Leishmania infantum nucleoside triphosphate diphosphohydrolase 1 (NTPDase 1) B-domain: Antibody antiproliferative effect on the promastigotes and IgG subclass responses in canine visceral leishmaniasis

Author(s):Show less -

Ribeiro Gomes Maia, Ana Carolina ^[1] ; Porcino, Gabriane Nascimento ^[1] ; Faria-Pinto, Priscila ^[1] ; Mendes, Tulio Vieira ^[2] ; Ribeiro Antinarelli, Luciana Maria ^[3] ; Coimbra, Elaine Soares ^[3] ; Reis, Alexandre Barbosa ^{[4, 5]} ; Juliano, Luiz ^[6] ; Juliano, Maria Aparecida ^[6] ; Marques, Marcos Jose ^[7] ; Vasconcelos, Eveline Gomes ^[1]

Affiliation

^[1] Univ Fed Juiz de Fora, Inst Ciencias Biol, Lab Estrutura & Funcao Prot, Dept Bioquim, Rua Jose Lourenco Kelmer S-N, Campus Univ, BR-36036900 Juiz De Fora, MG - Brazil

^[2] Marinha Brasil, Hosp Naval Marcilio Dias, Doencas Infecciosas & Parasitarias, Rio De Janeiro, RJ - Brazil

^[3] Univ Fed Juiz De Fora, Inst Ciencias Biol, Dept Parasitol Microbiol & Imunol, Juiz De Fora, MG - Brazil

^[4] Univ Fed Ouro Preto, Escola Farm, Dept Anal Clin, Ouro Preto, MG - Brazil

^[5] Univ Fed Ouro Preto, Lab Imunopatol, Nucleo Pesquisas Ciencias Biol, Escola Farm, Ouro Preto, MG - Brazil

^[6] Univ Fed Sao Paulo, Escola Paulista Med, Dept Biofis, Sao Paulo, SP - Brazil

^[7] Univ Fed Alfenas, Inst Ciencias Biomed, Dept Ciencias Biol, Alfenas, MG - Brazil

• Document type: Journal article
• Source: Veterinary Parasitology; v. 271, p. 38-44, JUL 2019.
• Web of Science Citations: 0

Abstract

A nucleoside triphosphate diphosphohydrolase-1 (NTPDase 1) was identified on the surface, flagellum and kinetoplast from L. infantum promastigotes by immunocytochemistry and confocal laser scanning microscopy, using immune sera that recognized specifically the B domain of NTPDase 1 and produced against synthetic peptides (LbB1LJ and LbB2LJ) derived from this domain. The polyclonal antibodies had effective antileishmanial effect, reducing significantly in vitro promastigotes growth (21-25%), an antiproliferative effect also demonstrated by immune sera produced against recombinant r-pot B domain, and two other synthetic peptides (potB1LJ and potB2LJ). In addition, using these biomolecules in ELISA technique, IgG1 and IgG2 subclasses reactivities of either healthy dogs or infected by L. infantum and classified clinically as asymptomatic, oligo-symptomatic and symptomatic were tested. Analysis of distinct IgG1 and IgG2 seropositivities patterns suggested antibody subclasses binding epitopes along B domain for protection against infection, indicating this domain as a new tool for prophylactic and immunotherapeutic investigations. (AU)

• FAPESP's process: 12/50191-4 - Synthesis, kinetic studies and applications of substrates and inhibitors for proteolytic enzymes
• Grantee: Maria Aparecida Juliano
• Support Opportunities: Research Projects - Thematic Grants