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An antigenic domain of the Leishmania amazonensis nucleoside triphosphate diphosphohydrolase (NTPDase 1) is associated with disease progression in susceptible infected mice

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Abstract

An antigenic conserved B domain was previously identified within nucleoside triphosphate diphosphohydrolases (NTPDases) of plants and parasites. Now, the r-potDomain B, a 6× His-tag polypeptide belonging to the conserved B domain from the potato apyrase, and synthetic peptides LbB1LJ and LbB2LJ derived from the B domain from Leishmania NTPDase 1 were used as molecular tools for studies of the Leishmania amazonensis NTPDase 1. Widespread subcellular location of the specific NTPDase 1 was detected by Western blots of promastigote fractions and ultrastructural immunocytochemical microscopy using immune sera raised against these biomolecules. In addition, the L. amazonensis-infected BALB/c mice were evaluated at 12 to 120 days after infection, which progresses showing typical nodular lesion. High antibody reactivity with either r-potDomain B, LbB1LJ, or LbB2LJ was found in L. amazonensis-infected BALB/c mice indicating the antigenicity of the B domain from NTPDase 1 isoform. The IgG1 antibody reactivity significantly increased at 90–120 days postinfection, 18- to 24-fold when compared to the 12th day, and remained elevated even at 120th after infection, coinciding with the most active stage of the disease. In contrast, significantly higher IgG2a antibody reactivity with each biomolecule was observed at 40th day, about two- to fourfold higher than those found at 12th or 20th day, and decreased along 120-day period. Apparently, the conserved B domain is capable to induce IgG2a production in early disease stages. All together, these results suggest that r-potDomain B or synthetic peptides could be molecular starting points in experimental protocols of immunotherapy and/or vaccination for leishmaniasis.

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Acknowledgments

This work was supported in part by grants from the Fundação de Amparo à Pesquisa do Estado de Minas Gerais (FAPEMIG), Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq), Fundação Oswaldo Cruz (FAPES), and Instituto Oswaldo Cruz. M.A. Juliano, L. Juliano, and S.C. Gonçalves-da-Costa are recipients of senior fellowships from CNPq. M.L. Detoni, A.C.R.G. Maia, G.N. Porcino, and L.R. Quellis were recipients of Master’s and Doctoral fellowships from FAPEMIG, PROQUALIS/UFJF, CAPES/REUNI.

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Authors and Affiliations

  1. Departamento de Bioquímica, Instituto de Ciências Biológicas, Universidade Federal de Juiz de Fora, Rua José Lourenço Kelmer s/n, Campus Universitário, Juiz de Fora, Minas Gerais, Brazil, CEP 36036-900

    M. L. Detoni, M. R. Fessel, A. C. R. G. Maia, G. N. Porcino, L. R. Quellis, P. Faria-Pinto & E. G. Vasconcelos

  2. Departamento de Ciências Biológicas, Instituto de Ciências Biomédicas, Universidade Federal de Alfenas, Alfenas, Minas Gerais, Brazil

    M. J. Marques

  3. Departamento de Biofísica, Escola Paulista de Medicina, Universidade Federal de São Paulo, São Paulo, São Paulo, Brazil

    M. A. Juliano & L. Juliano

  4. Laboratório de Biologia Estrutural, Instituto Oswaldo Cruz, FIOCRUZ, Rio de Janeiro, Rio de Janeiro, Brazil

    V. A. Diniz & S. Côrte-Real

  5. Laboratório de Imunomodulação e Protozoologia, Instituto Oswaldo Cruz/FIOCRUZ, Rio de Janeiro, Rio de Janeiro, Brazil

    S. C. Gonçalves-da-Costa & C. S. F. Souza

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  1. M. L. Detoni
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  2. M. R. Fessel
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  3. A. C. R. G. Maia
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  4. G. N. Porcino
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  5. L. R. Quellis
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  6. P. Faria-Pinto
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  7. M. J. Marques
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  8. M. A. Juliano
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  9. L. Juliano
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  10. V. A. Diniz
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  11. S. Côrte-Real
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  12. S. C. Gonçalves-da-Costa
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  13. C. S. F. Souza
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  14. E. G. Vasconcelos
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Correspondence to E. G. Vasconcelos.

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Detoni, M.L., Fessel, M.R., Maia, A.C.R.G. et al. An antigenic domain of the Leishmania amazonensis nucleoside triphosphate diphosphohydrolase (NTPDase 1) is associated with disease progression in susceptible infected mice. Parasitol Res 112, 2773–2782 (2013). https://doi.org/10.1007/s00436-013-3445-9

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  • DOI: https://doi.org/10.1007/s00436-013-3445-9

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