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BIBTEX RIS

Occurrence of a conserved domain in ATP diphosphohydrolases from pathogenic organisms associated to antigenicity in human parasitic diseases

2011; Elsevier BV; Volume: 35; Issue: 10 Linguagem: Inglês

10.1016/j.dci.2011.03.026

1879-0089

Ana Carolina Ribeiro Gomes Maia, Michelle Lima Detoni, Gabriane Nascimento Porcino, Thais Vieira Soares, Michélia Antônia do Nascimento Gusmão, Melissa Regina Fessel, Marcos José Marques, Maria Aparecida de Souza, Paulo Marcos Zech Coelho, Juliana de Assis Silva Gomes, Manoel Otávio da Costa Rocha, Marcelo de Oliveira Santos, Priscila de Faria Pinto, Eveline Gomes Vasconcelos,

Complement system in diseases

A polypeptide (r78–117) belonging to the potato apyrase was identified as a conserved domain shared with apyrase-like proteins from distinct pathogenic organisms, and was obtained as a 6xHis tag polypeptide (r-Domain B). By ELISA, high IgG, and IgG1 and IgG2a subtypes levels were detected in BALB/c mice pre-inoculated with r-Domain B. In Schistosoma mansoni adult worm or Leishmania (V.) braziliensis promastigote preparation, anti-r-Domain B antibodies inhibit 22–72% of the phosphohydrolytic activities and when immobilized on Protein A-Sepharose immunoprecipitate 42–91% of them. Western blots of the immunoprecipitated resin–antibody–antigen complexes identified bands of mw similar to those predicted for parasite proteins. Total IgG and subclasses of patients with leishmaniasis or schistosomiasis exhibited cross-immunoreactivity with r-Domain B. Therefore, the domain B within both S. mansoni SmATPDase 2 (r156–195) and L. (V.) braziliensis NDPase (r83–122) are potentially involved in the host immune response, and also seem to be conserved during host and parasites co-evolution.