tuberculosis H37Ra. This is one of the components of
the high-affinity ATP-driven potassium transport system that catalyzes the hydrolysis of ATP coupled with the exchange of hydrogen and potassium ions. The gene encoding this protein was found to be non-essential for mycobacterial growth [53]. Taken together, these proteins and the ones with no defined physiological role present in higher amounts on the surface of M. tuberculosis H37Ra, provide a lead to elucidate the biological functions that might take us a step closer to understand the fundamental differences between the two strains and hence the mechanisms that influence pathogenicity. Gao and colleagues (2004) [34], investigated the aggregation of mycobacteria into GDC-0941 chemical structure structures known as cords which is an intrinsic property of the human tubercle bacillus. This property is thought to be determined by the lipid composition Selleckchem Mizoribine of the bacterial cell surface and may contribute to the virulence of the organism [54]. Using microarray technology, they compared the pattern of gene expression of M. tuberculosis H37Rv with M. tuberculosis H37Ra under five different nutrient combinations and growth conditions. Under all of the conditions tested, M. tuberculosis H37Rv formed cords and M. tuberculosis H37Ra did not. By focusing their analysis only on genes that were differentially expressed under all conditions tested, they identified
4SC-202 cost 22 genes that were consistently expressed at higher levels in H37Rv than in H37Ra. In our study we have observed 5 of those proteins, where 4 of them were observed in both strains, and one only in M. tuberculosis H37Rv strain. Interestingly, 5 proteins had a relative abundance higher than 5 fold in M. tuberculosis H37Rv which is in line with Gao’s report, however, one of them (Rv2289) were Montelukast Sodium >5x more abundant in M. tuberculosis H37Ra (Figure 3). This indicates that RNA level for genes are not directly proportional with the protein level, emphasizing the importance of transcriptome validation at protein level [55, 56]. Figure 3 Proteins reported by Gao et. al., (2004) to be consistently expressed at higher levels in H37Rv than in H37Ra, and are also
observed in our study. In a comparative genome analysis of M. tuberculosis H37Rv and H37Ra to determine the basis of attenuation of virulence in H37Ra, Zheng and colleagues (2008) reported 57 genetic sequence variations between the two strains. They suggested that these variations may account for the attenuation of virulence in M. tuberculosis H37Ra and various other phenotypic changes that are different from its virulent counterpart M. tuberculosis H37Rv. Interestingly, the majority of these variations occurred in proteins thought to be exported to the membrane or involved in cell wall metabolism. We observed 12 of them, of which were up-regulated in M. tuberculosis H37Rv, while 7 had similar expression. Contrary to the expectation, we observed a 3.