Effect of protein extracts of Amaranthus retroflexus (Amaranthaceae) and Cuminum cyminum (Apiaceae) on digestive proteinases and biological characters of Helicoverpa (Heliothis) armigera (Hübner) (Lepidoptera: Noctuidae)

2020 ◽  
Vol 152 (5) ◽  
pp. 646-662
Author(s):  
Solmaz Azimi ◽  
Shima Rahmani ◽  
Maghsoud Pazhouhandeh
Keyword(s):  
Seed Protein ◽  
Proteinase Inhibitors ◽  
Larval Mortality ◽  
Polyacrylamide Gel Electrophoresis ◽  
Heliothis Armigera ◽  
Amaranthus Retroflexus ◽  
Cuminum Cyminum ◽  
Digestive Proteinases ◽  
Lepidoptera Noctuidae ◽  
Seed Extracts

AbstractPlant proteinase inhibitors are among the promising biopesticides which are induced in plants tissues against the several Lepidoptera pests to inhibit digestive proteases. In this study, protein extracts of two nonhost plant seeds, Amaranthus retroflexus Linnaeus (Amaranthaceae) and Cuminum cyminum Linnaeus (Apiaceae), were examined on Helicoverpaarmigera (Hübner) (Lepidoptera: Noctuidae). The results obtained by using azocasein as a substrate showed that inhibitory activity of general proteases of the larvae fed on a diet incorporated with both inhibitors was dose dependent. Seed extracts of A. retroflexus and C. cyminum at the highest concentration showed that inhibition activities of chymotrypsin-like proteinase and trypsin-like proteinase were between 31–45% and 28–61%, respectively. Based on polyacrylamide gel electrophoresis, all of the proteinase isoforms, including those of A. retroflexus seed extracts, disappeared entirely, and only one band was detected in the seed extracts of C. cyminum. Larval mortality in the larvae fed on A. retroflexus and C. cyminum seed extracts was 56 ± 2.15 and 68 ± 2.23, respectively, but mortality in control (no seed protein extract) was 12 ± 2.34 individuals. Also, the life table parameters were affected significantly by A. retroflexus and C. cyminum protein seed extracts. Therefore, A. retroflexus and C. cyminum seed protein extracts showed inhibitory effect on H. armigera digestive proteinases and adverse effects on survival and fitness of the pest; hence, they could be introduced as a successful biopesticide in the near future.

scholarly journals Evaluation of indigenous the nucleopolyhedrovirus (NPV) of Spodoptera litura (Fabricius) (Lepidoptera: Noctuidae) in combination with chlorantraniliprole against Spodoptera species

2021 ◽  
Vol 31 (1) ◽  
Author(s):  
Ghulam Sarwar ◽  
Naeem Arshad Maan ◽  
Muhammad Ahsin Ayub ◽  
Muhammad Rafiq Shahid ◽  
Mubasher Ahmad Malik ◽  
...  
Keyword(s):  
Larval Mortality ◽  
Adult Emergence ◽  
Lethal Concentration ◽  
Pest Species ◽  
Vegetable Crops ◽  
Chemical Insecticide ◽  
Larval Instars ◽  
Novel Method ◽  
High Larval Mortality ◽  
Lepidoptera Noctuidae

Abstract Background The armyworms, Spodoptera exigua (Hübner), and S. litura (Fabricius) (Lepidoptera: Noctuidae) are polyphagous pests of many cash crops. Heavy crop losses have been reported for the fruit and vegetable crops each year owing to the diverse impact on global economies. The present study was aimed to sort out a novel method of pest control using the insect’s own nucleopolyhedrosis virus (NPV) alone and in combination with a new chemistry insecticide chlorantraniliprole. Results In the study, the effect of indigenous isolated nucleopolyhedrovirus (NPV) and the chemical insecticide (chlorantraniliprole) formulations against the 2nd and 4th larval instars of S. litura and S. exigua, collected from the different geographical region of Punjab (Pakistan) province, was evaluated. Three concentrations of the NPV isolate, sub-lethal (1 × 104, 6 × 104 POB ml−1), lethal (3 × 105 POB ml−1), and chlorantraniliprole 0.01 μl l−1, were applied alone and in combination against the 2nd and 4th larval instars of both pest species. The lethal concentration of NPV + chlorantraniliprole exhibited synergistic interaction and caused high larval mortality against both instars, while in all other combinations, additive effect was observed. Moreover, NPV + chlorantraniliprole at lethal concentration exhibited decreased pupation, adult emergence, and egg eclosion. Conclusion The implications of using NPV alone and in combination with an insecticide are discussed briefly in this study.

scholarly journals Pathogenicity of Metarhizium rileyi (Farlow) Kepler, S.A. Rehner and Humber isolates against Spodoptera litura (Fabricius) and their extracellular enzymatic activities

2021 ◽  
Vol 31 (1) ◽  
Author(s):  
Gurmehar Kaur Grewal ◽  
Neelam Joshi ◽  
Yadhu Suneja
Keyword(s):  
Spodoptera Litura ◽  
Larval Mortality ◽  
Screening Methods ◽  
Metarhizium Rileyi ◽  
Percent Mortality ◽  
Commercially Important ◽  
Extracellular Enzymatic Activities ◽  
Chemical Pesticides ◽  
Lepidoptera Noctuidae

Abstract Background Spodoptera litura (Fab.) (Lepidoptera: Noctuidae) is a serious agricultural pest that infests many commercially important crops of Southeast Asian countries. Indiscriminate use of chemical pesticides has led to various health hazards as well as insecticide resistance. Entomopathogenic fungi (EPF) provide an important alternative as biological control agents. Metarhizium rileyi is an EPF with a specific host range for lepidopteran pests. The present study aimed to identify virulent M. rileyi isolate against S. litura larvae and analyse their extracellular cuticle-degrading enzyme activities. Results Three M. rileyi isolates viz M. rileyi NIPHM, M. rileyi MTCC 4254 and M. rileyi MTCC 10395 formulations were evaluated at different concentrations against 2nd instar larvae of S. litura. A maximum percent mortality of 63.33% was recorded in M. rileyi NIPHM (12 g/l), followed by M. rileyi MTCC 4254 (58.33%) at the same concentration, 10 days post-treatment. Maximum means of chitinase, protease and lipase activities (0.44, 1.58 and 2.95 U/ml, respectively) were recorded in the case of M. rileyi NIPHM. Correlation analysis was positive between enzyme activity and larval mortality. Conclusions Metarhizium rileyi NIPHM recorded the highest enzymatic activity and exhibited the maximum mortality rate against 2nd instar larvae of S. litura, suggesting the possible role of these enzymes in the pathogenicity of the fungus. Further knowledge in this regard may help in the development of enzyme-based screening methods for selecting virulent fungal isolates for the eco-friendly management of crop pests.

scholarly journals Biological activities of spores and metabolites of some fungal isolates on certain aspects of the spiny bollworms Earias insulana (Boisd.) (Lepidoptera: Noctuidae)

2019 ◽  
Vol 29 (1) ◽  
Author(s):  
Eman Mohammed Abd-ElAzeem ◽  
Warda Ahmed Zaki El-Medany ◽  
Hend Mohammed Sabry
Keyword(s):  
Biological Activities ◽  
Larval Mortality ◽  
Adult Emergence ◽  
Pupal Weight ◽  
Earias Insulana ◽  
Dead Larva ◽  
Fungal Isolates ◽  
Protease Enzyme ◽  
Newly Hatched Larvae ◽  
Lepidoptera Noctuidae

AbstractBiological activities of spores and metabolites of some fungi isolated from dead larva of the spiny bollworms (SBW), Earias insulana (Boisd.) (Lepidoptera: Noctuidae), against the newly hatched larvae of the pest were carried out. Results showed that the fungi Metarhizium anisopliae, Acremonium sp., and Paecilomyces variotii had affected the newly hatched larvae of (SBW). Acremonium sp. was the most potent one as it had the highest newly hatched larval mortality percentage (65 and 58.33%) for its spore suspension and metabolites, respectively, while the lowest one (41%) was for P. variotii metabolites. Also, spore suspensions of the all fungal isolates had the highest larval mortality than fungal metabolites. Studying the enzymatic activity showed that Acremonium sp. produced protease enzyme on media containing gelatin, which caused the highest larval mortality (72.22%).These isolates showed different effects on all stages of the pest and decreased pupal weight, adult emergence percentages, deposited eggs, and hatchability percentages than the control. Identification of Acremonium sp. EZ1 was confirmed using 18 s rRNA and its accession number MN25101.

Incidence of Helicoverpa armigera (Lepidoptera: Noctuidae) and its natural enemies on smallholder crops in Kenya

1993 ◽  
Vol 83 (3) ◽  
pp. 321-328 ◽  
Author(s):  
H. van den Berg ◽  
M. J. W. Cock ◽  
G. I. Oduor ◽  
E. K. Onsongo
Keyword(s):  
Helicoverpa Armigera ◽  
Heliothis Armigera ◽  
Population Densities ◽  
Parasitoid Species ◽  
Larval Parasitoid ◽  
Total Percentage ◽  
Four Seasons ◽  
Helicoverpa Armígera ◽  
Lepidoptera Noctuidae ◽  
Experimental Plots

AbstractSmallholder crops (sunflower, maize, sorghum and cotton) were grown in experimental plots at seven sites, representing different agricultural zones of Kenya, over four seasons. Helicoverpa armigera (Hübner) (formerly Heliothis armigera) only occasionally achieved population densities sufficient to cause obvious damage to the crops, and was virtually absent from the coastal sites. At the inland sites, infestation and mortality levels varied greatly. Information is presented on the incidence of H. armigera, and the identity, distribution and frequency of its common parasitoids and (potential) predators, sampled in the experimental plots. Trichogrammatoidea spp., egg parasitoids, and Linnaemya longirostris (Macquart), a tachinid late-larval parasitoid, were the most common parasitoid species, but total percentage parasitism was rather low. Of the large complex of predators, only anthocorids and ants (predominantly Pheidole spp., Myrmicaria spp. and Camponotus spp.) were sufficiently common and widespread to be of importance in suppressing H. armigera. The abundance of predators fluctuated widely between sites, but anthocorids were most abundant at the western sites.

scholarly journals Peptides of human bronchial mucus glycoproteins. Size determination by electron microscopy and by biosynthetic experiments

1987 ◽  
Vol 248 (1) ◽  
pp. 189-195 ◽  
Author(s):  
T Marianne ◽  
J M Perini ◽  
J J Lafitte ◽  
N Houdret ◽  
F R Pruvot ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Proteinase Inhibitors ◽  
Polyacrylamide Gel Electrophoresis ◽  
Length Distribution ◽  
Molecular Size ◽  
Pulse Labelling ◽  
Bronchial Mucosa ◽  
Chase Period ◽  
Bronchial Mucus ◽  
Multiple Treatments

Secreted human bronchial mucins, directly collected from macroscopically healthy bronchial mucosa, were prepared in the presence of six proteinase inhibitors, and analysed by electron microscopy. These mucins were similar in length distribution to molecules prepared from sputum [Slayter, Lamblin, Le Treut, Galabert, Houdret, Degand & Roussel (1984) Eur. J. Biochem. 142, 209-218], although they were a little longer, their lengths ranging up to about 1,650 nm. This length corresponds to an extended mucin peptide of about 450 kDa. In order to compare these peptide lengths with the molecular size of biosynthetic precursors, an antiserum raised against trifluoromethanesulphonic acid-treated highly glycosylated regions of human bronchial mucins was used to isolate mucin precursors synthesized in explants of human bronchial mucosa during pulse-labelling with [3H]threonine or [3H]glucosamine. A main precursor labelled with [3H]threonine and with an apparent molecular mass of about 400 kDa was detected by fluorography following SDS/polyacrylamide-gel electrophoresis. This band was observed as early as 20 min; it was more intense after a 40 min chase and had disappeared after a chase period of 280 min in unlabelled medium, presumably owing to glycosylation. Much fainter bands at about 200 kDa and between 200 and 400 kDa, also labelled with [3H]threonine, were observed mainly after a 40 min chase and had disappeared after a 280 min chase. None of these bands was labelled with [3H]glucosamine, nor did they disappear after multiple treatments with immobilized lectins. After a 280 min chase, [3H]threonine-labelled material appeared in the stacking gel, which also contained [3H]glucosamine label. The results indicate that the 200-400 kDa species are mucin precursors, whose size is comparable with that obtained by electron microscopy for respiratory mucins collected directly from the macroscopically healthy bronchial mucosa.

Catabolism of streptokinase and polyethylene glycol-streptokinase: evidence for transport of intact forms through the biliary system in the mouse

Blood ◽  
1990 ◽  
Vol 76 (1) ◽  
pp. 73-79 ◽  
Author(s):  
FH Brucato ◽  
SV Pizzo
Keyword(s):  
Molecular Weight ◽  
Polyethylene Glycol ◽  
Gel Electrophoresis ◽  
Proteinase Inhibitors ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gi Tract ◽  
Substantial Fraction ◽  
Sds Page ◽  
Derivatives Of

Abstract The catabolism of streptokinase (SK) and polyethylene glycol derivatives of SK (PEG-SK) were studied in mice. The clearance and catabolism of SK:plasmin (SK:Pm) and PEG-SK:Pm activator complexes were also investigated. Native 125I-SK cleared rapidly (t1/2 = 15 minutes) from the circulation, with the majority of the ligand accumulating in the liver and gastrointestinal (GI) tract and a substantial fraction also localizing in the kidneys. SK, which was removed from the plasma by the liver, was secreted into bile and then the GI tract. Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) demonstrated that 125I-SK recovered from liver and bile was homogeneous and of the same molecular weight (mol wt approximately 50,200) as native SK. PEG-125I-SK cleared slowly (t1/2 greater than 200 minutes), with more than 80% of the preparation localizing in liver and GI tract. The PEG-125I-SK secreted into the bile was also intact. The bile containing 125I-SK was incubated with stoichiometric amounts of plasminogen and electrophoresed under nondenaturing conditions. This study demonstrated that the secreted SK was able to form SK:Pg complexes. SDS-PAGE also showed activation of 125I-Pg that was incubated with recovered bile containing the SK. 125I-SK:Pm catabolism was also studied. In these experiments, the mol wt approximately 42,000 fragment obtained when SK is cleaved by plasmin was found in the bile. This fragment of 125I-SK was not recovered as part of a complex with plasmin, consistent with our previous observations that catabolism of SK:Pm involves transfer of the plasmin to plasma proteinase inhibitors while SK is catabolized independently. By contrast, when PEG-125I-SK:Pm was injected into mice, only intact PEG-125I-SK was found in the bile, consistent with our previous observations that the PEG derivatization blocks its degradation by plasmin.

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