Abstract：
:We have identified the 2-Cys peroxiredoxin (Prx) from a bovine Babesia parasite, B. bovis. Prx is a recently described family of antioxidant enzymes that are highly conserved in eukaryotes and prokaryotes. B. bovis 2-Cys Prx (BbTPx-1) contained two conserved cysteine residues that corresponded to Cys47 and Cys170 of the yeast Prx and the amino acid sequences of two catalytic domains showed significant similarities to those of mammalian typical 2-Cys Prx. The antioxidant activity of the recombinant BbTPx-1 protein expressed in E. coli was demonstrated by a thiol mixed-function oxidation assay. Furthermore, we confirmed that BbTPx-1 was expressed in the cytoplasm of intra-erythrocytic B. bovis merozites. These results suggest that B. bovis likely uses TPx-1 as a way to reduce peroxides as a control of its intracellular redox balance so that it can live and grow in the host cell.
journal_name
Parasitol Resjournal_title
Parasitology researchauthors
Tanaka M,Sakurai T,Yokoyama N,Inoue N,Kawazu Sdoi
10.1007/s00436-009-1587-6subject
Has Abstractpub_date
2009-10-01 00:00:00pages
1473-7issue
5eissn
0932-0113issn
1432-1955journal_volume
105pub_type
杂志文章abstract：:The tegumental membrane of platyhelminth parasites is of crucial importance for modulation of the host response and parasite survival. A cDNA encoding a novel tegumental protein 20.8 kDa (TP20.8) was found by large-scale sequencing of a Clonorchis sinensis cDNA library. This new cDNA was 755 bp long containing an open...
journal_title：Parasitology research
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journal_title：Parasitology research
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更新日期：1999-08-01 00:00:00
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journal_title：Parasitology research
pub_type： 杂志文章,多中心研究
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journal_title：Parasitology research
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journal_title：Parasitology research
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更新日期：2009-03-01 00:00:00
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journal_title：Parasitology research
pub_type： 杂志文章,评审
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journal_title：Parasitology research
pub_type： 杂志文章
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更新日期：1989-01-01 00:00:00
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journal_title：Parasitology research
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doi：10.1007/s00436-015-4697-3
更新日期：2015-10-01 00:00:00
