Expression and immunolocalization of the 14-3-3 protein of Schistosoma mansoni

Schechtman, Deborah; Winnen, Ralf; Tarrab‐Hazdai, Rebeca; Ram, Daniela; Shinder, Vera; Grevelding, Christoph G.; Kunz, Werner; Arnon, Ruth

doi:10.1017/s0031182001008769

Cited by 30 publications

(23 citation statements)

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“…The next most abundant ES protein was 14-3-3 protein, which was reported to localize to the excretory system and tegument of female S. mansoni worms (72) and has been used as a vaccine candidate against schistosomiasis (73). In S. japonicum ESP, several cytosolic glycolytic enzymes were unexpectedly identified, including enolase, pyruvate kinase, and GAPDH.…”

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

168

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

168

139

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“…In some parasites, such as Echinococcus multilocularis and Schistosoma mansoni, 14-3-3 proteins have been described to be immunogenic, and therefore have been promoted as potential vaccine targets (Schechtman et al 2001;Siles-Lucas et al 2008;Wang et al 2009). In addition, the 14-3-3 protein has been identified as a prominent product in the S. mansoni female worm reproductive system (Schechtman et al 2001). This may explain previous findings showing the female reproductive system as the main source of antigenic targets useful for the diagnosis of abdominal angiostrongyliasis caused by A. costarecensis (Bender, 2003).…”

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confidence: 99%

The 31-kDa Antigen of Angiostrongylus cantonensis Comprises Distinct Antigenic Glycoproteins

Morassutti

Levert

Perelygin

et al. 2012

Vector-Borne and Zoonotic Diseases

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Human angiostrongyliasis results from accidental infection with Angiostrongylus, an intra-arterial nematode. Angiostrongylus cantonensis infections result in eosinophilic meningitis, and A. costaricensis infections cause eosinophilic enteritis. Immunological methodologies are critical to the diagnosis of both infections, since these parasites cannot be isolated from fecal matter and are rarely found in cerebrospinal fluid samples. A. costaricensis and A. cantonensis share common antigenic epitopes which elicit antibodies that recognize proteins present in either species. Detection of antibodies to a 31-kDa A. cantonensis protein present in crude adult worm extracts is a sensitive and specific method for immunodiagnosis of cerebral angiostrongyliasis. The objective of the present work was to isolate and characterize the 31-kDa proteins using soluble protein extracts derived from adult female worms using both one-(1DE) and two-dimensional (2DE) gel electrophoresis. Separated proteins were blotted onto nitrocellulose and probed using sera from infected and non-infected controls. The 31-kDa band present in 1DE gels and the 4 spots identified in 2DE gels were excised and analyzed by electrospray ionization mass spectrometry. Using the highest scores obtained following Mascot analysis, amino acid sequences were obtained that matched four unique proteins: tropomyosin, the 14-3-3 phosphoserine-binding protein, a protein containing a nascent polypeptide-associated complex domain, and the putative epsilon subunit of coatomer protein complex isoform 2. Oxidative cleavage of diols using sodium m-periodate demonstrated that carbohydrate moieties are essential for the antigenicity of all four spots of the 31-kDa antigen. In this article we describe the identification of the 31-kDa antigen, and provide DNA sequencing of the targets. In conclusion, these data suggest that reactivity to the 31-kDa proteins may represent antibody recognition of more than one protein, and recombinant protein-based assays for cerebral angiostrongyliasis diagnosis may require eukaryotic expression systems to maintain antigenicity.

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“…Mecozzi et al (2000) have demonstrated the localisation of calcineurin to the flame cells of the schistosomula and adult worms and Schechtman et al (2001) have found 14-3-3 protein in the protonephridial system of the female worm.…”

mentioning

confidence: 99%

The effects of drugs, ions, and poly-l-lysine on the excretory system of Schistosoma mansoni

Kusel

Oliveira

Todd

et al. 2006

Mem. Inst. Oswaldo Cruz

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Expression and immunolocalization of the 14-3-3 protein of Schistosoma mansoni

Cited by 30 publications

References 0 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

The 31-kDa Antigen of Angiostrongylus cantonensis Comprises Distinct Antigenic Glycoproteins

The effects of drugs, ions, and poly-l-lysine on the excretory system of Schistosoma mansoni

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