African Journal of
Microbiology Research

  • Abbreviation: Afr. J. Microbiol. Res.
  • Language: English
  • ISSN: 1996-0808
  • DOI: 10.5897/AJMR
  • Start Year: 2007
  • Published Articles: 5210

Full Length Research Paper

Interaction of Mycobacterium tuberculosis ESAT-6 protein with ADAM9 protein

Huixing Liang1,2* and Aihui Chen1
  1College of Chemical and Biological Engineering, Yancheng Institute of Technology, Yancheng 224051, China. 2College of Forest Resources and Environment, Nanjing Forestry University, Nanjing 210000, China.
Email: [email protected]

  •  Accepted: 29 March 2011
  •  Published: 18 April 2011



The ESAT-6 protein of Mycobacterium tuberculosis (M. tb) is an important structural and functional protein, which has been known to be involved in the virulence, pathogenesis as well as proliferation of the pathogen; however, how ESAT-6 protein interact with host protein is still unclear. In order to study the function of the M. tuberculosis protein ESAT-6 in the infection process, we searched for host proteins that interact with this secreted mycobacterial protein. Using a yeast two-hybrid system we identified the ADAM9 (a disintegrin and metalloprotease) protein as a candidate to interact with ESAT-6. This interaction was further confirmed by protein overlay and surface plasmon resonance binding assay using recombinant ESAT-6 and ADAM9, and by GST pull-down analysis of the mycobacterial expressed ESAT-6 and ADAM9. The interaction domains were localized by yeast two-hybrid studies using truncated derivatives of ESAT-6 protein. The C-terminus of ESAT-6 binds to the ADAM9, Thus, the host protein ADAM9 represents a possible cellular receptor for the mycobacterial protein ESAT-6. This is the first report demonstrating the interaction of ADAM9 with a structural protein of M. tb.


Key words: ESAT-6 protein, ADAM9 protein, Mycobacterium tuberculosis, yeast two-hybrid, GST pull-down assay, surface plasmon resonance binding