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Impact of Structural Domains of the Heparin Binding Hemagglutinin of Mycobacterium tuberculosis on Function

[ Vol. 19 , Issue. 10 ]


Giovanni Delogu, Giovanni Fadda and Michael J. Brennan   Pages 1035 - 1039 ( 5 )


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.


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


Istituto di Microbiologia, Universita Cattolica del Sacro Cuore, Largo A. Gemelli, 8 – 00168 – Rome (Italy).

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