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Thioredoxin from Brugia malayi: defining a 16-kilodalton class of thioredoxins from nematodes.
Infect Immun. 2003 Jul; 71(7):4119-26.II

Abstract

Thioredoxins are a family of small redox proteins that undergo NADPH-dependent reduction by thioredoxin reductase. This results in a supply of reducing equivalents that cells use in a wide variety of biological reactions, which include maintaining reduced forms of the enzymes important for protection against damage from high-energy oxygen radicals, the regulation of transcription factor activity, and the inhibition of apoptosis. Here we report on a new member of the thioredoxin family of proteins from the filarial nematode Brugia malayi, Bm-TRX-1, which defines a new subclass of 16-kDa thioredoxins that occur widely in nematodes, including Caenorhabditis elegans. In addition to being larger than the thioredoxins found in mammalian and bacterial species, the putative active site sequence of Bm-TRX-1, WCPPC, does not conform to the highly conserved WCGPC reported for thioredoxins from mammals to bacteria. Interestingly, an allelic form of Bm-TRX-1 was identified with an active site sequence WCPQC, which appears to be unique to the thioredoxins from filarial species. Bm-TRX-1 was between 98% and 35% identical to thioredoxins from other nematodes and approximately 20% identical to the thioredoxins from mammals and Escherichia coli. Bm-TRX-1 was constitutively transcribed throughout the B. malayi life cycle, and Bm-TRX protein was detectable in somatic extracts and excretory-secretory products from adults and microfilariae. Recombinant Bm-TRX-1 had thiodisulfide reductase activity, as measured by the reduction of insulin, and protected DNA from the nicking activity of oxygen radicals. Overexpression of Bm-TRX-1 in a human monocyte cell line negatively regulated tumor necrosis factor alpha-induced p38 mitogen-activated protein kinase activity, suggesting a possible role of the 16-kDa Bm-TRX-1 in immunomodulation.

Authors+Show Affiliations

Centre for Biotechnology, Anna University, Chennai, India.No 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

12819103

Citation

Kunchithapautham, Kannan, et al. "Thioredoxin From Brugia Malayi: Defining a 16-kilodalton Class of Thioredoxins From Nematodes." Infection and Immunity, vol. 71, no. 7, 2003, pp. 4119-26.
Kunchithapautham K, Padmavathi B, Narayanan RB, et al. Thioredoxin from Brugia malayi: defining a 16-kilodalton class of thioredoxins from nematodes. Infect Immun. 2003;71(7):4119-26.
Kunchithapautham, K., Padmavathi, B., Narayanan, R. B., Kaliraj, P., & Scott, A. L. (2003). Thioredoxin from Brugia malayi: defining a 16-kilodalton class of thioredoxins from nematodes. Infection and Immunity, 71(7), 4119-26.
Kunchithapautham K, et al. Thioredoxin From Brugia Malayi: Defining a 16-kilodalton Class of Thioredoxins From Nematodes. Infect Immun. 2003;71(7):4119-26. PubMed PMID: 12819103.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Thioredoxin from Brugia malayi: defining a 16-kilodalton class of thioredoxins from nematodes. AU - Kunchithapautham,Kannan, AU - Padmavathi,B, AU - Narayanan,R B, AU - Kaliraj,P, AU - Scott,Alan L, PY - 2003/6/24/pubmed PY - 2003/7/23/medline PY - 2003/6/24/entrez SP - 4119 EP - 26 JF - Infection and immunity JO - Infect Immun VL - 71 IS - 7 N2 - Thioredoxins are a family of small redox proteins that undergo NADPH-dependent reduction by thioredoxin reductase. This results in a supply of reducing equivalents that cells use in a wide variety of biological reactions, which include maintaining reduced forms of the enzymes important for protection against damage from high-energy oxygen radicals, the regulation of transcription factor activity, and the inhibition of apoptosis. Here we report on a new member of the thioredoxin family of proteins from the filarial nematode Brugia malayi, Bm-TRX-1, which defines a new subclass of 16-kDa thioredoxins that occur widely in nematodes, including Caenorhabditis elegans. In addition to being larger than the thioredoxins found in mammalian and bacterial species, the putative active site sequence of Bm-TRX-1, WCPPC, does not conform to the highly conserved WCGPC reported for thioredoxins from mammals to bacteria. Interestingly, an allelic form of Bm-TRX-1 was identified with an active site sequence WCPQC, which appears to be unique to the thioredoxins from filarial species. Bm-TRX-1 was between 98% and 35% identical to thioredoxins from other nematodes and approximately 20% identical to the thioredoxins from mammals and Escherichia coli. Bm-TRX-1 was constitutively transcribed throughout the B. malayi life cycle, and Bm-TRX protein was detectable in somatic extracts and excretory-secretory products from adults and microfilariae. Recombinant Bm-TRX-1 had thiodisulfide reductase activity, as measured by the reduction of insulin, and protected DNA from the nicking activity of oxygen radicals. Overexpression of Bm-TRX-1 in a human monocyte cell line negatively regulated tumor necrosis factor alpha-induced p38 mitogen-activated protein kinase activity, suggesting a possible role of the 16-kDa Bm-TRX-1 in immunomodulation. SN - 0019-9567 UR - https://www.unboundmedicine.com/medline/citation/12819103/Thioredoxin_from_Brugia_malayi:_defining_a_16_kilodalton_class_of_thioredoxins_from_nematodes_ L2 - https://journals.asm.org/doi/10.1128/IAI.71.7.4119-4126.2003?url_ver=Z39.88-2003&rfr_id=ori:rid:crossref.org&rfr_dat=cr_pub=pubmed DB - PRIME DP - Unbound Medicine ER -