Aggarwal G

References (7)

Title : Cyperus rotundus L.: Invasive weed plant with insecticidal potential against Aphis craccivora Koch and Planococcus lilacinus (Cockerell) - Singh_2024_Pestic.Biochem.Physiol_198_105720
Author(s) : Singh R , Gupta H , Anmol , Aggarwal G , Bhattacharyya K , Sharma U , Reddy SGE
Ref : Pestic Biochem Physiol , 198 :105720 , 2024
Abstract : Cyperus rotundus L. is a widely distributed invasive weed plant with vast traditional medicinal uses. Herein, the methanolic root extract of C. rotundus and its fractions (n-hexane, chloroform, n-butanol, and aqueous) were evaluated for insecticidal activity against nymphs of Aphis craccivora Koch and crawlers of Planococcus lilacinus (Cockerell) to find promising lead (s). In contact topical assay, among extract/fractions, n-hexane fraction exhibited more toxicity against A. craccivora (LD(50) = 1.12 microg/insect) and P. lilacinus (LD(50) = 0.94 microg/insect). The chemical analysis of n-hexane fraction revealed a volatile composition similar to that of the essential oil (EO) of C. rotundus roots. Hence, EO was extracted using water and deep eutectic solvents (DESs) as cosolvent, which revealed enhancement in EO yield (from 0.28 to 0.46% w/w) on implementing DESs. A total of 35 diverse volatile metabolites were identified in all EO samples, accounting for 85.0 to 91.8% of chemical composition, having cyperotundone, cyperene mustakone, isolongifolen-5-one, boronia butenal as major constituents. The EO obtained with DES-7 [choline chloride: ethylene glycol (1:4)] and DES-6 [choline chloride: lactic acid (1:3)] were found effective against A. craccivora (LD(50) = 0.62-0.87 microg/insect) and P. lilacinus (LD(50)= 0.59-0.67 microg/insect) after 96 h. NMR analysis of EO revealed cyperotundone as a major compound, which was isolated along with cyperene and cyperene epoxide. All the molecules were found effective against P. lilacinus, whereas against A. craccivora cyperotundone, cyperene and cyperene epoxide showed promising toxicity (LD(50) = 0.74-0.86 microg/insect). Extract/fractions, EO, and isolated molecules showed a significant reproductive inhibition rate of A. craccivora at higher concentrations. All the tested concentrations of cyperotundone showed significant inhibition of acetylcholinesterase (AChE) and glutathione-S-transferase (GST) in A. craccivora and P. lilacinus. Based upon the present study, C. rotundus can be recommended to control targeted insects in the greenhouse/field conditions after performing bio-efficacy and phytotoxicity studies.
ESTHER : Singh_2024_Pestic.Biochem.Physiol_198_105720
PubMedSearch : Singh_2024_Pestic.Biochem.Physiol_198_105720
PubMedID: 38225075

Title : Refolded Recombinant Human Paraoxonase 1 Variant Exhibits Prophylactic Activity Against Organophosphate Poisoning - Bajaj_2016_Appl.Biochem.Biotechnol_180_165
Author(s) : Bajaj P , Tripathy RK , Aggarwal G , Datusalia AK , Sharma SS , Pande AH
Ref : Appl Biochem Biotechnol , 180 :165 , 2016
Abstract : Organophosphate (OP) compounds are neurotoxic chemicals, and current treatments available for OP-poisoning are considered as unsatisfactory and inadequate. There is an urgent need for the development of more effective treatment(s) for OP-poisoning. Human paraoxonase 1 (h-PON1) is known to hydrolyze a variety of OP-compounds and is a leading candidate for the development of prophylactic and therapeutic agent against OP-poisoning in humans. Non-availability of effective system(s) for the production of recombinant h-PON1 (rh-PON1) makes it hard to produce improved variant(s) of this enzyme and analyze their in vivo efficacy in animal models. Production of recombinant h-PON1 (rh-PON1) using an Escherichia coli expression system is a key to develop variant(s) of h-PON1. Recently, we have developed a procedure to produce active rh-PON1 enzymes by using E. coli expression system. In this study, we have characterized the OP-hydrolyzing properties of refolded rh-PON1(wt) and rh-PON1(H115W;R192K) variant. Our results show that refolded rh-PON1(H115W;R192K) variant exhibit enhanced OP-hydrolyzing activity in in vitro and ex vivo assays and exhibited prophylactic activity in mouse model of OP-poisoning, suggesting that refolded rh-PON1 can be developed as a therapeutic candidate.
ESTHER : Bajaj_2016_Appl.Biochem.Biotechnol_180_165
PubMedSearch : Bajaj_2016_Appl.Biochem.Biotechnol_180_165
PubMedID: 27131877

Title : Expression and purification of biologically active recombinant human paraoxonase 1 from inclusion bodies of Escherichia coli - Bajaj_2015_Protein.Expr.Purif_115_95
Author(s) : Bajaj P , Tripathy RK , Aggarwal G , Pande AH
Ref : Protein Expr Purif , 115 :95 , 2015
Abstract : Human PON1 (h-PON1) is a Ca(2+)-dependent serum enzyme and can hydrolyze (and inactivate) a wide range of substrates. It is a multifaceted enzyme and exhibit anti-inflammatory, anti-oxidative, anti-atherogenic, anti-diabetic, anti-microbial, and organophosphate (OP)-detoxifying properties. Thus, h-PON1 is a strong candidate for the development of therapeutic intervention against these conditions in humans. Insufficient hydrolyzing activity of native h-PON1 against desirable substrate affirms the urgent need to develop improved variant(s) of h-PON1 having enhanced activity. Production of recombinant h-PON1 (rh-PON1) using an Escherichia coli expression system is a key to develop such variant(s). However, generation of rh-PON1 using E. coli expression system has been elusive until now because of the aggregation of over-expressed rh-PON1 protein in inactive form as inclusion bodies (IBs) in the bacterial cells. In this study, we have over-expressed rh-PON1(wt) and rh-PON1(H115W;R192K) proteins as IBs in E. coli, and refolded the inactive enzymes present in the IBs to their active form using in vitro refolding. The active enzymes were isolated from the refolding mixture by ion-exchange chromatography. The catalytic properties of the refolded enzymes were similar to their soluble counterparts. Our results show that the pure and the active variant of rh-PON1 enzyme having enhanced hydrolyzing activity can be produced in large quantities using E. coli expression system. This method can be used for the industrial scale production of rh-PON1 enzymes and will aid in developing h-PON1 as a therapeutic candidate.
ESTHER : Bajaj_2015_Protein.Expr.Purif_115_95
PubMedSearch : Bajaj_2015_Protein.Expr.Purif_115_95
PubMedID: 26003526

Title : Characterization of human paraoxonase 1 variants suggest that His residues at 115 and 134 positions are not always needed for the lactonase\/arylesterase activities of the enzyme - Bajaj_2013_Protein.Sci_22_1799
Author(s) : Bajaj P , Tripathy RK , Aggarwal G , Pande AH
Ref : Protein Science , 22 :1799 , 2013
Abstract : Human paraoxonase 1 (h-PON1) hydrolyzes variety of substrates and the hydrolytic activities of enzyme can be broadly grouped into three categories; arylesterase, phosphotriesterase, and lactonase. Current models of the catalytic mechanism of h-PON1 suggest that catalytic residues H115 and H134 mediate the lactonase and arylesterase activities of the enzyme. H-PON1 is a strong candidate for the development of catalytic bioscavenger for organophosphate poisoning in humans. Recently, Gupta et al. (Nat. Chem. Biol. 2011. 7, 120) identified amino acid substitutions that significantly increased the activity of chimeric-PON1 variant (4E9) against some organophosphate nerve agents. In this study we have examined the effect of these (L69G/S111T/H115W/H134R/R192K/F222S/T332S) and other substitutions (H115W/H134R and H115W/H134R/R192K) on the hydrolytic activities of recombinant h-PON1 (rh-PON1) variants. Our results show that the substitutions resulted in a significant increase in the organophosphatase activity of all the three variants of rh-PON1 enzyme while had a variable effect on the lactonase/arylesterase activities. The results suggest that H residues at positions 115 and 134 are not always needed for the lactonase/arylesterase activities of h-PON1 and force a reconsideration of the current model(s) of the catalytic mechanism of h-PON1.
ESTHER : Bajaj_2013_Protein.Sci_22_1799
PubMedSearch : Bajaj_2013_Protein.Sci_22_1799
PubMedID: 24123308

Title : The genome sequence of Trypanosoma cruzi, etiologic agent of Chagas disease - El-Sayed_2005_Science_309_409
Author(s) : El-Sayed NM , Myler PJ , Bartholomeu DC , Nilsson D , Aggarwal G , Tran AN , Ghedin E , Worthey EA , Delcher AL , Blandin G , Westenberger SJ , Caler E , Cerqueira GC , Branche C , Haas B , Anupama A , Arner E , Aslund L , Attipoe P , Bontempi E , Bringaud F , Burton P , Cadag E , Campbell DA , Carrington M , Crabtree J , Darban H , da Silveira JF , de Jong P , Edwards K , Englund PT , Fazelina G , Feldblyum T , Ferella M , Frasch AC , Gull K , Horn D , Hou L , Huang Y , Kindlund E , Klingbeil M , Kluge S , Koo H , Lacerda D , Levin MJ , Lorenzi H , Louie T , Machado CR , McCulloch R , McKenna A , Mizuno Y , Mottram JC , Nelson S , Ochaya S , Osoegawa K , Pai G , Parsons M , Pentony M , Pettersson U , Pop M , Ramirez JL , Rinta J , Robertson L , Salzberg SL , Sanchez DO , Seyler A , Sharma R , Shetty J , Simpson AJ , Sisk E , Tammi MT , Tarleton R , Teixeira S , Van Aken S , Vogt C , Ward PN , Wickstead B , Wortman J , White O , Fraser CM , Stuart KD , Andersson B
Ref : Science , 309 :409 , 2005
Abstract : Whole-genome sequencing of the protozoan pathogen Trypanosoma cruzi revealed that the diploid genome contains a predicted 22,570 proteins encoded by genes, of which 12,570 represent allelic pairs. Over 50% of the genome consists of repeated sequences, such as retrotransposons and genes for large families of surface molecules, which include trans-sialidases, mucins, gp63s, and a large novel family (>1300 copies) of mucin-associated surface protein (MASP) genes. Analyses of the T. cruzi, T. brucei, and Leishmania major (Tritryp) genomes imply differences from other eukaryotes in DNA repair and initiation of replication and reflect their unusual mitochondrial DNA. Although the Tritryp lack several classes of signaling molecules, their kinomes contain a large and diverse set of protein kinases and phosphatases; their size and diversity imply previously unknown interactions and regulatory processes, which may be targets for intervention.
ESTHER : El-Sayed_2005_Science_309_409
PubMedSearch : El-Sayed_2005_Science_309_409
PubMedID: 16020725
Gene_locus related to this paper: tryb2-q6h9e3 , tryb2-q6ha27 , tryb2-q38cd5 , tryb2-q38cd6 , tryb2-q38cd7 , tryb2-q38dc1 , tryb2-q38de4 , tryb2-q38ds6 , tryb2-q38dx1 , tryb2-q380z6 , tryb2-q382l4 , tryb2-q383a9 , tryb2-q386e3 , tryb2-q387r7 , tryb2-q388n1 , tryb2-q389w3 , trybr-PEPTB , trycr-q4cq28 , trycr-q4cq94 , trycr-q4cq95 , trycr-q4cq96 , trycr-q4cqq5 , trycr-q4csm0 , trycr-q4cwv3 , trycr-q4cx66 , trycr-q4cxr6 , trycr-q4cyc3 , trycr-q4cyc5 , trycr-q4cyf6 , trycr-q4czy3 , trycr-q4d1s2 , trycr-q4d2n1 , trycr-q4d3a2 , trycr-q4d3x3 , trycr-q4d3y4 , trycr-q4d6h1 , trycr-q4d8h8 , trycr-q4d8h9 , trycr-q4d8i0 , trycr-q4d786 , trycr-q4d975 , trycr-q4da08 , trycr-q4dab1 , trycr-q4dap6 , trycr-q4dap7 , trycr-q4dbm2 , trycr-q4dbn1 , trycr-q4ddw7 , trycr-q4de42 , trycr-q4dhn8 , trycr-q4dkk8 , trycr-q4dkk9 , trycr-q4dm56 , trycr-q4dp03 , trycr-q4dqa6 , trycr-q4dry8 , trycr-q4dt91 , trycr-q4dvl8 , trycr-q4dvp1 , trycr-q4dvp2 , trycr-q4dw34 , trycr-q4dwm3 , trycr-q4dy49 , trycr-q4dy82 , trycr-q4dzp6 , trycr-q4e3m8 , trycr-q4e4t5 , trycr-q4e5d1 , trycr-q4e5z2 , trycr-q6y3z8 , trycr-Q94795 , trycr-TCPO

Title : Comparative genomics of trypanosomatid parasitic protozoa - El-Sayed_2005_Science_309_404
Author(s) : El-Sayed NM , Myler PJ , Blandin G , Berriman M , Crabtree J , Aggarwal G , Caler E , Renauld H , Worthey EA , Hertz-Fowler C , Ghedin E , Peacock C , Bartholomeu DC , Haas BJ , Tran AN , Wortman JR , Alsmark UC , Angiuoli S , Anupama A , Badger J , Bringaud F , Cadag E , Carlton JM , Cerqueira GC , Creasy T , Delcher AL , Djikeng A , Embley TM , Hauser C , Ivens AC , Kummerfeld SK , Pereira-Leal JB , Nilsson D , Peterson J , Salzberg SL , Shallom J , Silva JC , Sundaram J , Westenberger S , White O , Melville SE , Donelson JE , Andersson B , Stuart KD , Hall N
Ref : Science , 309 :404 , 2005
Abstract : A comparison of gene content and genome architecture of Trypanosoma brucei, Trypanosoma cruzi, and Leishmania major, three related pathogens with different life cycles and disease pathology, revealed a conserved core proteome of about 6200 genes in large syntenic polycistronic gene clusters. Many species-specific genes, especially large surface antigen families, occur at nonsyntenic chromosome-internal and subtelomeric regions. Retroelements, structural RNAs, and gene family expansion are often associated with syntenic discontinuities that-along with gene divergence, acquisition and loss, and rearrangement within the syntenic regions-have shaped the genomes of each parasite. Contrary to recent reports, our analyses reveal no evidence that these species are descended from an ancestor that contained a photosynthetic endosymbiont.
ESTHER : El-Sayed_2005_Science_309_404
PubMedSearch : El-Sayed_2005_Science_309_404
PubMedID: 16020724
Gene_locus related to this paper: tryb2-q382c1 , trycr-q4dhv2 , trycr-q4dpt2 , trycr-q4dpy4

Title : The genome of the kinetoplastid parasite, Leishmania major - Ivens_2005_Science_309_436
Author(s) : Ivens AC , Peacock CS , Worthey EA , Murphy L , Aggarwal G , Berriman M , Sisk E , Rajandream MA , Adlem E , Aert R , Anupama A , Apostolou Z , Attipoe P , Bason N , Bauser C , Beck A , Beverley SM , Bianchettin G , Borzym K , Bothe G , Bruschi CV , Collins M , Cadag E , Ciarloni L , Clayton C , Coulson RM , Cronin A , Cruz AK , Davies RM , De Gaudenzi J , Dobson DE , Duesterhoeft A , Fazelina G , Fosker N , Frasch AC , Fraser A , Fuchs M , Gabel C , Goble A , Goffeau A , Harris D , Hertz-Fowler C , Hilbert H , Horn D , Huang Y , Klages S , Knights A , Kube M , Larke N , Litvin L , Lord A , Louie T , Marra M , Masuy D , Matthews K , Michaeli S , Mottram JC , Muller-Auer S , Munden H , Nelson S , Norbertczak H , Oliver K , O'Neil S , Pentony M , Pohl TM , Price C , Purnelle B , Quail MA , Rabbinowitsch E , Reinhardt R , Rieger M , Rinta J , Robben J , Robertson L , Ruiz JC , Rutter S , Saunders D , Schafer M , Schein J , Schwartz DC , Seeger K , Seyler A , Sharp S , Shin H , Sivam D , Squares R , Squares S , Tosato V , Vogt C , Volckaert G , Wambutt R , Warren T , Wedler H , Woodward J , Zhou S , Zimmermann W , Smith DF , Blackwell JM , Stuart KD , Barrell B , Myler PJ
Ref : Science , 309 :436 , 2005
Abstract : Leishmania species cause a spectrum of human diseases in tropical and subtropical regions of the world. We have sequenced the 36 chromosomes of the 32.8-megabase haploid genome of Leishmania major (Friedlin strain) and predict 911 RNA genes, 39 pseudogenes, and 8272 protein-coding genes, of which 36% can be ascribed a putative function. These include genes involved in host-pathogen interactions, such as proteolytic enzymes, and extensive machinery for synthesis of complex surface glycoconjugates. The organization of protein-coding genes into long, strand-specific, polycistronic clusters and lack of general transcription factors in the L. major, Trypanosoma brucei, and Trypanosoma cruzi (Tritryp) genomes suggest that the mechanisms regulating RNA polymerase II-directed transcription are distinct from those operating in other eukaryotes, although the trypanosomatids appear capable of chromatin remodeling. Abundant RNA-binding proteins are encoded in the Tritryp genomes, consistent with active posttranscriptional regulation of gene expression.
ESTHER : Ivens_2005_Science_309_436
PubMedSearch : Ivens_2005_Science_309_436
PubMedID: 16020728
Gene_locus related to this paper: leima-e9ady6 , leima-L2464.12 , leima-L2802.02 , leima-OPB , leima-q4fw33 , leima-q4fwg8 , leima-q4fwj0 , leima-q4fya7 , leima-q4q0a1 , leima-q4q0t5 , leima-q4q0v0 , leima-q4q1h9 , leima-q4q2c9 , leima-q4q4j7 , leima-q4q4t6 , leima-q4q5j1 , leima-q4q6e9 , leima-q4q7v8 , leima-q4q8a8 , leima-q4q9g9 , leima-q4q080 , leima-q4q398 , leima-q4q615 , leima-q4q819 , leima-q4q871 , leima-q4q942 , leima-q4qae7 , leima-q4qb85 , leima-q4qdz7 , leima-q4qe26 , leima-q4qe31 , leima-q4qe85 , leima-q4qe86 , leima-q4qe87 , leima-q4qe90 , leima-q4qec8 , leima-q4qgz4 , leima-q4qgz5 , leima-q4qhs0 , leima-q4qj45