Abstract
Among the few well characterized virulence factors of Mycobacterium tuberculosis (Mtb) is the heparinbinding hemagglutinin (HBHA). HBHA is a 21-kDa protein that localizes to the mycobacterial surface where it can interact with host components. Interaction with epithelial cells and components of the extracellular matrix is mediated by the methylated lysine-rich C-terminal domain of the protein. The N-terminal end of HBHA contains a coiled coil motif which is involved in protein oligomerization and bacterial-bacterial aggregation. In this report, we will focus our attention on what is known about the structure of the HBHA protein and the protein function and role in TB pathogenesis.
Original language | English |
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Pages (from-to) | 1035-1039 |
Number of pages | 5 |
Journal | Protein and Peptide Letters |
Volume | 19 |
Issue number | 10 |
DOIs | |
Publication status | Published - Oct 2012 |
Keywords
- Adhesion
- Heparin binding hemagglutinin
- Tuberculosis
ASJC Scopus subject areas
- Biochemistry
- Structural Biology