Publication: Bi-functionality of Opisthorchis viverrini aquaporins
Issued Date
2015-01-01
Resource Type
ISSN
61831638
03009084
03009084
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2-s2.0-84919340294
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Mahidol University
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SCOPUS
Bibliographic Citation
Biochimie. Vol.108, (2015), 149-159
Suggested Citation
Amornrat Geadkaew, Julia Von Bülow, Eric Beitz, Smarn Tesana, Suksiri Vichasri Grams, Rudi Grams Bi-functionality of Opisthorchis viverrini aquaporins. Biochimie. Vol.108, (2015), 149-159. doi:10.1016/j.biochi.2014.11.013 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/35580
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Title
Bi-functionality of Opisthorchis viverrini aquaporins
Abstract
© 2014 Elsevier B.V. and Société française de biochimie et biologie Moléculaire (SFBBM). Aquaporins (AQP) are essential mediators of water regulation in all living organisms and members of the major intrinsic protein (MIP) superfamily of integral membrane proteins. They are potential vehicles or targets for chemotherapy, e.g. in Trypanosoma brucei melarsoprol and pentamidine uptake is facilitated by TbAQP-2. Transcriptome data suggests that there are at least three active aquaporins in the human liver fluke, Opisthorchis viverrini, OvAQP-1, 2 and 3, and crude RNA silencing of OvAQP-1 and 2 has recently been shown to affect parasite swelling in destilled water. In the present work we demonstrate that OvAQP-3 is a major water-conducting channel of the parasite, that it can be detected from the newly excysted juvenile to the adult stage and that it is present in major tissues of the parasite. Furthermore, a comparative functional characterization of the three parasite AQPs was performed by using Xenopus oocyte swelling and yeast phenotypic assays. OvAQP-1, OvAQP-2, and OvAQP-3 were found to conduct water and glycerol while only the latter two were also able to conduct urea. In addition, all OvAQPs were found to transport ammonia and methylamine. Our findings demonstrate that the sequence-based classification into orthodox aquaporins and glycerol-conducting aquaglyceroporins is not functionally conserved in the parasite and implicate a broder range of functions for these channels.