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Identification and characterization of an atypical 2-cys peroxiredoxin from the silkworm, Bombyx mori.
Insect Mol Biol. 2016 08; 25(4):347-54.IM

Abstract

Peroxiredoxins (Prxs) play an important role in the protection of insects against the toxicity of reactive oxygen species. Here, we identified and characterized a novel, atypical 2-cysteine (Cys) peroxiredoxin (BmPrx3) from an expressed sequence tag database in a lepidopteran insect, Bombyx mori. The BmPrx3 cDNA contained an open reading frame of 684 bp that encodes a 228-amino-acid protein with a calculated molecular mass of 25 kDa. Sequence comparison revealed that BmPrx3 belongs to the atypical 2-Cys Prxs. Quantitative real-time PCR revealed that BmPrx3 can be detected in all tissues and developmental stages. Recombinant BmPrx3 purified from Escherichia coli exhibited antioxidant activity that removed hydrogen peroxide and protected DNA from oxidative damage. Disc diffusion and viability assays revealed that recombinant BmPrx3 increased bacterial survival under H2 O2 -mediated oxidative stress. In addition, quantitative real-time PCR analysis indicated that BmPrx3 transcription levels were significantly increased in response to various oxidative stresses. Furthermore, BmPrx3 transcription levels in the midgut were regulated by bacterial infection. Taken together, these results suggest that BmPrx3 acts as an antioxidant enzyme to protect the silkworm from various oxidative stresses.

Authors+Show Affiliations

Institute of Life Sciences, Jiangsu University, Zhenjiang, Jiangsu, China.Institute of Life Sciences, Jiangsu University, Zhenjiang, Jiangsu, China.Institute of Life Sciences, Jiangsu University, Zhenjiang, Jiangsu, China.School of Medicine, Jiangsu University, Zhenjiang, China.

Pub Type(s)

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

Language

eng

PubMed ID

26969823

Citation

Wang, Q, et al. "Identification and Characterization of an Atypical 2-cys Peroxiredoxin From the Silkworm, Bombyx Mori." Insect Molecular Biology, vol. 25, no. 4, 2016, pp. 347-54.
Wang Q, Zhou Y, Chen K, et al. Identification and characterization of an atypical 2-cys peroxiredoxin from the silkworm, Bombyx mori. Insect Mol Biol. 2016;25(4):347-54.
Wang, Q., Zhou, Y., Chen, K., & Ju, X. (2016). Identification and characterization of an atypical 2-cys peroxiredoxin from the silkworm, Bombyx mori. Insect Molecular Biology, 25(4), 347-54. https://doi.org/10.1111/imb.12224
Wang Q, et al. Identification and Characterization of an Atypical 2-cys Peroxiredoxin From the Silkworm, Bombyx Mori. Insect Mol Biol. 2016;25(4):347-54. PubMed PMID: 26969823.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Identification and characterization of an atypical 2-cys peroxiredoxin from the silkworm, Bombyx mori. AU - Wang,Q, AU - Zhou,Y, AU - Chen,K, AU - Ju,X, Y1 - 2016/03/11/ PY - 2016/3/13/entrez PY - 2016/3/13/pubmed PY - 2017/9/13/medline KW - Bombyx mori KW - antioxidant activity KW - oxidative stress KW - peroxiredoxin 3 SP - 347 EP - 54 JF - Insect molecular biology JO - Insect Mol. Biol. VL - 25 IS - 4 N2 - Peroxiredoxins (Prxs) play an important role in the protection of insects against the toxicity of reactive oxygen species. Here, we identified and characterized a novel, atypical 2-cysteine (Cys) peroxiredoxin (BmPrx3) from an expressed sequence tag database in a lepidopteran insect, Bombyx mori. The BmPrx3 cDNA contained an open reading frame of 684 bp that encodes a 228-amino-acid protein with a calculated molecular mass of 25 kDa. Sequence comparison revealed that BmPrx3 belongs to the atypical 2-Cys Prxs. Quantitative real-time PCR revealed that BmPrx3 can be detected in all tissues and developmental stages. Recombinant BmPrx3 purified from Escherichia coli exhibited antioxidant activity that removed hydrogen peroxide and protected DNA from oxidative damage. Disc diffusion and viability assays revealed that recombinant BmPrx3 increased bacterial survival under H2 O2 -mediated oxidative stress. In addition, quantitative real-time PCR analysis indicated that BmPrx3 transcription levels were significantly increased in response to various oxidative stresses. Furthermore, BmPrx3 transcription levels in the midgut were regulated by bacterial infection. Taken together, these results suggest that BmPrx3 acts as an antioxidant enzyme to protect the silkworm from various oxidative stresses. SN - 1365-2583 UR - https://www.unboundmedicine.com/medline/citation/26969823/Identification_and_characterization_of_an_atypical_2_cys_peroxiredoxin_from_the_silkworm_Bombyx_mori_ L2 - https://doi.org/10.1111/imb.12224 DB - PRIME DP - Unbound Medicine ER -