Schistosoma mansoni heat shock protein 70 elicits an early humoral immune response in S. mansoni infected baboons

Kanamura, Hermínia Yohko; Hancock, Kathy; Rodrigues, Vanderlei; Damian, Raymond T.

doi:10.1590/s0074-02762002000500022

Cited by 29 publications

(23 citation statements)

References 26 publications

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“…SmHSP70 elicits an early humoral immune response and may be a valid target for immunodiagnosis (69). However, when used as a diagnostic antigen, SmHSP70 cross-reacted with antibodies in sera from humans infected with schistosomes, filariae, and malaria but did not cross-react with sera from patients infected with S. japonicum (70).…”

Section: Discussionmentioning

confidence: 99%

Excretory/Secretory Proteome of the Adult Developmental Stage of Human Blood Fluke, Schistosoma japonicum

Liu

Cui

et al. 2009

Molecular & Cellular Proteomics

166

139

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Schistosomes are the causative agents of schistosomiasis, one of the most prevalent and serious of the parasitic diseases that currently infects ϳ200 million people worldwide. Schistosome excretory/secretory (ES) proteins have been shown to play important roles in modulating mammalian host immune systems. In our current study, we performed a global proteomics identification of the ES proteins from adult worms of Schistosoma japonicum, one of the three major schistosome species. Our results unambiguously identified 101 proteins, including 53 putatively secreted proteins. By quantitative analysis, we revealed fatty acid-binding protein as a major constituent of the in vitro ES proteome. Strikingly the heat shock proteins HSP70s, HSP90, and HSP97 constituted the largest protein family in the ES proteome, implying a central role for these proteins in immunomodulation in the hostparasite relationship. Other important S. japonicum ES proteins included actins, 14-3-3, aminopeptidase, enolase, and glyceraldehyde-3-phosphate dehydrogenase, some of which have been considered as viable vaccine candidates and therapeutic targets. A comparison with previous studies suggests that 48.5% of S. japonicum ES proteins are common to other parasite ES products, indicating that the molecular mechanisms involved in evading the host immune response may be conserved across different parasites. Interestingly seven host proteins, including antimicrobial protein CAP18, immunoglobulins, and a complement component, were identified among in vitro S. japonicum ES products likely originating from the schistosome tegument or gut, indicating that host innate and acquired immune systems could defend against schistosome invasion. Our present study represents the first attempt at profiling S. japonicum ES proteins, provides an insight into host-parasite interactions, and establishes a resource for the devel-

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Section: Discussionmentioning

confidence: 99%

Excretory/Secretory Proteome of the Adult Developmental Stage of Human Blood Fluke, Schistosoma japonicum

Liu

Cui

et al. 2009

Molecular & Cellular Proteomics

166

139

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“…This immune response was due to the activation of the NF-κB pathway, via the interaction between HSP70 and toll-like receptor 2 and/or 4 (TLR-2/ 4). In a recent study, Kanamura et al (2002) found that SmHSP70 could elicit an early humoral immune response in S. mansoni-infected baboons. In our study, we found that rSjMLP/hsp70 could elicit both the Th1-type and Th2-type immune response, particularly the Th1-type immune response, suggesting that the anti-rSjMLP/hsp70 immune response was mediated by both CD4 + and CD8 + T cells, but predominantly by the CD8 + T cells.…”

Section: Discussionmentioning

confidence: 98%

Molecular and functional characterization of a mortalin-like protein from Schistosoma japonicum (SjMLP/hsp70) as a member of the HSP70 family

et al. 2010

Parasitol Res

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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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“…Different antigenic preparations that are considered useful for diagnosis include worm proteins Sm31 and Sm32 (El-Sayed et al 1998), gut-associated polysaccharide (Oliveira et al 2005), and heat-shock protein 70 (Kanamura et al 2002).…”

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confidence: 99%

“…The use of recombinant S. mansoni HSP70 (SmHSP70) for immunodiagnostic purposes was suggested (Moser et al 1990), but few reports are found in the literature about the frequency of anti-SmHSP70 antibodies in healthy individuals and in patients with autoimmune diseases (Arora et al 1995). There is also a need to better identify the epitopes of the HSP70 specifically recognized by the host (Kanamura et al 2002).…”

mentioning

confidence: 99%

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Application of synthetic peptides in development of a serologic method for laboratory diagnosis of schistosomiasis mansoni

Oliveira

Kanamura

Takei

et al. 2006

Mem. Inst. Oswaldo Cruz

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Schistosoma mansoni heat shock protein 70 elicits an early humoral immune response in S. mansoni infected baboons

Cited by 29 publications

References 26 publications

Excretory/Secretory Proteome of the Adult Developmental Stage of Human Blood Fluke, Schistosoma japonicum

Excretory/Secretory Proteome of the Adult Developmental Stage of Human Blood Fluke, Schistosoma japonicum

Molecular and functional characterization of a mortalin-like protein from Schistosoma japonicum (SjMLP/hsp70) as a member of the HSP70 family

Application of synthetic peptides in development of a serologic method for laboratory diagnosis of schistosomiasis mansoni

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