Vikrant Nain

Gautam Buddha University

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Co-Authors

Rekha Puria

Gautam Buddha University

Polumetla Ananda Kumar

National Research Centre on Plant Biotechnology

Shakti Sahi

Gautam Buddha University

Preety Rawal

Gautam Buddha University

Savneet Kaur

Institute of Liver and Biliary Sciences

Dinesh Mani Tripathi

Institute of Liver and Biliary Sciences

Meenakshi Chaudhary

Shiv Nadar University

K. R. S. Sambasiva Rao

Mizoram University

Anju Verma

University of Georgia

Anuradha Bhardwaj

National Research Centre on Equines

Cooperative Institutions

Gautam Buddha University

Indian Agricultural Research Institute

National Research Centre on Plant Biotechnology

Institute of Liver and Biliary Sciences

University of Delhi

All India Institute of Medical Sciences

Indian Council of Agricultural Research

Institute of Microbial Technology

Amity University

Chaudhary Charan Singh Haryana Agricultural University

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Cloning and heterologous expression of cellulose free thermostable xylanase from Bacillus brevis

SpringerPlus (2014)

Girish K Goswami M. Krishnamohan Vikrant Nain Chetana Aggarwal Bandarupalli Ramesh

Xylanase gene isolated from Bacillus brevis was expressed in E. coli BL21. Sequencing of the gene (Gen Bank accession number: HQ179986) showed that it belongs to family 11 xylanases. The recombinant xylanase was predominantly secreted to culture medium and showed mesophilic nature (optimum activity at 55°C and pH 7.0). The cell free culture medium exhibited 30 IU/ml xylanse activity. The enzyme did not show any cellulose activity and was active under wide range of temperature (40°C to 80°C) and pH (4 to 9). The enzyme showed considerable thermo stability and regained over 90% of activity, when returned to 55°C after boiling for 5 min. These physiochemical properties of B. brevis xylanse show high potential of its applications in paper and pulp industry.

Heterologous expression

Heterologous

Cloning (programming)

Mesophile

10.1186/2193-1801-3-20

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Citations (27)

Selection and Screening Strategies

Springer eBooks (2010)

Haiying Liang Parveen Kumar Vikrant Nain William A. Powell John E. Carlson

Insert (composites)

10.1007/978-3-642-04809-8_4

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Citations (7)

KasI vs. SspDI: Comparative analysis of enzyme activity for restriction digestion

Indian Journal of Experimental Biology (2019)

Suman Rekha Puria Vikrant Nain

Digestion

Source

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Citations (0)

MYOD and HAND transcription factors have conserved recognition sites in mTOR promoter: insights from in silico analysis

Interdisciplinary Sciences Computational Life Sciences (2018)

Ankita Awasthi Vikrant Nain Rekha Puria

Conserved sequence

DNA binding site

Transcription

10.1007/s12539-018-0284-5

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Citations (2)

Comparative response of Spodoptera litura challenged per os with Serratia marcescens strains differing in virulence

Journal of Invertebrate Pathology (2021)

Chetana Aggarwal Sangeeta Paul Vikrant Nain Vishwas Tripathi Bishwajeet Paul

Hemolymph

10.1016/j.jip.2021.107562

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Citations (4)

Synergistic activity between Bacillus thuringiensis Cry1Ab and Cry1Ac toxins against maize stem borer (Chilo partellus Swinhoe)

Letters in Applied Microbiology (2010)

Pragya Sharma Vikrant Nain Suman Lakhanpaul Pankaj Kumar

Aim: To select a toxin combination for the management of maize stem borer (Chilo partellus) and to understand possible mechanism of synergism among Bacillus thuringiensis Cry1A toxins tested. Methods and Results: Three Cry1A toxins were over expressed in Escherichia coli strain JM105 and used for diet overlay insect bioassay against C. partellus neonate larvae, both alone and in combinations. Probit analysis revealed that the three Cry1A toxins tested have synergistic effect against C. partellus larvae. In vitro binding analysis of fluorescein isothiocyanate (FITC)-labelled Cry1A toxins to midgut brush border membrane vesicle (BBMV) shows that increase in toxicity is directly correlated to an increase in binding of toxin mix. Conclusions: A high Cry1Ac to Cry1Ab ratio leads to an increase in efficacy of these toxins towards C. partellus larvae and this increase in toxicity comes from an increase in toxin binding. Significance and Impact of the Study: Use of Cry1Ab and Cry1Ac combination could be an effective approach to control C. partellus. Furthermore, we show it first time that possible reason behind increase in toxicity of synergistic Cry1A proteins is an increase in toxin binding.

Chilo

Bacillus thuringiensis

Cry1Ac

Brush border

10.1111/j.1472-765x.2010.02856.x

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Citations (45)

Enhanced Toxicity of Purified Bacillus thuringiensis Cry1Ac-endotoxin

Current Trends in Biotechnology and Pharmacy (2015)

Vivek Kumar Singh Vikrant Nain Priyanka Sharma K. R. S. Sambasiva Rao Ananta Birah

Use of Cry1Ac δ-endotoxin of Bacillus thuringiensis (Bt) has revolutionized crop protection especially in cotton. Large quantities of Cry1Ac protein are needed for several basic studies. Heterologous expression in E. coli facilitates production of large quantities of recombinant Cry1Ac protein. However, earlier studies reported that E. coli expressed recombinant protein leads to large variations in LC50 values. Here we report a method of active Cry1Ac δ-endotoxin purification that is simple, robust and exhibits higher toxicity with consistent results in insect bioassays. In this protocol proteolysis separates completely folded Cry1Ac δ-endotoxin molecules (active toxin) from nonnative protein folding forms and other host proteins, followed by extraction of active Cry1Ac toxin by micro filtration. Insect bioassay of purified Cry1Ac toxin with Helicoverpa armigera showed 125 times enhanced toxicity (LC50 40 pg/cm2) as compared to the earlier reports (LC50 ng/cm2) 4.5 to 3500 ng/cm2. These results provide a new prospective in determination of baseline susceptibility, monitoring resistance development and utilization of its potential.

Cry1Ac

Bacillus thuringiensis

Heterologous

Source

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Citations (0)

Rapamycin and Torin2 inhibit Candida auris TOR: Insights through growth profiling, docking, and MD simulations

Journal of Biomolecular Structure and Dynamics (2022)

Biswambhar Biswas Garima Gangwar Vikrant Nain Ishaan Gupta Anil Thakur

The fungus Candida auris is a pathogen of utmost concern due to its rapid emergence across the globe, acquired antifungal drug tolerance, thermotolerance, and ability to survive in hospital settings and preserved foods. Recent incidences of comorbidity of corona patients with its infection in hospital settings highlighted the importance of understanding the pathobiology and drug tolerance of this fungus on priority. The Target of rapamycin (TOR) is a central regulator of growth across eukaryotes with an illustrated role in fungal pathology. The role of the TOR signalling pathway in the growth of C. auris is yet to be described. In-silico, analysis revealed the presence of highly conserved Tor kinase, components of TORC, and key downstream components in C. auris. Rapamycin and Torin2, the specific inhibitors of Tor reduce the growth of C. auris. An inhibition of Tor leads to cell cycle arrest at the G1 phase with a defect in cytokinesis. Interestingly, with an insignificant difference in growth at 30 and 37 °C, a sharp decline in growth is seen with Torin2 at 37 °C. The heterogeneous response emphasizes the importance of physiology-based differential cellular response at different temperatures. In addition, the inhibition of Tor suppresses the biofilm formation. In silico studies through docking and simulations showed rapamycin and torin2 as specific inhibitors of C. auris Tor kinase (CauTor kinase) and hence can be exploited for a thorough understanding of the TOR signalling pathway in pathobiology and drug tolerance of C. auris. HIGHLIGHTSConservation of TOR signalling pathway in Candida aurisRapamycin and torin2 are specific inhibitors of Cau TorUnderstanding of the role of TOR signalling pathway through the use of inhibitors rapamycin and torin2.Heterogenous response of C. auris to torin2 at different physiological conditions.Communicated by Ramaswamy H. Sarma

Candida auris

TOR signaling

Antifungal drugs

Drug Development

Drug repositioning

Docking (animal)

10.1080/07391102.2022.2134927

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Citations (12)

In silico identification and evaluation of Bacillus subtilis cold shock protein B (cspB)-like plant RNA chaperones

Journal of Biomolecular Structure and Dynamics (2020)

Suman Rani Meenakshi Chaudhary Vikrant Nain

Cold shock domain (CSD) proteins with nucleic acid binding properties are well conserved from bacteria to higher organisms. In bacteria, the cold shock proteins (CSPs) are single domain RNA chaperones, whereas in animals and plants, CSDs are accompanied by additional domains with roles in transcription regulation. Bacterial CSPs (Escherischia coli-cspA and Bacilus subtilis-cspB) have successfully imparted drought tolerance in transgenic plants; however, these cannot be deployed in food crops due to their low public acceptance of transgenics with bacterial genes. Therefore, this study aimed to identify CSPB-like proteins from plants that can be used for developing drought tolerant transgenic crops. Twelve single domain plant CSPs presenting >40% sequence identity with CSPB were identified. All 12 plant CSPs were modeled by homology modeling and refined by molecular dynamics simulation for 10 ns. Selected plant CSPs and CSPB exhibited high structural similarity (Tm-score: 0.63–0.86). Structure based phylogenetic analysis revealed that Triticum aestivum-csp1 and Aegilops tauschii-cspE are structurally closer to CSPB compared to their orthologs and paralogs. Molecular docking with three RNA molecules (5U, UC3U, and C2UC) indicates that Ricinus communis-csd1 and T. aestivum-csp1 have a binding pattern and docking scores similar to those of CSPB. Furthermore, MD simulations for 20 ns and analysis of RMSD, RMSF, Rg as well as the number of hydrogen bonds in all the three complexes revealed that plant CSP-RNA complexes behave in a similar manner to that of the CSPB-RNA complex, making them highly potential candidate genes for developing drought tolerance in transgenic plants. Communicated by Ramaswamy H. Sarma

Cold-shock domain

Docking (animal)

10.1080/07391102.2020.1719198

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Citations (2)

Optimization of fermentation condition for co-production of ethanol and 2,3-butanediol (2,3-BD) from hemicellolosic hydrolysates by Klebsiella oxytoca XF7

Chemical Engineering Communications (2018)

Anamika Sharma Vikrant Nain Rameshwar Tiwari Surender Singh Lata Nain

Microbial production of ethanol and 2,3-butanediol (2,3-BD) from agro-residues has been attracting interest because of their applications in various industries, including generation of biofuel molecules. In the present investigation, the hemicellulosic fraction of corncob was hydrolyzed by indigenous holocellulase from novel psychrotolerant Aspergillus niger SH3 resulting in high xylose release (34.61 g L−1), followed by the bioconversion of xylose to ethanol and 2,3-BD. Taguchi design was adopted to optimize the process which resulted in 5.25- and 3.31-fold increase in 2,3-BD (12.18 ± 0.53 g L−1) and ethanol (4.08 ± 0.03 g L−1), as compared with un-optimized condition. For the first time, co-production of ethanol and 2,3-BD from the corncob hemicellulosic hydrolysate was performed using a newly isolated Klebsiella oxytoca XF7 strain, under the optimized fermentation conditions. These results suggest that K. oxytoca XF7 is a promising candidate for co-production of ethanol and 2,3-BD, with high xylose conversion efficiency (96.65%), facilitating the economical production of biofuel molecules.

2,3-Butanediol

Klebsiella oxytoca

Bioconversion

Corncob

Ethanol Fermentation

Butanediol

10.1080/00986445.2017.1398743

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Citations (13)