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.
Keywords: Tuberculosis, heparin binding hemagglutinin, adhesion, Mycobacterium tuberculosis, coiled coil motif, bacterial-bacterial aggregation, C-terminal domain, TB pathogenesis, etiologic agent, gram-negative bacteria
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