title: Impact of structural domains of the heparin binding hemagglutinin of Mycobacterium tuberculosis on function.
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.
authors.affiliation: Istituto di Microbiologia, Università Cattolica del Sacro Cuore, Rome,Italy. gdelogu@rm.unicatt.it
authors.forename: Giovanni
authors.initials: G
authors.lastname: Delogu
authors.forename: Giovanni
authors.initials: G
authors.lastname: Fadda
authors.forename: Michael J
authors.initials: MJ
authors.lastname: Brennan
mesh_terms: D000818:Animals; D006801:Humans; D037102:Lectins / Q000737:chemistry / Q000378:metabolism*; D009169:Mycobacterium tuberculosis / Q000472:pathogenicity*; D017434:Protein Structure, Tertiary; D014376:Tuberculosis / Q000378:metabolism* / Q000473:pathology
chemical_list: D037102:Lectins; C104578:heparin-binding hemagglutinin