Abstract

Yanfen Wang, Ying Xiao, Yanhui Li, Yanhua Feng, Chunping Li and Haichun Ma*

Mycobacterium tuberculosis continues to be a leading cause of human deaths due to an infectious agent. 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, little is still known about the host factors that interact with ESAT6. Therefore, a yeast two-hybrid screening of a human lung complementary deoxyribonucleic acid (cDNA) library, using ESAT6 as bait, was performed to identify ESAT-6 interaction with host protein. A vascular endothelial growth factor (VEGF) was found to interact specifically with the ESAT6 protein. Subcellular localization and glutathione S-transferase (GST)-pull down assays were used in an attempt to further confirm the interaction of VEGF and esat-6. All our data suggest that the interaction of VEGF with a structural protein of M. tuberculosis may be important for modulation of virulence of M. tuberculosis.