Dimerisation and structural integrity of Heparin Binding Hemagglutinin A from Mycobacterium tuberculosis: Implications for bacterial agglutination

作者：Esposito Carla; Carullo Paola; Pedone Emilia; Graziano Giuseppe; Del Vecchio Pompea; Berisio Rita^*

来源：FEBS Letters, 2010, 584(6): 1091-1096.

DOI：10.1016/j.febslet.2010.02.044

• Coiled coil
• Tuberculosis
• Stability
• Agglutination
• Dimerisation

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.
Structured summary:
MINT-7709940, MINT-7709948: HBHA (uniprotkb: A5TZK3) and HBHA ( uniprotkb: A5TZK3) bind (MI: 0407) by circular dichroism ( MI: 0016)
MINT-7709966: HBHA ( uniprotkb: A5TZK3) and HBHA ( uniprotkb: A5TZK3) bind ( MI: 0407) by biophysical ( MI: 0013)
MINT-7709955: HBHA ( uniprotkb

• 出版日期2010-3-19