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Title: The saposin-like proteins 1, 2, and 3 of Fasciola gigantica
Authors: Rudi Grams
Poom Adisakwattana
Nonglucksanawan Ritthisunthorn
Veerachai Eursitthichai
Suksiri Vichasri-Grams
Vithoon Viyanant
Thammasat University
Mahidol University
Keywords: Biochemistry, Genetics and Molecular Biology;Immunology and Microbiology
Issue Date: 1-Aug-2006
Citation: Molecular and Biochemical Parasitology. Vol.148, No.2 (2006), 133-143
Abstract: The SAP genes of Fasciola encode proteins belonging to the saposin-like protein family. The saposin signature, a compact domain of mainly α-helical character, contains six conserved cysteine residues and has been implicated in membrane-binding, pore formation, and subsequent cell lysis in several family members. Recombinant SAP-2 of F. hepatica has been shown to induce lysis of human erythrocytes and peripheral blood mononuclear cells. This suggests that the SAPs are involved in the nutrition of Fasciola as the released content of lysed host cells is available for further enzymatic processing and uptake by the parasite. In the present study a new SAP-3 cDNA was obtained in an immunoscreen of an adult stage F. gigantica cDNA library with an antiserum against the parasite's excretion/secretion antigens. SAP-1 and SAP-2 cDNAs were isolated from F. gigantica cDNA libraries using oligonucleotide primers specific to the SAP-1 and SAP-2 DNA sequences from F. hepatica. Transcripts of the three SAPs are present from the metacercarial to the adult stage and are located to the gut epithelium. In immatures SAP-1 RNA is the predominant product whereas in adults SAP-2 and -3 are the more abundant products. Polyclonal anti-SAP-1 and SAP-2 antisera confirmed the tissue-specificity and revealed the subcellular localization of SAPs in large granules concentrated in the apical part of the gut epithelial cells of the parasite. Interestingly, evolutionary conservation of the Fasciola SAP sequences among other trematodes is low at 20-30% sequence identity comparable to the Entamoeba amoebapore sequences. © 2006 Elsevier B.V. All rights reserved.
ISSN: 01666851
Appears in Collections:Scopus 2006-2010

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