Antibody reactivity against potato apyrase, a protein that shares epitopes with Schistosoma mansoni ATP diphosphohydrolase isoforms, in acute and chronically infected mice, after chemotherapy and reinfection

Pinto, Priscila de Faria; Montesano, M. Angela; Jacinto, Alexandre Arthur; Santos, Ronaldo Soares; Bordin, Fábio Humberto S; Ferreira, Ana Paula; Penido, Marcus L. O.; Coelho, Paulo Marcos Zech; Vasconcelos, Eveline Gomes

doi:10.1590/s0074-02762010000400005

Cited by 9 publications

(5 citation statements)

References 15 publications

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“…Potato apyrase, synthetic peptide, SEA and soluble worm antigen preparation (SWAP) -Potato apyrase was purified from a commercial strain of Solanum tuberosum and used to obtain polyclonal antiserum in a New Zealand White rabbit or BALB/c mice, as earlier described (FariaPinto et al 2004, 2010b, Kettlun et al 2005. A peptide (SmB2LJ; r175-194; AALSLTKLINIAETSLPVDV) belonging to a conserved domain from soluble S. mansoni SmATPDase 2 (GenBank accession ABI79456.1) was designed based on a strategic comparative study with its potato apyrase counterpart (r97-116; AANSLEPLLDGAE-GVVPQEL; 40% identity and 65% similarity over 20 amino acids) (GenBank accession P80595), which maintained the predicted epitopes available for antibody binding (Faria-Pinto et al 2008).…”

Section: Methodsmentioning

confidence: 99%

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

Gusmão

Maia

et al. 2011

Mem. Inst. Oswaldo Cruz

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A peptide (SmB2LJ; r175-194) that belongs to a conserved domain from Schistosoma mansoni SmATPDase 2 and is shared with potato apyrase, as predicted by in silico analysis as antigenic, was synthesised and its immunostimulatory property was analysed. When inoculated in BALB/c mice, this peptide induced high levels of SmB2LJ-specific IgG1 and IgG2a subtypes, as detected by enzyme linked immunosorbent assay. In addition, dot blots were found to be positive for immune sera against potato apyrase and SmB2LJ. These results suggest that the conserved domain r175-194 from the S. mansoni SmATPDase 2 is antigenic. Western blots were performed and the anti-SmB2LJ antibody recognised in adult worm (soluble worm antigen preparation) or soluble egg antigen antigenic preparations two bands of approximately 63 and 55 kDa, molecular masses similar to those predicted for adult worm SmATPDase 2. This finding strongly suggests the expression of this same isoform in S. mansoni eggs. To assess localisation of SmATPDase 2, confocal fluorescence microscopy was performed using cryostat sections of infected mouse liver and polyclonal antiserum against SmB2LJ. Positive reactions were identified on the external surface from the miracidium in von Lichtenberg's envelope and, in the outer side of the egg-shell, showing that this soluble isoform is secreted from the S. mansoni eggs

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Section: Methodsmentioning

confidence: 99%

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

Gusmão

Maia

et al. 2011

Mem. Inst. Oswaldo Cruz

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“…Sm ATPDase 1 is located on the surface and Sm ATPDase 2 is in the tegument and secreted by eggs and adult worms ( Faria-Pinto et al., 2004 ; Fietto et al., 2004 ; Levano-Garcia et al., 2007 ). Both isoforms showed immune cross-reactivity with antipotato apyrase antibodies ( Faria-Pinto et al., 2008 ; Faria-Pinto et al., 2010 ). Macrophages incubated with antibodies against the ATPDase isoforms of S. mansoni showed reduced NTPDase 1 activity, and the parasite proliferation was inhibited ( Marconato et al., 2017 ).…”

Section: Development Of E-ntpdases Inhibitorsmentioning

confidence: 99%

E-NTPDases: Possible Roles on Host-Parasite Interactions and Therapeutic Opportunities

Paes-Vieira

Gomes-Vieira

Meyer‐Fernandes

2021

Front. Cell. Infect. Microbiol.

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Belonging to the GDA1/CD39 protein superfamily, nucleoside triphosphate diphosphohydrolases (NTPDases) catalyze the hydrolysis of ATP and ADP to the monophosphate form (AMP) and inorganic phosphate (Pi). Several NTPDase isoforms have been described in different cells, from pathogenic organisms to animals and plants. Biochemical characterization of nucleotidases/NTPDases has revealed the existence of isoforms with different specificities regarding divalent cations (such as calcium and magnesium) and substrates. In mammals, NTPDases have been implicated in the regulation of thrombosis and inflammation. In parasites, such as Trichomonas vaginalis, Trypanosoma spp., Leishmania spp., Schistosoma spp. and Toxoplasma gondii, NTPDases were found on the surface of the cell, and important processes like growth, infectivity, and virulence seem to depend on their activity. For instance, experimental evidence has indicated that parasite NTPDases can regulate the levels of ATP and Adenosine (Ado) of the host cell, leading to the modulation of the host immune response. In this work, we provide a comprehensive review showing the involvement of the nucleotidases/NTPDases in parasites infectivity and virulence, and how inhibition of NTPDases contributes to parasite clearance and the development of new antiparasitic drugs.

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“…4,9,10 Previously, our group showed that SmATPDases 1 and 2 isoforms are antigenic and have cross-reactivity with antipotato apyrase antibodies. 4,[11][12][13] Furthermore, the alignment of the primary sequence of NTPDase of many organisms shows shared domains, 14 encouraging studies comparing the isoforms present in the parasite with the protein expressed in the mammalian host.…”

Section: Introductionmentioning

confidence: 99%

Antischistosome antibodies change NTPDase 1 activity from macrophages

Marconato

Gusmão

Melo

et al. 2017

Parasite Immunology

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NTPDases are enzymes that hydrolyse diphosphate and triphosphate nucleosides, regulating purinergic signalling in many organisms. The Schistosoma mansoni NTPDases, SmATPDases 1 and 2, are antigenic proteins and display a significant homology with the isoforms found in mammalian cells. In this work, we investigated whether anti-SmATPDase antibodies from S. mansoni-infected mice sera show cross-reactivity with the NTPDase 1 isoform from macrophages and how this event affects the cell proliferation. By Western blot, anti-SmATPDase antibodies present in serum from infected mice recognized 2 bands with approximately 53 and 58 kDa, corresponding to NTPDase 1. Additionally, the enzyme was identified in macrophages by immunofluorescence and the anti-SmATPDase antibodies were able to reduce activity enzyme (22%). Macrophages incubated with commercial polyclonal antibodies reactive with NTPDase 1 (anti-CD39) showed a reduction of 40% of the enzyme activity. In proliferation assays, macrophage proliferation was inhibited 11% and 90% by pooled sera from infected animals and anti-CD39, respectively. The results suggest that inhibition of NTPDase 1 in macrophages by antibodies produced against the isoforms of the S. mansoni ATPDases could be a mechanism of regulation in the immune response during experimental schistosomiasis.

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Antibody reactivity against potato apyrase, a protein that shares epitopes with Schistosoma mansoni ATP diphosphohydrolase isoforms, in acute and chronically infected mice, after chemotherapy and reinfection

Abstract: Apyrase and experimental schistosomiasis • P Faria-Pinto et al.

Cited by 9 publications

References 15 publications

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

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

E-NTPDases: Possible Roles on Host-Parasite Interactions and Therapeutic Opportunities

Antischistosome antibodies change NTPDase 1 activity from macrophages

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