Abstract：
:Here we describe the cloning and characterization of the Schistosoma mansoni Alkaline Phosphatase (SmAP), previously identified in the tegument of adult worms. SmAP encodes a complete sequence composed of 536 amino acids containing an N-terminal signal peptide, five N-glycosylation sites, and a GPI anchor signal, similar to that described for mammalian orthologs. Real-time RT-PCR and Western blot experiments suggest a rapid translation as soon as cercariae are transformed into schistosomula. Immunolocalization analysis shows that the protein is widely distributed in the worm tissues, with increased concentration in the vitelline glands of female parasites. Furthermore, the surface localization of this enzyme was quantitatively supported by its enzymatic activity in live ex vivo or cultured parasites throughout the life cycle stages. The fact that cercariae accumulate large amounts of SmAP mRNA, which rapidly translates into protein upon schistosomula transformation, indicates it may have an important role in host invasion.
journal_name
Exp Parasitoljournal_title
Experimental parasitologyauthors
Araujo-Montoya BO,Rofatto HK,Tararam CA,Farias LP,Oliveira KC,Verjovski-Almeida S,Wilson RA,Leite LCdoi
10.1016/j.exppara.2011.07.008subject
Has Abstractpub_date
2011-11-01 00:00:00pages
284-91issue
3eissn
0014-4894issn
1090-2449pii
S0014-4894(11)00213-Xjournal_volume
129pub_type
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