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Please use this identifier to cite or link to this item: http://repository.li.mahidol.ac.th/dspace/handle/123456789/21488
Title: Molecular cloning and characterization of a glutathione S-transferase encoding gene from Opisthorchis viverrini
Authors: Veerachai Eursittichai
Vithoon Viyanant
Suksiri Vichasri-Grams
Prasert Sobhon
Smarn Tesana
Suchart Edward Upatham
Annemarie Hofmann
Günter Korge
Rudi Grams
Mahidol University
Thammasat University
Khon Kaen University
Burapha University
Freie Universitat Berlin
Keywords: Medicine
Issue Date: 1-Dec-2004
Citation: Asian Pacific Journal of Allergy and Immunology. Vol.22, No.4 (2004), 219-228
Abstract: An adult stage Opisthorchis viverrini cDNA library was constructed and screened for abundant transcripts. One of the isolated cDNAs was found by sequence comparison to encode a glutathione S-transferase (GST) and was further analyzed for RNA expression, encoded protein function, tissue distribution and cross-reactivity of the encoded protein with other trematode protein counterparts. The cDNA has a size of 893 bp and encodes a GST of 213 amino acids length (OV28GST). The most closely-related GST of OV28GST among those published for trematodes is a 28 kDa GST of Clonorchis sinensis as shown by multiple sequence alignment and phylogenetic analysis. Northern analysis of total RNA with a gene-specific probe revealed a 900 nucleotide OV28GST transcriptional product in the adult parasite. Through RNA in situ hybridization OV28GST RNA was detected in the parenchymal cells of adult parasites. This result was confirmed by immunolocalization of OV28GST with an antiserum generated in a mouse against bacterially-produced recombinant OV28GST. Both, purified recombinant and purified native OV28GST were resolved as 28 kDa proteins by SDS-PAGE. Using the anti-recOV28GST antiserum, no or only weak cross-reactivity was observed in an immunoblot of crude worm extracts against the GSTs of Schistosoma mansoni, S. japonicum, S. mekongi, Eurytrema spp. and Fasciola gigantica. The enzyme activity of the purified recombinant OV28GST was verified by a standard 1-chloro-2, 4-dinitrobenzene (CDNB) based activity assay. The present results of our molecular analysis of OV28GST should be helpful in the ongoing development of diagnostic applications for opisthorchiasis viverrini.
URI: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=14844348836&origin=inward
http://repository.li.mahidol.ac.th/dspace/handle/123456789/21488
ISSN: 0125877X
Appears in Collections:Scopus 2001-2005

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