Please use this identifier to cite or link to this item: https://ir.sc.mahidol.ac.th/handle/123456789/749
Title: Fasciola gigantica: molecular analysis of a water channel protein (Aquaporin)
Authors: Suksiri Vichasri Grams
Keywords: Fasciola gigantica;aquaporin;water;in vitro mutagenesis
Issue Date: 2010
Publisher: The Thai Pharmacological and Therapeutic Society of Thailand.
Citation: Thai J Pharmacol. 2010;32(1):263-265.
Abstract: Fasciolosis caused by Fasciola gigantica is an important disease of cattle in Thailand. In order to develop new drugs and vaccines we have recently started to conduct research on aquaporins in Fasciola. Aquaporins (AQPs) are essential for the maintenance of water homeostasis in all organisms including animals, plants, and bacteria. Structure, function, and pathology of AQPs have been extensively studied in vertebrates but data for AQPs of trematodes is still limited. In the present study, a cDNA encoding an aquaporin (FgAQP-1) was molecular cloned from a metacercarial stage cDNA library of F. gigantica. The FgAQP- 1 cDNA contained the complete coding sequence for a protein of 299 amino acid residues. Comparison of the deduced amino acid sequence with protein sequences in public databases using NCBI-BLASTP showed highest similarity to aquaporin-1 of Bos taurus. Expression and distribution of FgAQP-1 has been characterized at the nucleic acid and protein level in the adult parasite. Functional data of FgAQP-1 will be obtained after transformation of yeast with a plasmid carrying FgAQP-1 DNA by stopped flow analysis. Furthermore, it is planned to introduce mutations into the original FgAQP-1 sequence to analyze the importance of single amino acid residues for the functional integrity of the protein.
URI: https://ir.sc.mahidol.ac.th/handle/123456789/749
ISSN: 0125-3832
Appears in Collections:Biology: National Journal Publications

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