the tegument of the human parasitic worm schistosoma mansoni as an excretory organ the surface aquaporin smaqp is a lactate transporter人类寄生虫的外皮曼氏裂体吸虫作为一个排泄器官表面水通道蛋白smaqp乳酸转运体.pdfVIP
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the tegument of the human parasitic worm schistosoma mansoni as an excretory organ the surface aquaporin smaqp is a lactate transporter人类寄生虫的外皮曼氏裂体吸虫作为一个排泄器官表面水通道蛋白smaqp乳酸转运体
The Tegument of the Human Parasitic Worm
Schistosoma mansoni as an Excretory Organ: The Surface
Aquaporin SmAQP Is a Lactate Transporter
1. 2. 2 2 1
Zahra Faghiri , Simone M. R. Camargo , Katja Huggel , Ian C. Forster , David Ndegwa , Franc¸ois
2 1
Verrey , Patrick J. Skelly *
1 Molecular Helminthology Laboratory, Division of Infectious Diseases, Department of Biomedical Sciences, Cummings School of Veterinary Medicine, Tufts University,
Grafton, Massachusetts, United States of America, 2 Institute of Physiology, University of Zurich, Zurich, Switzerland
Abstract
Adult schistosomes are intravascular parasites that metabolize imported glucose largely via glycolysis. How the parasites get
rid of the large amounts of lactic acid this generates is unknown at the molecular level. Here, we report that worms whose
aquaporin gene (SmAQP) has been suppressed using RNAi fail to rapidly acidify their culture medium and excrete less
lactate compared to controls. Functional expression of SmAQP in Xenopus oocytes demonstrates that this protein can
transport lactate following Michaelis-Menten kinetics with low apparent affinity (Km = 41 65. 8 mM) and with a low energy
of activation (Ea = 7.1860.7 kcal/mol). Phloretin, a known inhibitor of lactate release from schistosomes, also inhibits lactate
movement in SmAQP-expressing oocytes. In keeping with the substrate promiscuity of other aquaporins, SmAQP is shown
here to be also capable of transporting water, mannitol, fructose and alanine but not glucose. Using immunofluorescent
and immuno-EM, we confirm that SmAQP is localized in the tegument of adult worms. These findings extend the proposed
functions of the schistosome tegument
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