Two isoforms of a divalent metal transporter (DMT1) in Schistosoma mansoni suggest a surface-associated pathway for iron absorption in schistosomes

Smyth, Danielle J., Glanfield, Amber, McManus, Donald P., Hacker, Elke, Blair, David, Anderson, Greg J. and Jones, Malcolm K. (2006) Two isoforms of a divalent metal transporter (DMT1) in Schistosoma mansoni suggest a surface-associated pathway for iron absorption in schistosomes. Journal of Biological Chemistry, 281 4: 2242-2248. doi:10.1074/jbc.M511148200

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Author Smyth, Danielle J.
Glanfield, Amber
McManus, Donald P.
Hacker, Elke
Blair, David
Anderson, Greg J.
Jones, Malcolm K.
Title Two isoforms of a divalent metal transporter (DMT1) in Schistosoma mansoni suggest a surface-associated pathway for iron absorption in schistosomes
Journal name Journal of Biological Chemistry   Check publisher's open access policy
ISSN 0021-9258
Publication date 2006-01-27
Year available 2005
Sub-type Article (original research)
DOI 10.1074/jbc.M511148200
Open Access Status File (Publisher version)
Volume 281
Issue 4
Start page 2242
End page 2248
Total pages 7
Place of publication Bethesda, M.D., U.S.A.
Publisher American Society for Biochemistry and Molecular Biology
Collection year 2006
Language eng
Subject C1
110803 Medical Parasitology
110309 Infectious Diseases
Formatted abstract
 We describe two homologues of the mammalian divalent metal transporter (DMT1) for Schistosoma mansoni, a pathogenic intravascular parasite of humans. Schistosomes have a high nutritional and metabolic demand for iron. Nucleotide sequences of the parasite homologues, designated SmDMT1A and -B, are identical in all but the 5′-regions. The predicted amino acid sequences share at least 60% identity with DMT1 (=Nramp2) of humans, mice, and rats, and at least 55% identity with Nramp1 from mice, humans and Caenorhabditis elegans. SmDMT1A is expressed in differentiating eggs, miracidia, cercariae, schistosomula, and adults, whereas SmDMT1B is expressed in all but the miracidium and occurs at lower levels than SmDMT1A in differentiating eggs and cercariae. An iron-responsive element, present at the 3′-untranslated region of many DMT1 molecules, is not present in schistosome mRNAs studied here. A Western blot analysis of adult worm preparations using a homologous rabbit serum raised against a schistosome DMT1 peptide and a heterologous serum raised against mammalian DMT1, revealed a band approximating 115 kDa. By immunofluorescence microscopy, the schistosome DMT1s localize primarily to the tegument. Iron uptake assays demonstrated that SmDMT1s were able to rescue yeast growth in ferrous iron-transport deficient yeast (fet3fet4). The results suggest that schistosomes express molecules for ferrous iron transport in their tegument, suggesting trans-tegumental transport as one means of iron acquisition for these parasites.
Keyword Biochemistry & Molecular Biology
Transferrin Receptor
Sequence Alignment
Adult Worms
Expression
Localization
Japonicum
Nramp2
Ferritin
Protein
Evolutionary
Q-Index Code C1
Additional Notes First Published on November 2, 2005

 
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Created: Wed, 15 Aug 2007, 09:26:34 EST