Temephos Resistance and Esterase Activity in Selected Laboratory Population of Culex Pipiens from Tunisia

2017 ◽  
Vol 3 (4) ◽  
pp. 14-17
Author(s):  
Ahmed Tabbabi ◽  
Ali Lamari ◽  
Jaber Daaboub
Keyword(s):  
Esterase Activity ◽  
Culex Pipiens ◽  
Laboratory Population

Comparative study of resistance to organophosphate and carbamate insecticides in four strains of the Culex pipiens L. complex (Diptera: Culicidae)

1986 ◽  
Vol 76 (3) ◽  
pp. 505-511 ◽  
Author(s):  
Z. H. Tang ◽  
R. J. Wood
Keyword(s):  
Esterase Activity ◽  
Culex Pipiens ◽  
Larval Instar ◽  
Piperonyl Butoxide ◽  
Lower Sensitivity ◽  
Pyrethroid Insecticides ◽  
Carbamate Insecticides ◽  
High Production ◽  
Resistant Strains ◽  
General Esterase

AbstractFive strains of Culex pipiens L. (four resistant and one susceptible) were compared at the fourth larval instar for tolerance to organophosphate, carbamate and pyrethroid insecticides, with and without the addition of three synergists (piperonyl butoxide, triphenyl phosphate (TPP) and S, S, S-tributyl phosphorotrithiote (TBPT)). The DAR/D strain from Tanzania showed the highest levels and broadest range of resistance (temephos 37 ×, malathion 579×, propoxur 3032× and permethrin 100×). A strain from Rangoon and two from France (S54, BLEUET) showed lower resistance, restricted to organophosphates. Temephos and malathion resistance in the RANGOON strain was strongly inhibited by TBPT but not by TPP or piperonyl butoxide. Temephos and permethrin resistance in the DAR/D strain was slightly inhibited by TBPT and permethrin resistance by piperonyl butoxide. The DAR/D, RANGOON and CfCA (susceptible) strains were also compared for general esterase activity and phosphatase activity, both of which were higher in the resistant strains. It is concluded that resistance in RANGOON is associated with high production of an esterase sensitive to inhibition by TBPT but with little or no sensitivity to TPP, resembling but not identical in properties with the enzyme in strain S54 investigated earlier. Resistance in DAR/D was also associated with some increase in esterase activity, but the basis of resistance was different from that in S54 and RANGOON, having a much lower sensitivity to inhibition by TBPT.

scholarly journals First Report of Biochemical Mechanisms of Insecticide Resistance in the Field Population of Culex pipiens (Diptera: Culicidae) From Sari, Mazandaran, North of Iran

2020 ◽  
Author(s):  
Seyed Hassan Nikookar ◽  
Mahmoud Fazeli-Dinan ◽  
Seyyed Payman Ziapour ◽  
Fatemeh Ghorbani ◽  
Yaser Salim-Abadi ◽  
...  
Keyword(s):  
Insecticide Resistance ◽  
Culex Pipiens ◽  
Pyrethroid Resistance ◽  
Cytochrome P450s ◽  
Field Population ◽  
Susceptible Strain ◽  
Laboratory Population ◽  
Significant Difference ◽  
North Of Iran ◽  
The Mean

  Background: Culex pipiens play an important role in transmission of infectious diseases. Vector control by chemical pesticides, leads inevitably to resistance development. Understanding the underlying resistance mechanisms can help improve the control programmes and insecticide resistance management. Methods: The total contents of cytochrome p450s and the activities of glutathione S-transferases, alpha- and beta-esterases and inhibition rates of acetylcholine esterase (by propoxur) were measured in the field population of Cx. pipiens collected from Sari County, North of Iran, in 2016 and the results were compared with those of the laboratory susceptible strain according to the biochemical assay methods of WHO for adult mosquitoes. Independent sample t-test was used to compare the mean values of enzyme activities/contents between filed and laboratory susceptible popula-tions. Results: The enzyme ratio of cytochrome p450s, alpha- and beta-esterases in the field population was 2.07, 3.72 and 1.36 respectively when compared with the results of the laboratory population. Although not statistically significant, the mean GSTs activities in the field population was marginally less than the laboratory population (ER=0.92). Ace-tylcholinesterase was insensitive to propoxur in 62.82% of the individuals of the tested field population. There was a significant difference (P< 0.05) between all values of the activities/contents of the enzyme in the field population except for GSTs compared with the laboratory susceptible strain. The highest enzyme activity was related to alpha esterase. Conclusion: The present study showed a range of metabolic mechanisms, comprising p450s and esterases combined with target site insensitivity of AChE, contributing to organophosphate, carbamate and pyrethroid resistance in the field population of Cx. pipiens.

Toxicity of Four Pyrethroid-based Insecticides and Kerosene to a Laboratory Population of Culex pipiens

2005 ◽  
Vol 8 (5) ◽  
pp. 751-753
Author(s):  
Hamdy I. Hussein . ◽  
DiefAlla Al-Rajhy . ◽  
Mohamed Al-Assiry .
Keyword(s):  
Culex Pipiens ◽  
Laboratory Population

Fine Structure of the Malpighian Tubules of the Mosquito, Culex pipiens

1971 ◽  
Vol 29 ◽  
pp. 402-403
Author(s):  
Brendan Clifford
Keyword(s):  
Fine Structure ◽  
Culex Pipiens ◽  
Stellate Cell ◽  
Malpighian Tubule ◽  
Cell Types ◽  
Instar Larva ◽  
Malpighian Tubules ◽  
Calliphora Erythrocephala ◽  
Distinct Cell ◽  
Basal Plasma

An ultrastructural investigation of the Malpighian tubules of the fourth instar larva of Culex pipiens was undertaken as part of a continuing study of the fine structure of transport epithelia.Each of the five Malpighian tubules was found to be morphologically identical and regionally undifferentiated. Two distinct cell types, the primary and stellate, were found intermingled along the length of each tubule. The ultrastructure of the stellate cell was previously described in the Malpighian tubule of the blowfly, Calliphora erythrocephala by Berridge and Oschman.The basal plasma membrane of the primary cell is extremely irregular, giving rise to a complex interconnecting network of basal channels. The compartments of cytoplasm entrapped within this system of basal infoldings contain mitochondria, free ribosomes, and small amounts of rough endoplasmic reticulum. The mitochondria are distinctive in that the cristae run parallel to the long axis of the organelle.

Insecticidal properties of extracts and phytochemicals isolated from three Egyptian plants against Culex pipiens

Planta Medica ◽  
2011 ◽  
Vol 77 (12) ◽  
Author(s):  
SA Abdelgaleil ◽  
T Suganuma ◽  
K Kitahara ◽  
M Fujii
Keyword(s):  
Culex Pipiens

Study of Thrombin-Coagulase

1967 ◽  
Vol 17 (03/04) ◽  
pp. 321-334 ◽  
Author(s):  
J. P Soulier ◽  
Odette Prou-Wartelle ◽  
Liliane Hallé ◽  
Keyword(s):  
Esterase Activity ◽  
Adsorption Chromatography ◽  
The Difference

SummaryThe preparation of thrombin-coagulase is described. The properties of thrombin-coagulase are compared with those of biothrombin: kinetics, thermostability, adsorption, chromatography, esterase activity, clotting activity, action on platelets and on factors V and VIII, susceptibility to inhibitors.Biothrombin and thrombin-coagulase are closely related but distinct. Both apparently derive from prothrombin. Prothrombin and coagulase combine to form a complex: thrombin-coagulase wherein both factors are necessary for its activity. Possible explanations for the difference between thrombin-coagulase and biothrombin are proposed.

Activity of Plasmin and Streptokinase-Activator on Substituted Arginine and Lysine Esters

1966 ◽  
Vol 16 (01/02) ◽  
pp. 018-031 ◽  
Author(s):  
S Sherry ◽  
Norma Alkjaersig ◽  
A. P Fletcher
Keyword(s):  
Molecular Structure ◽  
Methyl Ester ◽  
Comparative Studies ◽  
Esterase Activity ◽  
Methyl Esters ◽  
Hydrolytic Activity ◽  
The Other ◽  
Other Hand

SummaryComparative studies have been made of the esterase activity of plasmin and the streptokinase-activator of plasminogen on a variety of substituted arginine and lysine esters. Human plasmin preparations derived by different methods of activation (spontaneous in glycerol, trypsin, streptokinase (SK) and urokinase) are similar in their esterase activity; this suggests that the molecular structure required for such esterase activity is similar for all of these human plasmins. Bovine plasmin, on the other hand, differs from human plasmin in its activity on several of the substrates studied (e.g., the methyl esters of benzoyl arginine and tosyl, acetyl and carbobenzoxy lysine), a finding which supports the view that molecular differences exist between the two animal plasmins. The streptokinase-activator hydrolyzes both arginine and lysine esters but the ratios of hydrolytic activity are distinct from those of plasmin and of other activators of plasminogen. The use of benzoyl arginine methyl ester as a substrate for the measurement of the esterase activity of the streptokinase-activator is described.

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