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Thioredoxin peroxidase from Onchocerca volvulus: a major hydrogen peroxide detoxifying enzyme in filarial parasites.
Mol Biochem Parasitol. 1998 Mar 15; 91(2):221-35.MB

Abstract

Random screening of an Onchocerca volvulus third-stage (L3) cDNA library identified a highly abundant cDNA encoding a newly discovered antioxidant enzyme, thioredoxin peroxidase (TPx), a member of the peroxidoxin superfamily. This TPx cDNA (Ov-tpx-2) encodes a polypeptide of 199 amino acid residues with a calculated molecular weight of 21,890 Da. The Ov-tpx-2 cDNA represents roughly 2.5% of the total cDNAs from the L3 cDNA library. The gene was expressed in Escherichia coli and the protein product was shown to have antioxidant activity. Antiserum raised against Ov-TPX-2 recognized a native protein from extracts of both the L3 and adult-stages with a molecular weight of 22 kD. The localization and stage-specificity of Ov-TPX-2 protein was analyzed by immunocytochemistry and immunoelectron microscopy using monospecific antibodies. Expression was detected in late first-stage larvae during development in the vector and increased in intensity during differentiation to the infective L3-stage. The antigen was also detected in post-infective larvae and adult worms. In larvae, Ov-TPX-2 protein was predominantly localized to the hypodermis and cuticle, with additional sites in the hypodermal chords and multivesicular bodies. In adult worms, the primary sites of expression were the uterine epithelium and intestine, with additional labeling of the body wall and cuticle. Developing embryos and microfilariae in utero were bathed in Ov-TPX-2 protein discharged from epithelial cells. These results suggest that Ov-TPX-2 may protect the parasites from being damaged by host-generated oxidative stress and that Ov-TPX-2 protein provides the H2O2-detoxifying activity predicted but not previously identified in filarial parasites. Its highly upregulated expression in infective larvae may aid in parasite establishment following transmission to the definitive host.

Authors+Show Affiliations

Department of Biological Sciences, Clark Science Center, Smith College, Northampton, MA 01063, USA.No 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

9566516

Citation

Lu, W, et al. "Thioredoxin Peroxidase From Onchocerca Volvulus: a Major Hydrogen Peroxide Detoxifying Enzyme in Filarial Parasites." Molecular and Biochemical Parasitology, vol. 91, no. 2, 1998, pp. 221-35.
Lu W, Egerton GL, Bianco AE, et al. Thioredoxin peroxidase from Onchocerca volvulus: a major hydrogen peroxide detoxifying enzyme in filarial parasites. Mol Biochem Parasitol. 1998;91(2):221-35.
Lu, W., Egerton, G. L., Bianco, A. E., & Williams, S. A. (1998). Thioredoxin peroxidase from Onchocerca volvulus: a major hydrogen peroxide detoxifying enzyme in filarial parasites. Molecular and Biochemical Parasitology, 91(2), 221-35.
Lu W, et al. Thioredoxin Peroxidase From Onchocerca Volvulus: a Major Hydrogen Peroxide Detoxifying Enzyme in Filarial Parasites. Mol Biochem Parasitol. 1998 Mar 15;91(2):221-35. PubMed PMID: 9566516.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Thioredoxin peroxidase from Onchocerca volvulus: a major hydrogen peroxide detoxifying enzyme in filarial parasites. AU - Lu,W, AU - Egerton,G L, AU - Bianco,A E, AU - Williams,S A, PY - 1998/5/5/pubmed PY - 1998/5/5/medline PY - 1998/5/5/entrez SP - 221 EP - 35 JF - Molecular and biochemical parasitology JO - Mol Biochem Parasitol VL - 91 IS - 2 N2 - Random screening of an Onchocerca volvulus third-stage (L3) cDNA library identified a highly abundant cDNA encoding a newly discovered antioxidant enzyme, thioredoxin peroxidase (TPx), a member of the peroxidoxin superfamily. This TPx cDNA (Ov-tpx-2) encodes a polypeptide of 199 amino acid residues with a calculated molecular weight of 21,890 Da. The Ov-tpx-2 cDNA represents roughly 2.5% of the total cDNAs from the L3 cDNA library. The gene was expressed in Escherichia coli and the protein product was shown to have antioxidant activity. Antiserum raised against Ov-TPX-2 recognized a native protein from extracts of both the L3 and adult-stages with a molecular weight of 22 kD. The localization and stage-specificity of Ov-TPX-2 protein was analyzed by immunocytochemistry and immunoelectron microscopy using monospecific antibodies. Expression was detected in late first-stage larvae during development in the vector and increased in intensity during differentiation to the infective L3-stage. The antigen was also detected in post-infective larvae and adult worms. In larvae, Ov-TPX-2 protein was predominantly localized to the hypodermis and cuticle, with additional sites in the hypodermal chords and multivesicular bodies. In adult worms, the primary sites of expression were the uterine epithelium and intestine, with additional labeling of the body wall and cuticle. Developing embryos and microfilariae in utero were bathed in Ov-TPX-2 protein discharged from epithelial cells. These results suggest that Ov-TPX-2 may protect the parasites from being damaged by host-generated oxidative stress and that Ov-TPX-2 protein provides the H2O2-detoxifying activity predicted but not previously identified in filarial parasites. Its highly upregulated expression in infective larvae may aid in parasite establishment following transmission to the definitive host. SN - 0166-6851 UR - https://www.unboundmedicine.com/medline/citation/9566516/Thioredoxin_peroxidase_from_Onchocerca_volvulus:_a_major_hydrogen_peroxide_detoxifying_enzyme_in_filarial_parasites_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0166-6851(97)00230-2 DB - PRIME DP - Unbound Medicine ER -