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1.
Parasitol Res ; 88(3): 280-2, 2002 Mar.
Article in English | MEDLINE | ID: mdl-11954917

ABSTRACT

Cysticercosis caused by the metacestode of the tapeworm Taenia solium causes economic losses in pork meat production, as well as being a human health hazard in some parts of the world. In order to determine if the glucose transporters TGTPI and TGTP2 are recognized by antibodies in the sera from cysticercotic humans and pigs, western blot assays were carried out using membrane fractions of insect cells expressing the two T. solium glucose transporters. Results demonstrated a complete lack of recognition of both TGTPs. These results are unexpected, because at least one transporter is present on the apical surface of the cysticercus tegument.


Subject(s)
Antigens, Helminth/immunology , Helminth Proteins , Monosaccharide Transport Proteins/immunology , Swine/parasitology , Taenia/immunology , Taenia/metabolism , Animals , Glucose Transport Proteins, Facilitative , Humans , Protein Conformation
2.
Parasitology ; 117 ( Pt 6): 579-88, 1998 Dec.
Article in English | MEDLINE | ID: mdl-9881383

ABSTRACT

Tapeworms absorb and consume large quantities of glucose through their syncytial tegument, storing the excess as glycogen. Although some studies on the metabolism of glucose in several tapeworms are available, the proteins that mediate its uptake and distribution in their tissue have not been identified. We describe the isolation and characterization of cDNA clones encoding 2 facilitated diffusion glucose transporters (TGTP1 and TGTP2) from Taenia solium, the causal agent of human and porcine cysticercosis. Radio-isotope labelled hexose uptake mediated by TGTP1 expressed in Xenopus oocytes is inhibited by the natural stereoisomers D-glucose and D-mannose but not by L-glucose. Transport by TGTP1 is sensitive to classical inhibitors of facilitated diffusion such as phloretin and cytochalasin B, and insensitive to ouabain. TGTP2 did not function in Xenopus oocytes. Localization studies using specific anti-TGTP1 and anti-TGTP2 antibodies show that TGTP1 is abundant in a number of structures underlying the tegument in adult parasites and larvae, whereas TGTP2 appears to be localized only on the tegumentary surface of the larvae and is not detected in adults.


Subject(s)
Helminth Proteins/metabolism , Monosaccharide Transport Proteins/metabolism , Taenia/chemistry , Amino Acid Sequence , Animals , Antibodies, Helminth/blood , Antibody Specificity , Baculoviridae/genetics , Cricetinae , DNA, Complementary/genetics , Fluorescent Antibody Technique, Indirect , Genetic Vectors , Glucose/metabolism , Glucose Transport Proteins, Facilitative , Helminth Proteins/chemistry , Mannose/metabolism , Mice , Mice, Inbred BALB C , Molecular Sequence Data , Monosaccharide Transport Proteins/chemistry , Monosaccharide Transport Proteins/genetics , Oocytes/chemistry , Polymerase Chain Reaction , Swine , Taenia/growth & development
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