Abstract

Mycobacterium tuberculosis H₃₇Rv (M. tuberculosis) genetic evaluation found various conditional mutants that are being unsuccessful in surviving in non-permissive temperature or need enriched sources for growing in non-adaptive conditions. In M. tuberculosis basically, these mutants refer to as Filamentous Temperature Sensitive (FTS) gene family which have Rv3102c, Rv3610c, Rv2748c, Rv2151c, Rv2154c, Rv3101c, Rv2921c and Rv2150cproteins that are involved in major processes like cell division, cell growth and cell signalling.This manuscript provides a straightforward conduit towards finding the exact role of Rv3101c and Rv3102c genes in cellular cell divisionand survival of this bacterium by using computational approaches. The physiochemical properties shows both the proteins are stable and protein-protein interaction shows Rv2150c R2151c, smpB, Rv3104c and Rv2921c commonly interacted with each other but Rv3101c protein, a transmembrane protein which has four transmembrane helices which provide a clue for these proteins that act in various signalling cascades and protein exporting system. The protein phosphorylation play important role in several cellular processes and in Rv3101c phosphorylation occurs at Thr75, Ser89 and in Rv3102c phosphorylation occurs at residues Thr54, Thr166, Thr173, Ser174, Ser212 and Tyr225. The predicted structure was validated by SAVES metaserver and Ramachandran plot shows above 90% residues were present in the allowed region. In the prediction of B-cell and T-cell on Rv3101c and Rv3102c, protein antigen presentation and antibody binding properties were determined. These epitopes can be used to develop more effective vaccines and identify neutralizing antibodies. The mutation identification on the F126 and F1397 in Rv3101c whereas in Rv3102c on position F45 cause a drastic loss in inter-atomic interactions. As Rv3101c and Rv3102c proteins are essential class of proteins in M. tuberculosis, therefore, understanding of this class is crucial for analyzing cell division mechanism of this bacterium and thus help in clarifying its pathogenesis mechanism inside the host. 

Keywords

Rv3101c, Rv3102c, cell division proteins, molecular modelling, structural stability