title: Metabolite movement across the schistosome surface.
abstract: Intravascular schistosome parasites are covered by an unusual double lipid bilayer. Nutrients, such as glucose and amino acids, as well as other metabolites, are known to be transported across this surface via specific transporter proteins. For instance, the glucose transporter protein SGTP4 is found in the host-interactive tegumental membranes. A second glucose transporter, SGTP1, localizes to the tegumental basal membrane (and internal tissues). Following expression in Xenopus oocytes, SGTP1 and SGTP4 both function as facilitated-diffusion sugar transporters. Suppressing the expression of SGTP1 and SGTP4 in juvenile schistosomes using RNA interference (RNAi) impairs the parasite's ability to import glucose and severely decreases worm viability. Amino acids can also be imported into schistosomes across their surface and an amino acid transporter (SPRM1lc) has been localized in the parasite surface membranes (as well as internally). In Xenopus oocytes, SPRM1lc can import the basic amino acids arginine, lysine and histidine as well as leucine, phenylalanine, methionine and glutamine. To function, this protein requires the assistance of a heavy-chain partner (SPRM1hc) which acts as a chaperone. Water is transported across the tegument of schistosomes via the aquaporin protein SmAQP. Suppressing SmAQP gene expression makes the parasites less able to osmoregulate and decreases their viability. In addition, SmAQP-suppressed adult parasites have been shown to be impaired in their ability to excrete lactate. Analysis of tegumental transporter proteins, as described in this report, is designed to generate a comprehensive understanding of the role of such proteins in promoting parasite survival by controlling the movement of metabolites into and out of the worms.
authors.affiliation: Molecular Helminthology Laboratory, Department of Biomedical Sciences, Division of Infectious Diseases, Cummings School of Veterinary Medicine, Tufts University, North Grafton, Massachusetts, USA.
authors.forename: A
authors.initials: A
authors.lastname: Da'dara
authors.forename: G
authors.initials: G
authors.lastname: Krautz-Peterson
authors.forename: Z
authors.initials: Z
authors.lastname: Faghiri
authors.forename: P J
authors.initials: PJ
authors.lastname: Skelly
mesh_terms: D000596:Amino Acids / Q000378:metabolism*; D000818:Animals; D003001:Cloning, Molecular; D020868:Gene Silencing; D005947:Glucose / Q000378:metabolism*; D026901:Membrane Transport Proteins / Q000235:genetics / Q000378:metabolism*; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D012547:Schistosoma / Q000378:metabolism*; D013534:Survival; D014867:Water / Q000378:metabolism*; D014981:Xenopus
chemical_list: D000596:Amino Acids; D026901:Membrane Transport Proteins; D011994:Recombinant Proteins; D014867:Water; D005947:Glucose