Molecular Docking MPB83 Protein on β2, β3, and α5β1 Integrins: Pathogenesis of Bovine Tuberculosis in Humans

Abstract

Tuberculosis is a chronic infectious disease caused by the Mycobacterium tuberculosis complex (MTBC). Two MTBC species that causes infection in human are Mycobacterium tuberculosis (M. tuberculosis) and Mycobacterium bovis (M. bovis). Bovine tuberculosis (bTB) is a zoonotic disease with 2.55 times higher mortality rate compared to tuberculosis due to M. tuberculosis. Mycobacterium infect humans through the bonding between adhesin molecules on the bacteria surface and fibronectin receptors on the human body such as β2, β3, and α5β1 integrins. β2, β3, and α5β1 integrins are responsible for migrating bacterial activity and strengthening cell adhesion. MPB83 is a bacterial surface protein expressed more by M. bovis than by M. tuberculosis. This study aims to examine the binding of MPB83 protein to β2, β3, and α5β1 integrins as potential pathogenesis of bTB in humans by molecular docking method. Molecular docking was carried out using ClusPro to determine the interaction between the MPB83 protein and β2, β3, and α5β1 integrins based on binding energy and binding interaction model. The results showed that in silico, bonds occur between MPB83 protein and β2, β3, and α5β1 integrins which can potential for the pathogenesis of bTB in humans.