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Thioredoxin peroxidases from Brugia malayi.
Mol Biochem Parasitol. 1998 Mar 15; 91(2):207-20.MB

Abstract

Parasite-derived antioxidant proteins have been implicated in playing an important role in protection against the oxygen radicals that are generated during aerobic metabolism and in defense against host immune cell attack. Here we report that filarial nematodes include the thioredoxin peroxidase/thiol-specific antioxidant (TPx/TSA) family of antioxidant proteins as part of their complex defense against radical-mediated damage. At the protein level, the TPx/TSA from Brugia malayi (Bm-TPx-1) was approximately 50% identical and approximately 60% similar to TPx/TSAs from mammals, amphibians and yeast. Bm-TPx-1 was also approximately 60% identical to putative TPx proteins from a related filarial nematode, Onchocerca volvulus, and from the free-living nematode Caenorhabditis elegans. That B. malayi may express multiple forms of molecules with TPx/TSA activity was indicated by the identification of a B. malayi gene encoding a second, distinct member of the TPx/TSA family (Bm-tpx-2). Bm-tpx-1 was found to be transcribed in all stages of the parasite present in the mammalian host and the 25 kDa translation product was present in all of the developmental stages studied. The results of immunohistochemical, immunofluorescent and immunoprecipitation studies showed Bm-TPx-1 to be localized in the cells of the hypodermis/lateral chord in adult parasites and not to be present at the surface or in excretory/secretory products. The distribution in the parasite suggests that Bm-TPx-1 may play its major role in countering radicals produced within cells. A recombinant form of Bm-TPx-1 was biologically active and capable of protecting DNA from oxygen radical-mediated damage. Thioredoxin peroxidases may prove to be a critical component in the parasite's defense against injury caused by oxygen radicals derived from endogenous and exogenous sources.

Authors+Show Affiliations

Department of Molecular Microbiology and Immunology, School of Hygiene and Public Health, Johns Hopkins University, Baltimore, MD 21205, USA.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

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

Language

eng

PubMed ID

9566515

Citation

Ghosh, I, et al. "Thioredoxin Peroxidases From Brugia Malayi." Molecular and Biochemical Parasitology, vol. 91, no. 2, 1998, pp. 207-20.
Ghosh I, Eisinger SW, Raghavan N, et al. Thioredoxin peroxidases from Brugia malayi. Mol Biochem Parasitol. 1998;91(2):207-20.
Ghosh, I., Eisinger, S. W., Raghavan, N., & Scott, A. L. (1998). Thioredoxin peroxidases from Brugia malayi. Molecular and Biochemical Parasitology, 91(2), 207-20.
Ghosh I, et al. Thioredoxin Peroxidases From Brugia Malayi. Mol Biochem Parasitol. 1998 Mar 15;91(2):207-20. PubMed PMID: 9566515.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Thioredoxin peroxidases from Brugia malayi. AU - Ghosh,I, AU - Eisinger,S W, AU - Raghavan,N, AU - Scott,A L, PY - 1998/5/5/pubmed PY - 1998/5/5/medline PY - 1998/5/5/entrez SP - 207 EP - 20 JF - Molecular and biochemical parasitology JO - Mol Biochem Parasitol VL - 91 IS - 2 N2 - Parasite-derived antioxidant proteins have been implicated in playing an important role in protection against the oxygen radicals that are generated during aerobic metabolism and in defense against host immune cell attack. Here we report that filarial nematodes include the thioredoxin peroxidase/thiol-specific antioxidant (TPx/TSA) family of antioxidant proteins as part of their complex defense against radical-mediated damage. At the protein level, the TPx/TSA from Brugia malayi (Bm-TPx-1) was approximately 50% identical and approximately 60% similar to TPx/TSAs from mammals, amphibians and yeast. Bm-TPx-1 was also approximately 60% identical to putative TPx proteins from a related filarial nematode, Onchocerca volvulus, and from the free-living nematode Caenorhabditis elegans. That B. malayi may express multiple forms of molecules with TPx/TSA activity was indicated by the identification of a B. malayi gene encoding a second, distinct member of the TPx/TSA family (Bm-tpx-2). Bm-tpx-1 was found to be transcribed in all stages of the parasite present in the mammalian host and the 25 kDa translation product was present in all of the developmental stages studied. The results of immunohistochemical, immunofluorescent and immunoprecipitation studies showed Bm-TPx-1 to be localized in the cells of the hypodermis/lateral chord in adult parasites and not to be present at the surface or in excretory/secretory products. The distribution in the parasite suggests that Bm-TPx-1 may play its major role in countering radicals produced within cells. A recombinant form of Bm-TPx-1 was biologically active and capable of protecting DNA from oxygen radical-mediated damage. Thioredoxin peroxidases may prove to be a critical component in the parasite's defense against injury caused by oxygen radicals derived from endogenous and exogenous sources. SN - 0166-6851 UR - https://www.unboundmedicine.com/medline/citation/9566515/Thioredoxin_peroxidases_from_Brugia_malayi_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0166-6851(97)00213-2 DB - PRIME DP - Unbound Medicine ER -