electronic] England |
PMID | 20178790
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
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Copyright | Copyright 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. |
Chemical References |
- Antigens, Bacterial
- Lectins
- heparin-binding hemagglutinin
- Mycobacterium tuberculosis antigens
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Topics |
- Agglutination
- Amino Acid Sequence
- Antigens, Bacterial
(chemistry, metabolism)
- Bacterial Adhesion
(physiology)
- Lectins
(chemistry, metabolism, physiology)
- Light
- Models, Molecular
- Molecular Sequence Data
- Mycobacterium tuberculosis
(metabolism, physiology)
- Protein Conformation
- Protein Folding
- Protein Multimerization
- Protein Stability
- Scattering, Radiation
- Temperature
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