Please use this identifier to cite or link to this item: https://repositorio.unifesp.br/handle/11600/29455
Title: Characterization of Schistosoma mansoni ATPDase2 gene, a novel apyrase family member
Authors: Levano-Garcia, Julio
Mortara, Renato A.
Verjovski-Almeida, Sergio
DeMarco, Ricardo
Universidade de São Paulo (USP)
Universidade Federal de São Paulo (UNIFESP)
Keywords: Schistosoma mansoni
ATP-diphosphohydrolase isoforms
apyrase
cloning
tegument
Issue Date: 12-Jan-2007
Publisher: Elsevier B.V.
Citation: Biochemical and Biophysical Research Communications. San Diego: Academic Press Inc Elsevier Science, v. 352, n. 2, p. 384-389, 2007.
Abstract: Schistosoma mansoni is a major causative agent of schistosomiasis, which constitutes a severe health problem in developing countries. We have previously described the SmATPDase1 gene, encoding a protein from the external surface of the parasites. in this work, we describe the cloning and characterization of SmATPDase2, a novel C1339-like ATP diphosphohydrolase gene in S. mansoni. in silico analysis of the protein encoded by SmATPDase2 predicts a single N-terminal transmembrane domain similar to that described for secreted human apyrase isoforms. Immuno-colocalization experiments detected both SmATPDase proteins at the S. mansoni adult worm tegument basal and apical membranes, but only SmATPDase2 in the tegument syncytium. SmATPDase2 but not SmATPDase1 protein was detected by Western blot in culture medium supernatants following incubation of adult worms in vitro, indicating that SmATPDase2 was secreted by the parasite to the medium. Taken together these data suggest a non-redundant role for SmATPDase2 in the parasite-host interplay. (c) 2006 Elsevier Inc. All rights reserved.
URI: http://repositorio.unifesp.br/handle/11600/29455
ISSN: 0006-291X
Other Identifiers: http://dx.doi.org/10.1016/j.bbrc.2006.11.023
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