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Title: Leishmania (Viannia) braziliensis nucleoside triphosphate diphosphohydrolase (NTPDase 1): Localization and in vitro inhibition of promastigotes growth by polyclonal antibodies
Authors: Porcino, Gabriane Nascimento
Carvalho-Campos, Cristiane
Ribeiro Gomes Maia, Ana Carolina
Detoni, Michelle Lima
Faria-Pinto, Priscila
Coimbra, Elaine Soares
Marques, Marcos Jose
Juliano, Maria Aparecida [UNIFESP]
Juliano, Luiz [UNIFESP]
Diniz, Vanessa Alvaro
Corte-Real, Suzana
Vasconcelos, Eveline Gomes
Univ Fed Juiz de Fora
Univ Fed Alfenas
Fiocruz MS
Universidade Federal de São Paulo (UNIFESP)
Keywords: Apyrase
ATP diphosphohydrolase
Issue Date: 1-Oct-2012
Publisher: Elsevier B.V.
Citation: Experimental Parasitology. San Diego: Academic Press Inc Elsevier Science, v. 132, n. 2, p. 293-299, 2012.
Abstract: Nucleoside triphosphate diphosphohydrolase (NTPDase) activity was recently characterized in Leishmania (Viannia) braziliensis promastigotes (Lb), and an antigenic conserved domain (r82-121) from the specific NTPDase 1 isoform was identified. in this work, mouse polyclonal antibodies produced against two synthetic peptides derived from this domain (LbB1LJ, r82-103; LbB2LJ, r102-121) were used. the anti-LbB1LJ or anti-LbB2LJ antibodies were immobilized on protein A-sepharose and immunoprecipitated the NTPDase 1 of 48 kDa and depleted approximately 40% of the phosphohydrolytic activity from detergent-homogenized Lb preparation. Ultrastructural immunocytochemical microscopy identified the NTPDase 1 on the parasite surface and in its subcellular cytoplasmic vesicles, mitochondria, kinetoplast and nucleus. the ATPase and ADPase activities of detergent-homogenized Lb preparation were partially inhibited by anti-LbB1LJ antibody (43-79%), which was more effective than that inhibition (18-47%) by anti-LbB2LJ antibody. in addition, the immune serum anti-LbB1LJ (67%) or anti-LbB2LJ (33%) was cytotoxic, significantly reducing the promastigotes growth in vitro. the results appoint the conserved domain from the L braziliensis NTPDase as an important target for inhibitor design and the potential application of these biomolecules in experimental protocols of disease control. (c) 2012 Elsevier Inc. All rights reserved.
ISSN: 0014-4894
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