Glycation of calmodulin binding domain of iNOS may increase the chance of occurrence of tuberculosis in chronic diabetic state.

Tuberculosis is known to occur more in cases of chronic diabetes mellitus. The exact cause of such an association is mostly unknown. Recently we have shown using tools of computational biology that glycation of the subunits of respiratory burst enzyme NADPH oxidase may impair intra-macrophage killing of Mycobacterium tuberculosis. Since glycation of proteins including subunits of NADPH oxidase will be significantly increased in long standing uncontrolled diabetes we have concluded that it may be an important factor for increased association of tuberculosis in diabetic state. Analogous to NADPH oxidase, role of NOS is proved beyond any doubt for killing of intracellular pathogen like Mycobacterium tuberculosis. Based on the above mentioned premises, in this work we have studied glycation of various domains of iNOS using tools of computational biology and observed that glycation of K531 of Calmodulin binding domain of iNOS may impair the enzyme activity. We have concluded that the above phenomenon can happen at chronic diabetic state which may render the host susceptible to tuberculosis.