Heparin-binding hemagglutinin HBHA from Mycobacterium tuberculosis affects actin polymerisation

Carla Esposito, Daniela Marasco, Giovanni Delogu, Emilia Pedone, Rita Berisio

Research output: Contribution to journalArticlepeer-review


HBHA is a mycobacterial cell surface protein that mediates adhesion to epithelial cells and that has been implicated in the dissemination of Mycobacterium tuberculosis (Mtb) from the site of primary infection. In this work, we demonstrate that HBHA is able to bind G-actin whereas its shorter form, deprived of the lysine-rich C-terminal region (HBHAΔC), does not bind. Consistently, interaction of actin with HBHA is competitive with heparin binding. Notably, we also observe that HBHA, but not HBHAΔC, clearly hampers G-actin polymerisation into F-actin filaments. Since Mtb escapes from the phagosome into the cytosol of host cells, where it can persist and replicate, HBHA is properly localised on the bacterial surface to regulate the dynamic process of cytoskeleton formation driven by actin polymerisation and depolymerisation.

Original languageEnglish
Pages (from-to)339-344
Number of pages6
JournalBiochemical and Biophysical Research Communications
Issue number2
Publication statusPublished - Jul 1 2011


  • Actin dynamics
  • Protein structure
  • Tuberculosis

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Molecular Biology


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