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Articles by Vinay Kumar
Total Records ( 3 ) for Vinay Kumar
  S.K. Singh , S. Mehra , S.K. Shukla , Vinay Kumar , A. Tiwari , M. Mehra , Giriraj Goyal , Jose Mathew and Deepak Sharma
  The MHC class I gene was amplified, cloned and sequenced in guinea fowl using the primers specific to BF2 gene in chicken. The nucleotide sequence of 571 bp partial CDS of BF2 gene includes 32 nucleotides of signal peptide (exon 1), complete α1 domain (270 nucleotides) and 269 nucleotides of α2 domain. For α1 and α domain no sequence variation was observed within guinea fowl sequences, however, high variability was observed within the other poultry species (15.93-28.03%) except chicken (7.95-9.16%). Between the guinea fowl and other poultry species, the α1 domain showed high nucleotide variability (29.26-43.70%). Among poultry species, guinea fowl showed least variability with chicken and maximum with duck. Among the substitutions, majorities were of non-synonymous (76.27%) with a ration of 1:3 between synonymous to non-synonymous substitutions. Guinea fowl showed lower genetic distances (Kimura 2-parameter) with chicken and quail (0.211-0.215), while with duck and goose, it showed higher genetic distances (0.343-0.350). Phylogenetic tree, based these genetic distances revealed two major clusters, comprising of guinea fowl, quail and chicken in one with guinea fowl as separate branch, while duck and goose in other.
  G. Goyal , V. Upmanyu , S.K. Singh , S.K. Shukla , S. Mehra , Vinay Kumar and Deepak Sharma
  Differential expression of IL-6 and IGF-II genes were studied in guinea fowl and broiler chicken using semi-quantitative analysis. A 219 bp fragment of IL-6 and 215 bp fragment of IGF-II were amplified in guinea fowl and broiler chicken using chicken specific primers. Semi-quantitative analysis revealed the adjusted Integral Density of 0.853 and 0.051 for IL-6 band in guinea fowl and broiler chicken respectively, revealing 16.62 fold higher IL-6 mRNA expression in LPS induced PBMCs from guinea fowl as compared to that from broiler. However, adjusted Integral Density of IGF-II band was 0.082 and 1.106 for IGF-II band in guinea fowl and broiler chicken respectively, which revealed 13.43 fold increase in IGF-II mRNA expression in LPS induced PBMCs in broiler chicken as compared to that in guinea fowl. Hence, guinea fowl showed higher expression of pro-inflammatory cytokine (IL-6) and lower expression of IGF-II in comparison to broiler chicken. These findings were as per expectation in view of much higher immuno-competence and lower growth rate in guinea fowl in comparison to chicken.
  Jay Kumar Singh , Ravindra D. Makde , Vinay Kumar and Dulal Panda
  SepF (Septum Forming) protein has been recently identified through genetic studies, and it has been suggested to be involved in the division of Bacillus subtilis cells. We have purified functional B. subtilis SepF from the inclusion bodies overexpressed in Escherichia coli. Far-UV circular dichroism and fluorescence spectroscopic analysis involving the extrinsic fluorescent probe 1-anilinonaphthalene-8-sulfonic acid suggested that the purified SepF had characteristics of folded proteins. SepF was found to promote the assembly and bundling of FtsZ protofilaments using three complimentary techniques, namely 90° light scattering, sedimentation, and transmission electron microscopy. SepF also decreased the critical concentration of FtsZ assembly, prevented the dilution-induced disassembly of FtsZ protofilaments, and suppressed the GTPase activity of FtsZ. Further, thick bundles of FtsZ protofilaments were observed using fluorescein isothiocyanate-labeled SepF (FITC-SepF). Interestingly, FITC-SepF was found to be uniformly distributed along the length of the FtsZ protofilaments, suggesting that SepF copolymerizes with FtsZ. SepF formed a stable complex with FtsZ, as evident from the gel filtration analysis. Using a C-terminal tail truncated FtsZ (FtsZΔ16) and a C-terminal synthetic peptide of B. subtilis FtsZ (366-382); we provided evidence indicating that SepF binds primarily to the C-terminal tail of FtsZ. The present work in concert with the available in vivo data support a model in which SepF plays an important role in regulating the assembly dynamics of the divisome complex; therefore, it may have an important role in bacterial cell division.
 
 
 
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