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At least 253 records · Page 14Linked to original sources
PubMed2000

Biotransformation of gamma-terpinene and (-)-alpha-phellandrene by the larvae of common cutworm (Spodoptera litura).

gamma-Terpinene was mixed in artificial diet at a concentration of 1 mg/g of diet, and the diet was fed to the last instar larvae of common cutworm (Spodoptera litura). Metabolites were recovered from frass and analyzed spectroscopically. gamma-Terpinene was transformed mainly to p-mentha-1,4-dien-7-oic acid and p-cymen-7-oic acid (cumic acid). Similarly, (-)-alpha-phellandrene was transformed mainly to (4R)-p-mentha-1,5-dien-7-oic acid and p-cymen-7-oic acid (cumic acid). The C-7 position (allylic methyl group) of gamma-terpinene and (-)-alpha-phellandrene was preferentially oxidized.

Animals↗
PubMed2000

Biotransformation of beta-myrcene by the larvae of common cutworm (Spodoptera litura).

beta-Myrcene was mixed in an artificial diet at a concentration of 1 mg/g of diet, and the diet was fed to the last instar larvae of common cutworm (Spodoptera litura). Metabolites were recovered from frass and analyzed spectroscopically. beta-Myrcene was transformed mainly to myrcene-3(10)-glycol and myrcene-1,2-glycol. Each pair of double bonds of beta-myrcene was converted to the corresponding diol by oxidation, respectively. The 3,10- and 1,2-double bonds of beta-myrcene were respectively oxidized.

Acyclic Monoterpenes↗
PubMed2000

Growth inhibitory effects on fall armyworm Spodoptera frugiperda of some limonoids isolated from Cedrela spp. (Meliaceae).

Dichloromethane extracts of Cedrela salvadorensis and Cedrela dugessi afforded a photogedunin epimeric mixture, gedunin and cedrelanolide. These compounds and the photogedunin epimeric acetates 3 and 4 at the 23-OH position were evaluated against Spodoptera frugiperda. Toosendanin, isolated from Melia azedarach, was used as a positive control. When tested for activity on neonate larvae into the no-choice bioassays, gedunin, photogedunin epimeric mixture, and photogedunin acetates mixture caused significant larval mortality with LC(50) of 39.0, 10.0, and 8.0 ppm at 7 days, respectively, as well as growth reduction. All the compounds tested inhibited larval growth, compared to the control, in a concentration-dependent manner. In addition, it was possible to observe significant reduced pupal weights and adult emergence. All the tested compounds except cedrelanolide showed comparable activity to that of toosendanin.

Animals↗
PubMed2005

Grayanane diterpenoids from the flowers of Rhododendron molle with cytotoxic activity against a Spodoptera frugiperda cell line.

Two new grayanane diterpenoids, rhodomolins A (1) and B (2), together with two known diterpenoids, rhodomolleins I and rhodojaponin III, were isolated from the flowers of Rhododendron molle. The structures of 1 and 2 were elucidated on the basis of interpretation of spectroscopic data. All compounds were evaluated for cytotoxic activity against the Spodoptera frugiperda cell line Sf-9 and gave IC(50) values in the range 12-80 microg/mL.

Animals↗
PubMed1997

Dioncophylline A as a growth-retarding agent against the herbivorous insect Spodoptera littoralis: structure-activity relationships.

Dioncophylline A (1) represents a novel insecticidal agent, as documented by its enhanced growth-retarding effect on larvae of the polyphagous pest insect Spodoptera littoralis. Within the scope of the work described here, the potential of this as yet most active naphthylisoquinoline alkaloid was further elucidated by the preparation and testing of selected analogues. Investigation of a broad series of structurally modified dioncophylline A analogues (2-20) revealed the free amine function to be essential for the growth inhibitory effect, whereas a modification of the OH function partially led to a distinct increase of activity. In particular, the 8-O-alkyl (especially 8-O-benzylated) derivatives (14 and 15 as well as 16-19) displayed pronounced effects. In the case of 8-O-(p-bromobenzyl)dioncophylline A (16), the activity of the natural parent compound dioncophylline A (1) (EC50 = 277 micrograms/g fresh wt of diet; concentration that inhibits larval growth by 50%) was even improved by a factor of > 15 (EC50 = 15.6 micrograms/g fresh wt).

Animals↗
PubMed1999

From a phagostimulant natural product to semisynthetic antifeedants against Spodoptera littoralis larvae: chemical transformations of the neoclerodane diterpenoid scutegalin B.

Scutegalin B (4), a natural neoclerodane diterpenoid possessing phagostimulant activity against larvae of the lepidopteran Spodoptera littoralis, has been subjected to a series of chemical transformations obtaining several derivatives. The activity of some of these changes to antifeedant (10, 12, 16, and 17), although other derivatives are inactive (6, 7, and 15) or maintain phagostimulant activity (8 and 9) of the starting material (4). The most potent antifeedant was 16, which possesses 16,15-lactone and a (19S)-19, 2alpha-hemiacetal groups instead of the 16,15-lactol and (19R)-(19-O-tigloyl)19,2alpha-hemiacetal of the phagostimulant precursor 4. These and other structure-activity relationships are discussed, establishing that the biological action is strongly modulated by minimal structural variations.

Agrochemicals↗
PubMed1997

Genomic localization and nucleotide sequence of a lef-8 gene of the Spodoptera littoralis nucleopolyhedrovirus.

A gene similar to lef-8 of the Autographa californica (Ac) nucleopolyhedrovirus (MNPV) was identified in the Spodoptera littoralis (Spli) MNPV. The SpliMNPV lef-8-like gene was localized on the genomic map between 26.9 and 29 map units and is flanked by a chitinase gene and p47 gene. This gene arrangement differs from that of similar genes in the AcMNPV genome, where the lef-8 gene is located about 62 kbp from the chitinase gene and about 7 kbp from the p47 gene. Sequence analyses of the lef-8 gene revealed an ORF of 2730 nucleotides, predicted to encode a protein with Mr 104876. The putative protein is 60.9% identical to the AcMNPV LEF-8 and contains an identical sequence of a conserved motif of DNA-dependent RNA polymerases. Sequences downstream of the lef-8 gene contain two sequence repeats which resemble a repeated motif of the SpliMNPV enhancer element and other repetitive sequences from the viral genome.

Amino Acid Sequence↗
PubMed2000

Comparative analysis of the granulin regions of the Phthorimaea operculella and Spodoptera littoralis granuloviruses.

The nucleotide sequence of two cloned restriction fragments encompassing the granulin genes from the granuloviruses of the potato tuber moth, Phthorimaea operculella, PhopGV, and the Egyptian cotton leaf worm, Spodoptera littoralis, SpliGV, have been determined. Although both viruses are able to infect the same Ph. operculella cell line, their granulins do not cluster in the same phylogenetic branches. PhopGV ganulin is closely related to Cydia pomonella GV (CpGV) and Cryptophlebia leucotreta GV (ClGV) (95.2 and 94% identity at the aminoacid level), while SpliGV granulin falls close to Trichoplusia ni GV and Xestia c-nigrum GV (91.6 and 92.0% respectively). The gene organization around the granulins reflects this clustering. Upstream the PhopGV granulin, an ORF belonging to the ME53 gene family (as ORF 124R of CpGV and 909 of ClGV) is present, while no equivalent ORF is found in this region in SpliGV. Downstream the granulin, both viruses present a gene homologous to the Autographa californica nucleopolyhedrovirus (AcMNPV) ORF 9 followed by a Protein Kinase (AcMNPV ORF10). The structure of this region seems thus conserved not only among nucleopolyhedroviruses but also in at least some granuloviruses.

Animals↗
PubMed2000

Adaptation of Spodoptera exigua (Lepidoptera: Noctuidae) to barley trypsin inhibitor BTI-CMe expressed in transgenic tobacco.

Nicotiana tabacum plants were transformed with the cDNA of barley trypsin inhibitor BTI-CMe under the control of the 35S CaMV promoter. Although the transgene was expressed and the protein was active in the homozygous lines selected, growth of Spodoptera exigua (Lepidoptera: Noctuidae) larvae reared on transgenic plants was not affected. The protease activity in larval midgut extracts after 2 days feeding on transformed tobacco leaves from the highest expressing plant showed a reduction of 25% in the trypsin-like activity compared to that from insects fed on non-transformed controls. The susceptibility of digestive serine-proteases to inhibition by BTI-CMe was confirmed by activity staining gels. This decrease was compensated with a significant induction of leucine aminopeptidase-like and carboxipeptidase A-like activities, while chymotrypsin-, elastase-, and carboxipeptidase B-like proteases were not affected.

Adaptation, Physiological↗
PubMed2002

Evaluation of synergism in the feeding deterrence of some furanocoumarins on Spodoptera littoralis.

The phagodepression activity of five furanocoumarins (FC), bergapten, xanthotoxin, psoralen, imperatorin, and angelicin, has been studied against larvae of Egyptian cotton leafworm Spodoptera littoralis (Boisduval) (Lepidoptera: Noctuidae) using a leaf-disk choice bioassay. The dose range used was 0-10 microg/cm2 for linear furocoumarins and 0-30 microg/cm2 for angelicin, the angular furanocoumarin. Dose-feeding deterrency activity correlations were governed by various sigmoidal functions, except in the case of imperatorin and bergapten, which had dose-response curves showing irregular traces with two maxima. All five FCs induced various degrees of phagodepression in S. littoralis; at 3 microg/cm2, the relative feeding deterrence was bergapten = xanthotoxin > psoralen = imperatorin = angelicin. Structure-activity correlations indicated that a methoxy group on C-5 or C-8 enhanced the activity. Comparison of experimental feeding deterrence of binary mixtures of imperatorin with xanthotoxin, bergapten, or psoralen at various relative concentrations with the calculated additive activity of each combination indicated that a proportion of 40% or more of imperatorin may exert a greater antifeedant effect on S. littoralis than the sum of individual compounds. The effect of angelicin also was examined in combination with psoralen, both of which are present in Psoralea plants. Their mixtures yielded a clear synergistic effect in the 20-80% angelicin range (coactivity coefficient = 124-133). By contrast, the effect of angelicin on xanthotoxin was only additive. In the dose-response curves of imperatorin/bergapten combinations, synergism was found at >60% imperatorin relative concentration and 1 microg/cm2, whereas lower proportions led to antagonism. The threshold between the two opposing effects was found to depend on the total FC concentration employed. Some natural systems contain FCs in the range of synergistic proportions recorded here and, thus, may have been produced by the host to increase its defensive effect at a lower metabolic cost.

Animals↗
PubMed2001

Characterization of the antiapoptotic (p35) gene homologue of Spodoptera litura nucleopolyhedrosis virus (SlNPV).

Antiapoptotic genes of baculoviruses have been shown to prevent virus induced apoptosis in insect cells. Dot blot and Southern hybridizations of EcoRI genomic library and genomic digests of Spodoptera litura nucleopolyhedrosis virus (SlNPV) respectively give strong hybridization signals with antiapoptotic DNA (p35 gene) probe of the prototype Autographa californica nucleopolyhedrosis virus (AcNPV). Both the hybridizations indicate the presence of a homologous gene in the 1.8 kb EcoRI-Y fragment of SlNPV. The sequence of 1.244 kb region of this fragment encompasses an open reading frame coding for a polypeptide of 296 amino acids under sequential early (TATA) and late (TAAG) promoter motifs like that in other baculovirus p35 genes. The putative SlNPV p35 ORF expresses abundantly as a 35 kDa protein in Spodopterafrugiperda (Sf9) cells when allowed to express under the polyhedrin promoter of AcNPV.

Amino Acid Sequence↗
PubMed2002

Avidin expressed in transgenic tobacco leaves confers resistance to two noctuid pests, Helicoverpa armigera and Spodoptera litura.

Fertile transgenic tobacco plants with leaves expressing avidin in the vacuole have been produced and shown to halt growth and cause mortality in larvae of two noctuid lepidopterans, Helicoverpa armigera and Spodoptera litura. Late first instar H. armigera larvae and neonate (< 12-h-old) S. litura larvae placed on leaves excised from T0 tobacco expressing avidin at 3.1-4.6 microM (micromoles/kg of fresh leaf tissue) had very poor growth over their first 8 days on the leaves, significant numbers had died by days 11 or 12 and all were dead by day 22 (H. armigera) or day 25 (S. litura). Similar results were obtained when late first instar H. armigera larvae were placed on leaves from T1 plants expressing avidin at six different average concentrations, ranging from 3.7 to 17.3 microM. Two larvae on the lowest expressing leaves survived to pupation, but there was total mortality among the other groups and no relationship between avidin concentration and the effects on the larvae. Synergistic effects between avidin-expressing tobacco plants and a purified Bt toxin, Cry1Ba, were demonstrated. Late instar H. armigera larvae fed with leaves from T2 plants expressing avidin at average concentrations of either <5.3 or > 12.9 microM, and painted with Cry1Ba protein at a rate equivalent to an expression level of 0.5% of total leaf protein, died significantly faster than larvae given either of the two treatments alone. Larvae fed with avidin-expressing leaves painted with the protease inhibitor, aprotinin, at a rate equivalent to 1% of total leaf protein had mortality similar to those given avidin-leaves alone. There was no evidence of antagonism between these two proteins.

Agrobacterium tumefaciens↗
PubMed2002

Characterization of a J domain gene of Spodoptera litura multicapsid nucleopolyhedrovirus.

Spodoptera litura multicapsid nucleopolyhedrovirus (SpltMNPV) ORF39 (designated as the bjdp gene) is the only J domain gene recorded in baculovirus genomes to date. Computer-assisted analysis revealed that its deduced amino acid sequences possessed a coiled-coil region and a RNA recognition motif (RRM). In vivo the bdjp gene transcription was detected from 24 h post infection (p.i.) and abundant from 72 to 96 h p.i., while in vitro it was first detected 6 h p.i. and was abundant from 12 to 24 h p.i., respectively. Western blot analysis of BJDP expression with an antiserum made against 6xHis tagged BJDP expressed in Escherichia coli showed that it was present from 24 through 96 h p.i. in vitro. Western blot analysis indicated that BJDP was found to be associated with budded and occlusion-derived virions (ODV). Furthermore, BJDP was shown to be present in both envelope and nucleocapsid fractions of ODV. These results suggested that BJDP might be a structural protein.

Amino Acid Sequence↗
PubMed2003

Identification of a novel protein associated with envelope of occlusion-derived virus in Spodoptera litura multicapsid nucleopolyhedrovirus.

Spodoptera litura multicapsid nucleopolyhedrovirus (SpltMNPV) ORF137 (Splt137) is one of 29 unique SpltMNPV ORFs. Splt137 has the potential to code for a polypeptide of 231 amino acid residues with predicted molecular weight of 27.5 kDa. Computer-assisted analysis of the predicted amino acid sequences of Splt137 protein showed 1 N-glycosylation site and 11 phosphorylation sites. For identification of Spit137, antibody was prepared by immunization of rabbits with purified Splt137 protein produced in Escherichia coli. This antibody was used to analyse Splt137 protein using Western blot. A 36-kDa protein was found both in the infected cells and envelope fractions of occlusion-derived virus (ODV) but could not be detected in the budded virus (BV). Tunicamycin treatment of SpltMNPV infected cells suggested that the 36-kDa protein had undergone N-glycosylation. Our data suggested that Splt137 protein was a novel envelope protein of ODV and might exist as a more complex form of 79-kDa protein in intact ODV. Further, transcriptional analysis with RT-PCR and 5' RACE analysis suggested that Splt137 might perform functions early and late in infection.

Amino Acid Sequence↗
PubMed2002

Purification of DNA for the transfection of a Spodoptera frugiperda cell line.

Spodoptera frugiperda (Sf-9) cells have been widely used in baculovirus expression systems, transient gene expression studies and transgenic cell lines. These applications commonly require the transfection of bacterial plasmid DNA. One of the most reliable methods of preparing transfection-quality plasmid DNA is cesium chloride (CsCl) density gradient centrifugation. However, the traditional CsCl DNA purification is a long and laborious process. We have made a series of modifications to the traditional method that makes it faster, safer and easier. In the current study we demonstrate that DNA prepared by our modified CsCl method was also better for the transfection of Sf-9 cells than DNA prepared by the traditional CsCl method.

Animals↗
PubMed2003

Effects of drought stressed cotton, Gossypium hirsutum L., on beet armyworm, Spodoptera exigua (Hübner), oviposition, and larval feeding preferences and growth.

The beet armyworm, Spodoptera exigua (Hübner), has been anecdotally reported to oviposit more on drought stressed than on nonstressed cotton plants. Using potted cotton plants in cages, this study demonstrated that beet armyworms deposited 3.3, 4.6, and 2.3 times more (P < or = 0.05) eggs on cotton plants that were grown on 1500, 1000, and 750 ml water/wk, respectively, than on cotton plants grown in well watered (4000 ml water/wk) soil. Third instars, however, showed no preference for stressed cotton foliage over nonstressed foliage. Third instar beet armyworms raised on well watered cotton plants were 1.5, 2.3, and 2.6 times heavier than those reared on cotton grown in the 1500, 1000, and 750 ml water/wk plants (P < or = 0.05), respectively. Physiochemical analyses showed that drought stressed leaves had significantly greater accumulations of free amino acids that are essential for insect growth and development. Soluble protein and soluble carbohydrates were also more abundant in stressed leaves compared to nonstressed leaves. Despite the apparent increase in nutritional quality in drought stressed plants, larval survival was reduced, probably because the limiting factor became water. Greater amounts of cotton leaf area were consumed from drought stressed leaves (P < or = 0.05) than from nonstressed leaves, probably because the larvae had to metabolize greater portions of assimilated energy to supplement body water with metabolic water derived from respiration. The association of greater host plant nutritional quality to oviposition preference, and conversely, to reduced survivorship, is discussed.

Amino Acids↗
PubMed2003

Characterization of bro-b gene of Spodoptera litura multicapsid nucleopolyhedrovirus.

Spodoptera litura multicapsid nucleopolyhedrovirus (SpltMNPV) ORF125 (designated as the bro-b gene) is a member of the unique multigene family called the baculovirus repeated ORFs (bro) family. Computer-assisted analysis revealed that BRO-B contains a conserved Bro-N domain in its N-terminus and a single-stranded DNA (ssDNA) binding motif in the middle region. In vitro the bro-b gene transcription was present at 12 h post-infection (p.i.) and remained detectable up to 96 h p.i. Western blot analysis of BRO-B expression with an antiserum made against 6xHis tagged BRO-B expressed in Escherichia coli showed that it was present from 12 h through 96 h p.i. in vitro. Structural localization revealed that BRO-B could be found in the nucleocapsid components of both occlusion-derived virus (ODV) and budded virus (BV). Immunofluorescence analysis indicated that BRO-B is located only in the nucleus of infected S. litura cells. Furthermore, Western blot analysis indicated that BRO-B was associated with nuclear structures. These results suggested that BRO-B might be a nuclear-associated protein.

Amino Acid Motifs↗
PubMed2004

Recombinant destabilase-lysozyme: synthesis de novo in E. coli and action mechanism of the enzyme expressed in Spodoptera frugiperda.

Destabilase-lysozyme (DL) from salivary gland secretion of the medicinal leech (Hirudo medicinalis) is as a member of the invertebrate lysozyme family, which sharply differs from other lysozyme families. In this study, DL lysozyme function was confirmed during expression of a gene encoding DL in Escherichia coli. Several constructs of the expression vectors pKK OmpA and pET-3A with or without bacterial, leech, or yeast signal peptides (SP) were used. The use of a construct without signal peptide genes resulted in normal growth of the transformed cells. Transformation of E. coli cells with the constructs containing SP was accompanied by the disruption of the forming cells. The use of the expression vector pET-32 LTC-System for production of DL as a fusion protein with thioredoxin also resulted in normal cell growth. However, specific activity of DL isolated from such cells was significantly lower than that of enzyme purified from extracts of Spodoptera frugiperda cells, which were infected with the baculovirus vector carrying DL cDNA. It is shown that the action mechanism of invertebrate lysozyme does not differ from that of other families: recombinant DL from S. frugiperda extracts catalyzed cleavage of synthetic substrate, hexamer of N-acetylglucosamine, to di- and tetramers, which is typical for enzymatic function of other lysozyme families.

Acetylglucosamine↗