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Articles by Vinayagamurthy Balamurugan
Total Records ( 2 ) for Vinayagamurthy Balamurugan
  Durlav Prasad Bora , Veerakyathappa Bhanuprakash , Gnanavel Venkatesan , Vinayagamurthy Balamurugan , Manimuthu Prabhu and Revanaiah Yogisharadhya
  The study describes the effect of stabilization on the stability of an indigenous live attenuated orf vaccine with stabilizers like LS, LHT and TAA after lyophilization and also reconstitution with NSS, PBS, distilled water and 1 M MgSO4 exposed at different temperatures under established lyophilization conditions. The stability of the vaccine was assessed both in freeze-dried and reconstituted forms at different temperatures. The results indicated that the orf vaccine lyophilized with LS stabilizer at 25 and 45°C and LHT at 37°C found superior over others in stabilizing the keeping quality of the vaccine. Intrinsic thermo-stability studies revealed the rapid deterioration of the vaccine, when compared to the vaccine stabilized with the either of the stabilizers. Among the diluents used for reconstitution of the vaccine, quality in terms of infectivity titers of the virus was well preserved in vaccine diluted with 0.85% NSS compared to other diluents like PBS, DW and 1 M MgSO4. The 1 M MgSO4 found unsuitable for diluting the orf vaccine. The study suggests that the LS at 25 and 45°C and LHT at 37°C are the choice of stabilizers and 0.85% NSS is the choice of diluent for orf vaccine at all temperatures contemplated.
  Naveen Kumar , Yashpal Singh Malik , Kuldeep Sharma , Vinayagamurthy Balamurugan , Sathish Bhadravati Shivachandra and Kuldeep Dhama
  Rotaviruses of group A (RVA) are foremost cause of diarrhoeal diseases in neonates of animals and humans worldwide leading to substantial economic losses. The RVA non-structural protein-4 (NSP-4), a viral enterotoxin, is known to be associated with infantile gastroenteritis/secretory diarrhoea by inducing pathological changes in the mature enterocytes. In this study, the carboxyl terminus of NSP4 protein (73M to 175M) from a bovine RVA was expressed in Escherichia coli Tuner (DE3) pLysS cells. The fusion protein (rNSP4ct, ~31 kDa) with hexa-histidine tags on its both termini was purified by affinity chromatography under native condition using Nickel-Nitrilotriacetic acid (Ni-NTA) agarose resin. The purified soluble recombinant NSP4ct was confirmed by Western blot. The structural analysis of rNSP4 protein revealed similarity between bovine RVA and human RVA (central tetrameric coiled-coil region) and confirmed that it was composed of mainly alpha helix (85%), lacking the beta strands. The rNSP4ct protein of bovine RVA has the potential of being used in developing diagnostics, assessing the biological activity (enterotoxin property) of rNSP4ct in understanding the pathogenesis in intestinal mucosa which would reveal the role of anti-NSP4 antibodies in protection against rotavirus infection and stimulation of mucosal immunity in animal model.
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