Immunostimulatory property of a synthetic peptide belonging to the soluble ATP diphosphohydro-lase isoform (SmATPDase 2) and immunolocalisation of this protein in the Schistosoma mansoni egg

Mendes, Rita; Gusmão, Michélia Antônia do Nascimento; Maia, Ana Carolina Ribeiro Gomes; Detoni, Michelle de Lima; Porcino, Gabriane Nascimento; Soares, Thais Vieira; Juliano, María A.; Juliano, Luiz; Coelho, Paulo Marcos Zech; Lenzi, Henrique Leonel; Pinto, Priscila de Faria; Vasconcelos, Eveline Gomes

doi:10.1590/s0074-02762011000700005

Cited by 17 publications

(18 citation statements)

References 26 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The analysis with the program ProtParam resulted in the following molecular weights after cleavage: ∼55kDa for SmATPDase2 and ∼45kDa for HsNTPDase6. These results are consistent with previous studies [4,8].…”

Section: Resultssupporting

confidence: 94%

“…The investigation of putative regions of signal peptide and cleavage sites was performed using the predictor SignalPv4.0. The molecular weight of the predicted secretable domain (ECD) of both proteins was calculated using the program ProtParam, in order to corroborate our results with those previously described in the literature [4,8].…”

Section: Detection Of Transmembrane Domain and Signal Peptidesupporting

confidence: 72%

See 1 more Smart Citation

Structural Comparative Analysis of Secreted NTPDase Models of Schistosoma mansoni and Homo sapiens

Souza

Nunes

Vasconcelos

et al. 2014

Advances in Bioinformatics and Computational Biology

Self Cite

View full text Add to dashboard Cite

The control of extracellular nucleoside concentrations by Nucleoside Triphosphate Diphosphohydrolase (NTPDase) is essential in the regulation of the purinergic signalling and also in immune response. In humans, eight members (HsNTPDase) were identified as transmembrane and secreted proteins. In Schistosoma mansoni, the causative agent of schistosomiasis, NTPDases similar to the humans enzymes have also been identified. The expression of these enzymes in S. mansoni (SmATPDases) is related to the weakening of the immune and inflammatory responses of the host against infections. Despite of the high phylogenetic conservation between these proteins, SmATPDases have been reported as molecular target candidates for antischistosomal treatment. In this work, we constructed three-dimensional models for secreted SmATPDase and HsNTPDase6, using comparative modeling technique. The comparative structural analysis aim the investigation of possible differences that could help future works in the development of new therapies that minimize the risk of cross inhibition.

show abstract

Section: Resultssupporting

confidence: 94%

Section: Detection Of Transmembrane Domain and Signal Peptidesupporting

confidence: 72%

Structural Comparative Analysis of Secreted NTPDase Models of Schistosoma mansoni and Homo sapiens

Souza

Nunes

Vasconcelos

et al. 2014

Advances in Bioinformatics and Computational Biology

Self Cite

View full text Add to dashboard Cite

show abstract

“…The developmental expression pattern of SmATPDase2 is quite different from that of SmATPDase1; its highest relative expression is in eggs. This is consistent with strong immunolocalization of SmATPDase2 throughout the S. mansoni egg [33].…”

Section: Discussionsupporting

confidence: 86%

Schistosome apyrase SmATPDase1, but not SmATPDase2, hydrolyses exogenous ATP and ADP

Da’dara¹,

Bhardwaj²,

Skelly³

2014

Purinergic Signalling

View full text Add to dashboard Cite

Schistosomes are parasitic worms that can live in the bloodstream of their vertebrate hosts for many years. It has been proposed that the worms impinge on host purinergic signalling by degrading proinflammatory molecules like ATP as well as prothrombotic mediators like ADP. This capability may help explain the apparent refractoriness of the worms to both immune elimination and thrombus formation. Three distinct ectoenzymes, expressed at the host-exposed surface of the worm's tegument, are proposed to be involved in the catabolism of ATP and ADP. These are alkaline phosphatase (SmAP), phosphodiesterase (SmNPP-5), and ATP diphosphohydrolase (SmATPDase1). It has recently been shown that only one of these enzymes-SmATPDase1-actually degrades exogenous ATP and ADP. However, a second ATP diphosphohydrolase homolog (SmATPDase2) is located in the tegument and has been reported to be released by the worms. It is possible that this enzyme too participates in the cleavage of exogenous nucleotide tri-and di-phosphates. To test this hypothesis, we employed RNA interference (RNAi) to suppress the expression of the schistosome SmATPDase1 and SmATPDase2 genes. We find that only SmATPDase1-suppressed parasites are significantly impaired in their ability to degrade exogenously added ATP or ADP. Suppression of SmATPDase2 does not appreciably affect the worms' ability to catabolize ATP or ADP. Furthermore, we detect no evidence for the secretion or release of an ATP-hydrolyzing activity by cultured parasites. The results confirm the role of tegumental SmATPDase1, but not SmADTPDase2, in the degradation of the exogenous proinflammatory and prothrombotic nucleotides ATP and ADP by live intravascular stages of the parasite.

show abstract

“…SmATPDase 1 is located in the border of the tegument while SmATPDase2 is located in internal structure of the tegument syncytium and can be secreted [81]. The immunogenicity of the synthetic peptide (r175–190) from SmATPDase2 has been demonstrated in Balb-c mice, however the protection induced by this epitope has not been evaluated [82]. …”

Section: Other Membrane Proteins Candidates To Be Used In Vaccine mentioning

confidence: 99%

Schistosoma Tegument Proteins in Vaccine and Diagnosis Development: An Update

Fonseca

Carvalho

Alves

et al. 2012

Journal of Parasitology Research

View full text Add to dashboard Cite

The development of a vaccine against schistosomiasis and also the availability of a more sensitive diagnosis test are important tools to help chemotherapy in controlling disease transmission. Bioinformatics tools, together with the access to parasite genome, published recently, should help generate new knowledge on parasite biology and search for new vaccines or therapeutic targets and antigens to be used in the disease diagnosis. Parasite surface proteins, especially those expressed in schistosomula tegument, represent interesting targets to be used in vaccine formulations and in the diagnosis of early infections, since the tegument represents the interface between host and parasite and its molecules are responsible for essential functions to parasite survival. In this paper we will present the advances in the development of vaccines and diagnosis tests achieved with the use of the information from schistosome genome focused on parasite tegument as a source for antigens.

show abstract

Immunostimulatory property of a synthetic peptide belonging to the soluble ATP diphosphohydro-lase isoform (SmATPDase 2) and immunolocalisation of this protein in the Schistosoma mansoni egg

Cited by 17 publications

References 26 publications

Structural Comparative Analysis of Secreted NTPDase Models of Schistosoma mansoni and Homo sapiens

Structural Comparative Analysis of Secreted NTPDase Models of Schistosoma mansoni and Homo sapiens

Schistosome apyrase SmATPDase1, but not SmATPDase2, hydrolyses exogenous ATP and ADP

Schistosoma Tegument Proteins in Vaccine and Diagnosis Development: An Update

Contact Info

Product

Resources

About