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

Giovanni Delogu, Giovanni Fadda, Michael J. Brennan

Research output: Contribution to journalArticlepeer-review

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 languageEnglish
Pages (from-to)1035-1039
Number of pages5
JournalProtein and Peptide Letters
Volume19
Issue number10
DOIs
Publication statusPublished - Oct 2012

Keywords

  • Adhesion
  • Heparin binding hemagglutinin
  • Tuberculosis

ASJC Scopus subject areas

  • Biochemistry
  • Structural Biology

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