Source:http://linkedlifedata.com/resource/pubmed/id/20602114
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
2010-9-8
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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.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Helminth,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Helminth,
http://linkedlifedata.com/resource/pubmed/chemical/HSP70 Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/HSP72 Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Helminth Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Molecular Chaperones,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/mortalin
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
1432-1955
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
107
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
955-66
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pubmed:meshHeading |
pubmed-meshheading:20602114-Animals,
pubmed-meshheading:20602114-Antibodies, Helminth,
pubmed-meshheading:20602114-Blotting, Western,
pubmed-meshheading:20602114-Computational Biology,
pubmed-meshheading:20602114-DNA, Complementary,
pubmed-meshheading:20602114-DNA, Helminth,
pubmed-meshheading:20602114-Escherichia coli,
pubmed-meshheading:20602114-Female,
pubmed-meshheading:20602114-Gene Expression,
pubmed-meshheading:20602114-Gene Expression Profiling,
pubmed-meshheading:20602114-HSP70 Heat-Shock Proteins,
pubmed-meshheading:20602114-HSP72 Heat-Shock Proteins,
pubmed-meshheading:20602114-Helminth Proteins,
pubmed-meshheading:20602114-Leukocytes, Mononuclear,
pubmed-meshheading:20602114-Mass Spectrometry,
pubmed-meshheading:20602114-Mice,
pubmed-meshheading:20602114-Mice, Inbred BALB C,
pubmed-meshheading:20602114-Molecular Chaperones,
pubmed-meshheading:20602114-Molecular Weight,
pubmed-meshheading:20602114-Rabbits,
pubmed-meshheading:20602114-Recombinant Proteins,
pubmed-meshheading:20602114-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:20602114-Schistosoma japonicum,
pubmed-meshheading:20602114-Schistosomiasis japonica,
pubmed-meshheading:20602114-Sequence Homology, Amino Acid,
pubmed-meshheading:20602114-Vaccination
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pubmed:year |
2010
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pubmed:articleTitle |
Molecular and functional characterization of a mortalin-like protein from Schistosoma japonicum (SjMLP/hsp70) as a member of the HSP70 family.
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pubmed:affiliation |
Department of Parasitology, Zhongshan School of Medicine, SunYat-sen University, 74 Zhongshan 2nd Road, Guangzhou, 510080, People's Republic of China.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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