期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 277, 期 34, 页码 31207-31213出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M204114200
关键词
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资金
- NIAID NIH HHS [R01 AI039066, R29 AI039066, R01 AI039066-06A2, N01 AI 55270, AI 39066, R01 AI039066-08] Funding Source: Medline
A homologue of the mammalian translationally controlled tumor protein (TCTP) was cloned from the human parasite Schistosoma mansoni (SmTCTP). Sequence analysis showed that SmTCTP differed from other reported TCTPs in having only one signature sequence. Subsequently, SmTCTP was cloned in a T7 expression system and expressed as a histidine-tagged fusion protein. Recombinant SmTCTP (rSmTCTP) has a molecular mass of similar to23 kDa with the histidine tag. Further analysis showed that SmTCTP transcripts and protein are expressed in all life cycle stages of the parasite within the vertebrate hosts. Interestingly, antibodies to SmTCTP were present in the sera of mice 9 weeks after infection with S. mansoni. Characterization studies showed that rSmTCTP is a calcium-binding protein that can cause histamine release from basophil/mast cells and induce eosinophil infiltration. These findings suggest that SmTCTP may have an important role in the development of allergic inflammatory responses associated with schistosomiasis and may be a target for new drug development.
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