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Heterologous expression and characterization of a sigma glutathione S-transferase involved in carbaryl detoxification from oriental migratory locust, Locusta migratoria manilensis (Meyen).
J Insect Physiol. 2012 Feb; 58(2):220-7.JI

Abstract

Glutathione S-transferases (GSTs) play a major role in detoxification of xenobiotics and resistance to insecticides in insects. In the present study, a sigma-class GST gene (LmGSTs3) was identified from the locust, Locusta migratoria manilensis. Its full-length cDNA sequence is 828 bp containing an open reading frame (ORF) of 612 bp that encodes 204 amino acid residues. The predicted protein molecular mass and pI are 23.4 kDa and 7.62, respectively. Recombinant LmGSTs3 was heterologously expressed in Escherichia coli as a soluble fusion protein. Its optimal activity was observed at pH 8.0. Incubation for 30 min at temperatures below 40 °C scarcely affected activity. The LmGSTs3 at pH values between 4.0 and 11.0 retained more than 80% of its original activity. Ethacrynic acid and cibacron blue were very effective inhibitors of LmGSTs3 with I50-values 1.7 and 3.7 μM, respectively. In response to heavy metal (CuSO4, CdCl2) exposure there was a concentration-dependent and time-dependent decrease in activity. The nymph mortalities after carbaryl treatment increased 38.7% after LmGSTs3 were silenced. These results suggest that LmGSTs3 may be involved in carbaryl detoxification in L. migratoria manilensis.

Authors+Show Affiliations

Research Institute of Applied Biology, Shanxi University, Taiyuan, Shanxi 030006, China.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

22075389

Citation

Qin, Guohua, et al. "Heterologous Expression and Characterization of a Sigma Glutathione S-transferase Involved in Carbaryl Detoxification From Oriental Migratory Locust, Locusta Migratoria Manilensis (Meyen)." Journal of Insect Physiology, vol. 58, no. 2, 2012, pp. 220-7.
Qin G, Jia M, Liu T, et al. Heterologous expression and characterization of a sigma glutathione S-transferase involved in carbaryl detoxification from oriental migratory locust, Locusta migratoria manilensis (Meyen). J Insect Physiol. 2012;58(2):220-7.
Qin, G., Jia, M., Liu, T., Zhang, X., Guo, Y., Zhu, K. Y., Ma, E., & Zhang, J. (2012). Heterologous expression and characterization of a sigma glutathione S-transferase involved in carbaryl detoxification from oriental migratory locust, Locusta migratoria manilensis (Meyen). Journal of Insect Physiology, 58(2), 220-7. https://doi.org/10.1016/j.jinsphys.2011.10.011
Qin G, et al. Heterologous Expression and Characterization of a Sigma Glutathione S-transferase Involved in Carbaryl Detoxification From Oriental Migratory Locust, Locusta Migratoria Manilensis (Meyen). J Insect Physiol. 2012;58(2):220-7. PubMed PMID: 22075389.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Heterologous expression and characterization of a sigma glutathione S-transferase involved in carbaryl detoxification from oriental migratory locust, Locusta migratoria manilensis (Meyen). AU - Qin,Guohua, AU - Jia,Miao, AU - Liu,Ting, AU - Zhang,Xueyao, AU - Guo,Yaping, AU - Zhu,Kun Yan, AU - Ma,Enbo, AU - Zhang,Jianzhen, Y1 - 2011/11/02/ PY - 2011/09/26/received PY - 2011/10/26/revised PY - 2011/10/27/accepted PY - 2011/11/15/entrez PY - 2011/11/15/pubmed PY - 2012/4/17/medline SP - 220 EP - 7 JF - Journal of insect physiology JO - J Insect Physiol VL - 58 IS - 2 N2 - Glutathione S-transferases (GSTs) play a major role in detoxification of xenobiotics and resistance to insecticides in insects. In the present study, a sigma-class GST gene (LmGSTs3) was identified from the locust, Locusta migratoria manilensis. Its full-length cDNA sequence is 828 bp containing an open reading frame (ORF) of 612 bp that encodes 204 amino acid residues. The predicted protein molecular mass and pI are 23.4 kDa and 7.62, respectively. Recombinant LmGSTs3 was heterologously expressed in Escherichia coli as a soluble fusion protein. Its optimal activity was observed at pH 8.0. Incubation for 30 min at temperatures below 40 °C scarcely affected activity. The LmGSTs3 at pH values between 4.0 and 11.0 retained more than 80% of its original activity. Ethacrynic acid and cibacron blue were very effective inhibitors of LmGSTs3 with I50-values 1.7 and 3.7 μM, respectively. In response to heavy metal (CuSO4, CdCl2) exposure there was a concentration-dependent and time-dependent decrease in activity. The nymph mortalities after carbaryl treatment increased 38.7% after LmGSTs3 were silenced. These results suggest that LmGSTs3 may be involved in carbaryl detoxification in L. migratoria manilensis. SN - 1879-1611 UR - https://www.unboundmedicine.com/medline/citation/22075389/Heterologous_expression_and_characterization_of_a_sigma_glutathione_S_transferase_involved_in_carbaryl_detoxification_from_oriental_migratory_locust_Locusta_migratoria_manilensis__Meyen__ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0022-1910(11)00315-5 DB - PRIME DP - Unbound Medicine ER -