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2. Unveiling and harnessing the human gut microbiome in the rising burden of non-communicable diseases during urbanization

Author

Huang, Ziyu, primary, Li, Yue, additional, Park, Heekuk, additional, Ho, Martin, additional, Bhardwaj, Kanchan, additional, Sugimura, Naoki, additional, Lee, Hye Won, additional, Meng, Huicui, additional, Ebert, Matthias P., additional, Chao, Kang, additional, Burgermeister, Elke, additional, Bhatt, Aadra P., additional, Shetty, Sudarshan A., additional, Li, Kai, additional, Wen, Weiping, additional, and Zuo, Tao, additional

Published
2023
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5. Physiological and biochemical evaluation of high anthocyanin pigmented tea (Camellia sinensis L. O. Kuntze) germplasm for purple tea production

Author

Patel, Pradeep Kumar, primary, Siddiqui, Shahida Anusha, additional, Kuča, Kamil, additional, Sabhapondit, Santanu, additional, Sarma, Rupak, additional, Gogoi, Boby, additional, Singh, Shobhit Kumar, additional, Bordoloi, Ranjeet Kumar, additional, Saikia, Jayanta Kumar, additional, Gogoi, Romen Chandra, additional, Bhardwaj, Kanchan, additional, Yang, Jie, additional, Tao, Yang, additional, Manickam, Sivakumar, additional, and Das, Buddhadeb, additional

Published
2022
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8. Phyto-Enrichment of Yogurt to Control Hypercholesterolemia: A Functional Approach

Author

Kumar, Harsh, primary, Bhardwaj, Kanchan, additional, Cruz-Martins, Natália, additional, Sharma, Ruchi, additional, Siddiqui, Shahida Anusha, additional, Dhanjal, Daljeet Singh, additional, Singh, Reena, additional, Chopra, Chirag, additional, Dantas, Adriana, additional, Verma, Rachna, additional, Dosoky, Noura S., additional, and Kumar, Dinesh, additional

Published
2022
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10. A Literature-Based Update on Benincasa hispida (Thunb.) Cogn.: Traditional Uses, Nutraceutical, and Phytopharmacological Profiles

Author

Islam, Muhammad Torequl, primary, Quispe, Cristina, additional, El-Kersh, Dina M., additional, Shill, Manik Chandra, additional, Bhardwaj, Kanchan, additional, Bhardwaj, Prerna, additional, Sharifi-Rad, Javad, additional, Martorell, Miquel, additional, Hossain, Rajib, additional, Al-Harrasi, Ahmed, additional, Al-Rawahi, Ahmed, additional, Butnariu, Monica, additional, Rotariu, Lia Sanda, additional, Suleria, Hafiz Ansar Rasul, additional, Taheri, Yasaman, additional, Docea, Anca Oana, additional, Calina, Daniela, additional, and Cho, William C., additional

Published
2021
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11. Applications of Fruit Polyphenols and Their Functionalized Nanoparticles Against Foodborne Bacteria: A Mini Review

Author

Kumar, Harsh, primary, Bhardwaj, Kanchan, additional, Cruz-Martins, Natália, additional, Nepovimova, Eugenie, additional, Oleksak, Patrik, additional, Dhanjal, Daljeet Singh, additional, Bhardwaj, Sonali, additional, Singh, Reena, additional, Chopra, Chirag, additional, Verma, Rachna, additional, Chauhan, Prem Parkash, additional, Kumar, Dinesh, additional, and Kuča, Kamil, additional

Published
2021
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12. Potential Usage of Edible Mushrooms and Their Residues to Retrieve Valuable Supplies for Industrial Applications

Author

Kumar, Harsh, primary, Bhardwaj, Kanchan, additional, Sharma, Ruchi, additional, Nepovimova, Eugenie, additional, Cruz-Martins, Natália, additional, Dhanjal, Daljeet Singh, additional, Singh, Reena, additional, Chopra, Chirag, additional, Verma, Rachna, additional, Abd-Elsalam, Kamel A., additional, Tapwal, Ashwani, additional, Musilek, Kamil, additional, Kumar, Dinesh, additional, and Kuča, Kamil, additional

Published
2021
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13. Conifers Phytochemicals: A Valuable Forest with Therapeutic Potential

Author

Bhardwaj, Kanchan, primary, Silva, Ana Sanches, additional, Atanassova, Maria, additional, Sharma, Rohit, additional, Nepovimova, Eugenie, additional, Musilek, Kamil, additional, Sharma, Ruchi, additional, Alghuthaymi, Mousa A., additional, Dhanjal, Daljeet Singh, additional, Nicoletti, Marcello, additional, Sharma, Bechan, additional, Upadhyay, Navneet Kumar, additional, Cruz-Martins, Natália, additional, Bhardwaj, Prerna, additional, and Kuča, Kamil, additional

Published
2021
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14. Detection of bacterial pathogens and antibiotic residues in chicken meat: a review

Author

Kumar, Harsh, Bhardwaj, Kanchan, Kaur, Talwinder, Nepovimova, Eugenie, Kuča, Kamil, Kumar, Vinod, Bhatia, Shashi Kant, Dhanjal, Daljeet Singh, Chopra, Chirag, Singh, Reena, Guleria, Shivani, Bhalla, Tek Chand, Verma, Rachna, and Kumar, Dinesh

Subjects
multidrug‐resistant bacteria, chromatography‐based method, immunology‐based method, chicken, molecular‐based methods, biosensors, antibiotics
Abstract

Detection of pathogenic microbes as well as antibiotic residues in food animals, especially in chicken, has become a matter of food security worldwide. The association of various pathogenic bacteria in different diseases and selective pressure induced by accumulated antibiotic residue to develop antibiotic resistance is also emerging as the threat to human health. These challenges have made the containment of pathogenic bacteria and early detection of antibiotic residue highly crucial for robust and precise detection. However, the traditional culture-based approaches are well-comprehended for identifying microbes. Nevertheless, because they are inadequate, time-consuming and laborious, these conventional methods are not predominantly used. Therefore, it has become essential to explore alternatives for the easy and robust detection of pathogenic microbes and antibiotic residue in the food source. Presently, different monitoring, as well as detection techniques like PCR-based, assay (nucleic acid)-based, enzyme-linked immunosorbent assays (ELISA)-based, aptamer-based, biosensor-based, matrix-assisted laser desorption/ionization-time of flight mass spectrometry-based and electronic nose-based methods, have been developed for detecting the presence of bacterial contaminants and antibiotic residues. The current review intends to summarize the different techniques and underline the potential of every method used for the detection of bacterial pathogens and antibiotic residue in chicken meat.

Published
2020

17. Conifer-Derived Metallic Nanoparticles: Green Synthesis and Biological Applications

Author

Bhardwaj, Kanchan, primary, Dhanjal, Daljeet Singh, additional, Sharma, Anirudh, additional, Nepovimova, Eugenie, additional, Kalia, Anu, additional, Thakur, Shabnam, additional, Bhardwaj, Sonali, additional, Chopra, Chirag, additional, Singh, Reena, additional, Verma, Rachna, additional, Kumar, Dinesh, additional, Bhardwaj, Prerna, additional, and Kuča, Kamil, additional

Published
2020
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18. Fruit Extract Mediated Green Synthesis of Metallic Nanoparticles: A New Avenue in Pomology Applications

Author

Kumar, Harsh, primary, Bhardwaj, Kanchan, additional, Dhanjal, Daljeet Singh, additional, Nepovimova, Eugenie, additional, Șen, Fatih, additional, Regassa, Hailemeleak, additional, Singh, Reena, additional, Verma, Rachna, additional, Kumar, Vinod, additional, Kumar, Dinesh, additional, Bhatia, Shashi Kant, additional, and Kuča, Kamil, additional

Published
2020
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20. Detection of Bacterial Pathogens and Antibiotic Residues in Chicken Meat: A Review

Author

Kumar, Harsh, primary, Bhardwaj, Kanchan, additional, Kaur, Talwinder, additional, Nepovimova, Eugenie, additional, Kuča, Kamil, additional, Kumar, Vinod, additional, Bhatia, Shashi Kant, additional, Dhanjal, Daljeet Singh, additional, Chopra, Chirag, additional, Singh, Reena, additional, Guleria, Shivani, additional, Bhalla, Tek Chand, additional, Verma, Rachna, additional, and Kumar, Dinesh, additional

Published
2020
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29. Identification, Purification, and Characterization of a Thermally Stable Lipase from Rice Bran. A New Member of the (Phospho) Lipase Family1

Author

Bhardwaj, Kanchan, Raju, Aruna, and Rajasekharan, Ram

Subjects
Detergents, Temperature, Lysophosphatidylcholines, Oryza, Lipase, Hydrogen-Ion Concentration, Phospholipases A, Substrate Specificity, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Enzyme Stability, Seeds, Electrophoresis, Gel, Two-Dimensional, Chromatography, High Pressure Liquid, Triolein, Research Article
Abstract

A thermally stable lipase (EC 3.1.1.3.) was first identified in rice (Oryza sativa) bran, and the enzyme was purified to homogeneity using octyl-Sepharose chromatography. The enzyme was purified to 7.6-fold with the final specific activity of 0.38 micromol min(-1) mg(-1) at 80 degrees C using [9,10-(3)H]triolein as a substrate. The purified enzyme was found to be a glycoprotein of 9.4 kD. Enzyme showed a maximum activity at 80 degrees C and at pH 11.0. The protein was biologically active and retained most of its secondary structure even at 90 degrees C as judged by the enzymatic assays and far-ultraviolet circular dichroism spectroscopy, respectively. Differential scanning calorimetric studies indicated that the transition temperature was 76 degrees C and enthalpy 1.3 x 10(5) Calorie mol(-1) at this temperature. The purified lipase also exhibited phospholipase A(2) activity. Colocalization of both the hydrolytic activities in reverse-phase high-performance liquid chromatography and isoelectric focusing showed that the dual activity was associated with a single protein. Further, a direct interaction between both the substrates and the purified protein was demonstrated by photoaffinity labeling, using chemically synthesized analogs of triolein and phosphatidylcholine (PC). Apparent K(m) for triolein (6.71 mM) was higher than that for PC (1.02 mM). The enzyme preferentially hydrolyzed the sn-2 position of PC, whereas it apparently exhibited no positional specificity toward triacylglycerol. Diisopropyl fluorophosphate inhibited both lipase and phospholipase activities of the purified enzyme. This enzyme is a new member from plants in the family of lipases capable of hydrolyzing phospholipids.

Published
2001

33. Variations on the tmRNA gene

Author

Mao, Chunhong, primary, Bhardwaj, Kanchan, additional, Sharkady, Stephen M., additional, Fish, Robert I., additional, Driscoll, Timothy, additional, Wower, Jacek, additional, Zwieb, Christian, additional, Sobral, Bruno W. S., additional, and Williams, Kelly P., additional

Published
2009
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38. Biochemical and Functional Analyses of the Human Toll-like Receptor 3 Ectodomain

Author

Ranjith-Kumar, C.T., primary, Miller, William, additional, Xiong, Jin, additional, Russell, William K., additional, Lamb, Roberta, additional, Santos, Jonathan, additional, Duffy, Karen E., additional, Cleveland, Larissa, additional, Park, Mary, additional, Bhardwaj, Kanchan, additional, Wu, Zhaoxiang, additional, Russell, David H., additional, Sarisky, Robert T., additional, Mbow, M. Lamine, additional, and Kao, C. Cheng, additional

Published
2007
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42. LL37 and Cationic Peptides Enhance TLR3 Signaling by Viral Double-stranded RNAs.

Author

Yvonne Lai, Adhikarakunnathu, Sreedevi, Bhardwaj, Kanchan, Ranjith-Kumar, C. T., Yahong Wen, Jordan, Jarrat L., Wu, Linda H., Dragnea, Bogdan, Mateo, Lani San, and Kao, C. Cheng

Subjects
PEPTIDES, PROTEINS, DOUBLE-stranded RNA, PEPTIDE antibiotics, EXFOLIATIVE cytology
Abstract

Background: Toll-like Receptor 3 (TLR3) detects viral dsRNA during viral infection. However, most natural viral dsRNAs are poor activators of TLR3 in cell-based systems, leading us to hypothesize that TLR3 needs additional factors to be activated by viral dsRNAs. The anti-microbial peptide LL37 is the only known human member of the cathelicidin family of antimicrobial peptides. LL37 complexes with bacterial lipopolysaccharide (LPS) to prevent activation of TLR4, binds to ssDNA to modulate TLR9 and ssRNA to modulate TLR7 and 8. It synergizes with TLR2/1, TLR3 and TLR5 agonists to increase IL8 and IL6 production. This work seeks to determine whether LL37 enhances viral dsRNA recognition by TLR3. Methodology/Principal Findings: Using a human bronchial epithelial cell line (BEAS2B) and human embryonic kidney cells (HEK 293T) transiently transfected with TLR3, we found that LL37 enhanced poly(I:C)-induced TLR3 signaling and enabled the recognition of viral dsRNAs by TLR3. The presence of LL37 also increased the cytokine response to rhinovirus infection in BEAS2B cells and in activated human peripheral blood mononuclear cells. Confocal microscopy determined that LL37 could co-localize with TLR3. Electron microscopy showed that LL37 and poly(I:C) individually formed globular structures, but a complex of the two formed filamentous structures. To separate the effects of LL37 on TLR3 and TLR4, other peptides that bind RNA and transport the complex into cells were tested and found to activate TLR3 signaling in response to dsRNAs, but had no effect on TLR4 signaling. This is the first demonstration that LL37 and other RNA-binding peptides with cell penetrating motifs can activate TLR3 signaling and facilitate the recognition of viral ligands. Conclusions/Significance: LL37 and several cell-penetrating peptides can enhance signaling by TLR3 and enable TLR3 to respond to viral dsRNA. [ABSTRACT FROM AUTHOR]

Published
2011
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43. Viral Double-Strand RNA-Binding Proteins Can Enhance Innate Immune Signaling by Toll-Like Receptor 3.

Author

Yvonne Lai, Guanghui Yi, Chen, Alice, Bhardwaj, Kanchan, Tragesser, Brady J., Valverde, Rodrigo A., Zlotnick, Adam, Mukhopadhyay, Suchetana, Ranjith-Kumar, C. T., and Kao, C. Cheng

Subjects
CARRIER proteins, IMMUNE response, GENETIC polymorphisms, CELLULAR immunity, EPITHELIAL cells, RNA viruses
Abstract

Toll-like Receptor 3 (TLR3) detects double-stranded (ds) RNAs to activate innate immune responses. While poly(I:C) is an excellent agonist for TLR3 in several cell lines and in human peripheral blood mononuclear cells, viral dsRNAs tend to be poor agonists, leading to the hypothesis that additional factor(s) are likely required to allow TLR3 to respond to viral dsRNAs. TLR3 signaling was examined in a lung epithelial cell line by quantifying cytokine production and in human embryonic kidney cells by quantifying luciferase reporter levels. Recombinant 1b hepatitis C virus polymerase was found to enhance TLR3 signaling in the lung epithelial BEAS-2B cells when added to the media along with either poly(I:C) or viral dsRNAs. The polymerase from the genotype 2a JFH-1 HCV was a poor enhancer of TLR3 signaling until it was mutated to favor a conformation that could bind better to a partially duplexed RNA. The 1b polymerase also co-localizes with TLR3 in endosomes. RNA-binding capsid proteins (CPs) from two positive-strand RNA viruses and the hepadenavirus hepatitis B virus (HBV) were also potent enhancers of TLR3 signaling by poly(I:C) or viral dsRNAs. A truncated version of the HBV CP that lacked an arginine-rich RNA-binding domain was unable to enhance TLR3 signaling. These results demonstrate that several viral RNA-binding proteins can enhance the dsRNA-dependent innate immune response initiated by TLR3. [ABSTRACT FROM AUTHOR]

Published
2011
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44. Biochemical and Genetic Analyses of Murine Hepatitis Virus Nsp15 Endoribonuclease.

Author

Hyojeung Kang, Bhardwaj, Kanchan, Yi Li, Palaninathan, Satheesh, Sacchettini, James, Guarino, Linda, Leibowitz, Julian L., and C. Cheng Kao

Subjects
*HEPATITIS viruses, *BIOCHEMISTRY, *VIRAL genetics, *RIBONUCLEASES, *ALANINE, *VIRAL proteins
Abstract

The goal of this project was to better define the relationship between the endoribonuclease activity of murine hepatitis virus (MHV) Nsp15 (mNsp15) and its role in virus infection. Molecular modeling demonstrated that the catalytic residues of mNsp15 are superimposable with its severe acute respiratory syndrome coronavirus ortholog. Alanine substitutions at three key residues in the mNsp15 catalytic pocket (H262, H277, and G275) and a double-mutant version (H262P and H277A) generated proteins with greatly reduced but detectable endoribonuclease activities. Furthermore, these mutant proteins demonstrated lower cleavage specificities for uridylate than wild-type (WT) mNsp15. These mutations were successfully incorporated into viruses named vH262A, vH277A, vG275A, and vH262P+H277A. All four mutant viruses formed plaques with diameters similar to that of MHV-A59 1000 (WT virus) on several different cell lines. Interestingly, viruses with a mutation at a noncatalytic residue, D324A, could not be recovered despite repeated attempts, and expression of mNsp15 containing the D324A mutation in Escherichia coli resulted in an insoluble protein. Plaques derived from vH262A produced approximately 6- to 13-fold fewer PFU than those from WT virus. Cells infected with mNsp15 mutant viruses accumulated lesser amounts of plus- and minus-sense subgenomic RNAs and spike protein than WT virus. The expression of mNsp15 in trans by transient transfection partially restored RNA synthesis by vH262A. These results demonstrate that mNsp15 is required for optimal infection by MHV. [ABSTRACT FROM AUTHOR]

Published
2007
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45. Anti-Diabetic, Anti-Cholinesterase, and Anti-Inflammatory Potential of Plant Derived Extracts and Column Semi-Purified Fractions of Ficus benghalensis .

Author

Rauf A, Almasoud N, Ibrahim M, Alomar TS, Khalil AA, Khursheed T, Khan MU, Jan MS, Bhardwaj K, Iriti M, and Sharma R

Subjects
Plant Leaves chemistry, Butyrylcholinesterase metabolism, Glycoside Hydrolase Inhibitors pharmacology, Glycoside Hydrolase Inhibitors isolation & purification, alpha-Amylases antagonists & inhibitors, Lipoxygenase Inhibitors pharmacology, Lipoxygenase Inhibitors isolation & purification, Acetylcholinesterase metabolism, Arachidonate 5-Lipoxygenase metabolism, Plant Roots chemistry, Ficus chemistry, Plant Extracts pharmacology, Plant Extracts chemistry, Cholinesterase Inhibitors pharmacology, Cholinesterase Inhibitors isolation & purification, Cholinesterase Inhibitors chemistry, Anti-Inflammatory Agents pharmacology, Anti-Inflammatory Agents isolation & purification, Anti-Inflammatory Agents chemistry, Hypoglycemic Agents pharmacology, Hypoglycemic Agents chemistry, Hypoglycemic Agents isolation & purification
Abstract

Background: The present study aimed to investigate the in-vitro anti-diabetic, anti-cholinesterase, and anti-inflammatory potential of extracts from different parts of Ficus benghalensis , including leaves, stem, and roots, as well as isolated column fractions (F-B-1 C, F-B-2 C, F-B-3 C, and F-B-4 C)., Methods: The extracts and subsequent fractions were evaluated for their inhibitory activity against key enzymes involved in diabetes [α-glucosidase and α-amylase], neurodegenerative diseases [acetylcholinesterase and butyrylcholinesterase], and inflammation (cyclooxygenase-2 (COX-2) and 5-lipoxygenase (5-LOX))., Results: The results showed that F. benghalensis leaf extract exhibited the highest α-glucosidase inhibitory activity (73.84%) and α-amylase inhibitory activity (76.29%) at 1000 µg/mL. The stem extract (65.50%) and F-B-2 C fraction (69.67%) also demonstrated significant α-glucosidase inhibitory activity. In terms of anti-cholinesterase activity, the extracts of roots, leaves, and stem showed promising inhibition of acetylcholinesterase (AChE) and butyrylcholinesterase (BChE), with half maximal inhibitory concentration (IC50) values ranging from 50.50 to 474.83 µg/mL. The derived fractions (F-B-1 C, F-B-2 C, F-B-3 C, and F-B-4 C) also exhibited notable inhibition of AChE and BChE, with IC50 values from 91.85 to 337.94 µg/mL. Moreover, the F-B-3 C fraction demonstrated the highest COX-2 inhibitory potential (85.72%), followed by F-B-1 C (83.13%), the stem extract (80.85%), and the leaves extract (79.00%). The F-B-1 C fraction showed the highest 5-LOX inhibitory activity (87.63%), while the root extract exhibited the lowest inhibition (73.39%)., Conclusions: The results demonstrated promising bioactivity, suggesting the potential of F. benghalensis as a source of natural compounds with therapeutic applications. Further studies are required to identify and isolate the active components responsible for these effects and to evaluate their in-vivo efficacy and safety., Competing Interests: The authors declare no conflict of interest. Given his role as Guest Editor and Editorial Board Member of Frontiers in Bioscience-Landmark, Marcello Iriti had no involvement in the peer-review of this article and has no access to information regarding its peer review. Full responsibility for the editorial process for this article was delegated to Jen-Tsung Chen., (© 2024 The Author(s). Published by IMR Press.)

Published
2024
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46. Viral double-strand RNA-binding proteins can enhance innate immune signaling by toll-like Receptor 3.

Author

Lai Y, Yi G, Chen A, Bhardwaj K, Tragesser BJ, Rodrigo A Valverde, Zlotnick A, Mukhopadhyay S, Ranjith-Kumar CT, and Kao CC

Subjects
Capsid Proteins metabolism, Endosomes metabolism, Genotype, HEK293 Cells, Hepacivirus enzymology, Hepacivirus genetics, Humans, Models, Molecular, Poly I-C metabolism, Protein Conformation, Protein Transport, RNA, Viral metabolism, RNA-Dependent RNA Polymerase chemistry, RNA-Dependent RNA Polymerase metabolism, Ross River virus metabolism, Hepacivirus metabolism, Immunity, Innate, RNA, Double-Stranded metabolism, RNA-Binding Proteins metabolism, Signal Transduction immunology, Toll-Like Receptor 3 metabolism, Viral Proteins metabolism
Abstract

Toll-like Receptor 3 (TLR3) detects double-stranded (ds) RNAs to activate innate immune responses. While poly(I:C) is an excellent agonist for TLR3 in several cell lines and in human peripheral blood mononuclear cells, viral dsRNAs tend to be poor agonists, leading to the hypothesis that additional factor(s) are likely required to allow TLR3 to respond to viral dsRNAs. TLR3 signaling was examined in a lung epithelial cell line by quantifying cytokine production and in human embryonic kidney cells by quantifying luciferase reporter levels. Recombinant 1b hepatitis C virus polymerase was found to enhance TLR3 signaling in the lung epithelial BEAS-2B cells when added to the media along with either poly(I:C) or viral dsRNAs. The polymerase from the genotype 2a JFH-1 HCV was a poor enhancer of TLR3 signaling until it was mutated to favor a conformation that could bind better to a partially duplexed RNA. The 1b polymerase also co-localizes with TLR3 in endosomes. RNA-binding capsid proteins (CPs) from two positive-strand RNA viruses and the hepadenavirus hepatitis B virus (HBV) were also potent enhancers of TLR3 signaling by poly(I:C) or viral dsRNAs. A truncated version of the HBV CP that lacked an arginine-rich RNA-binding domain was unable to enhance TLR3 signaling. These results demonstrate that several viral RNA-binding proteins can enhance the dsRNA-dependent innate immune response initiated by TLR3.

Published
2011
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47. Rectal schwannoma.

Author

Bhardwaj K, Bal MS, and Kumar P

Subjects
Adult, Female, Humans, Immunohistochemistry, S100 Proteins analysis, Neurilemmoma diagnosis, Rectal Neoplasms diagnosis
Abstract

Solitary schwannomas constitute only 2%-6% of stromal tumors of the gastrointestinal tract; the stomach is the preferred site of involvement. We report a 35-year-old woman who presented with difficulty in defecation. A mass on the posterior wall of the rectum was excised. Histologically, the lesion was a schwannoma, with S-100 proteins positivity and glial fibrillary acidic protein immunoreactivity. The patient is asymptomatic two years later.

Published
2002

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