pubmed-article:20602114 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:20602114 | lifeskim:mentions | umls-concept:C0015576 | lld:lifeskim |
pubmed-article:20602114 | lifeskim:mentions | umls-concept:C0680022 | lld:lifeskim |
pubmed-article:20602114 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:20602114 | lifeskim:mentions | umls-concept:C0243043 | lld:lifeskim |
pubmed-article:20602114 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
pubmed-article:20602114 | lifeskim:mentions | umls-concept:C1521991 | lld:lifeskim |
pubmed-article:20602114 | lifeskim:mentions | umls-concept:C0036317 | lld:lifeskim |
pubmed-article:20602114 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
pubmed-article:20602114 | pubmed:issue | 4 | lld:pubmed |
pubmed-article:20602114 | pubmed:dateCreated | 2010-9-8 | lld:pubmed |
pubmed-article:20602114 | pubmed:abstractText | Schistosomes are the causative agent of schistosomiasis. The 70-kDa heat-shock proteins (HSP70) are considered the predominant HSP family and play a key regulatory role in parasite development and pathogenesis. Based on the published sequences in Genbank/EMBL, an open-reading frame (ORF) encoding 653 amino acids (XP_002581385.1) and belonging to the Schistosoma HSP70 protein family with a molecular weight of 71.49 kDa was identified by bioinformatic analysis. Since the sequence shared 77% identity with the published full-length Homo sapiens HSP70 protein, it was named Schistosoma mortalin-like protein (MLP/Hsp70). Here, we report the molecular and functional characterization of the Schistosoma japonicum SjMLP/hsp70 as a member of the HSP70 family. The complete SjMLP/hsp70 coding sequence was amplified from a S. japonicum adult worm cDNA library by polymerase chain reaction (PCR) and subcloned into the pET28a expression vector. The purified recombinant protein, rSjMLP/hsp70, was identified as a member of 70-kDa HSP family by mass spectrometry and could be recognized by the S. japonicum-infected mouse serum. Reverse transcriptase polymerase chain reaction (RT-PCR) and western blotting analysis revealed that SjMLP/hsp70 was widely expressed in the eggs, cercariae, schistosomula, and adult worms of S. japonicum. A thermotolerance assay showed that rSjMLP/hsp70 could protect Escherichia coli cells from heat damage. This chaperone-like activity was demonstrated by full-length SjMLP/hsp70. The detection of specific antibody levels by indirect enzyme-linked immunosorbent assay and IFN-gamma secretion of splenocytes by ELISpot assay suggested that mice immunized with SjMLP/hsp70 were able to elicit Th1-type bias immune response. The challenge-protective experiment showed that DNA vaccine of SjGST combined with SjMLP/hsp70 could induce a 31.31% reduction of worm burden and 58.59% reduction of egg burden in intestinal tissue of immunized mice. Our results imply that SjMLP/hsp70 has a potential adjuvant function and might be a vaccine candidate for schistosomiaisis, which is the first report of the expression and preliminary characterization analysis of this molecule. | lld:pubmed |
pubmed-article:20602114 | pubmed:language | eng | lld:pubmed |
pubmed-article:20602114 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20602114 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:20602114 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20602114 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20602114 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20602114 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20602114 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20602114 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20602114 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20602114 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20602114 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20602114 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:20602114 | pubmed:month | Sep | lld:pubmed |
pubmed-article:20602114 | pubmed:issn | 1432-1955 | lld:pubmed |
pubmed-article:20602114 | pubmed:author | pubmed-author:YaoQQ | lld:pubmed |
pubmed-article:20602114 | pubmed:author | pubmed-author:RoeP EPE | lld:pubmed |
pubmed-article:20602114 | pubmed:author | pubmed-author:YangJieJ | lld:pubmed |
pubmed-article:20602114 | pubmed:author | pubmed-author:HeSijieS | lld:pubmed |
pubmed-article:20602114 | pubmed:author | pubmed-author:LiShuS | lld:pubmed |
pubmed-article:20602114 | pubmed:author | pubmed-author:CaoJianpingJ | lld:pubmed |
pubmed-article:20602114 | pubmed:author | pubmed-author:ZhengHuanqinH | lld:pubmed |
pubmed-article:20602114 | pubmed:author | pubmed-author:WuZhongdaoZ | lld:pubmed |
pubmed-article:20602114 | pubmed:author | pubmed-author:LvZhiyueZ | lld:pubmed |
pubmed-article:20602114 | pubmed:author | pubmed-author:YangLinlinL | lld:pubmed |
pubmed-article:20602114 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:20602114 | pubmed:volume | 107 | lld:pubmed |
pubmed-article:20602114 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:20602114 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:20602114 | pubmed:pagination | 955-66 | lld:pubmed |
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pubmed-article:20602114 | pubmed:year | 2010 | lld:pubmed |
pubmed-article:20602114 | pubmed:articleTitle | Molecular and functional characterization of a mortalin-like protein from Schistosoma japonicum (SjMLP/hsp70) as a member of the HSP70 family. | lld:pubmed |
pubmed-article:20602114 | pubmed:affiliation | Department of Parasitology, Zhongshan School of Medicine, SunYat-sen University, 74 Zhongshan 2nd Road, Guangzhou, 510080, People's Republic of China. | lld:pubmed |
pubmed-article:20602114 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:20602114 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |