| Balamuthia mandrillaris: role of galactose in encystment and identification of potential inhibitory targets. | |
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MedLine Citation:
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PMID: 19766634 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Balamuthia mandrillaris is a causative agent of granulomatous encephalitis that almost always proves fatal. A major concern during the course of therapy is that B. mandrillaris can transform into cysts. Cysts are highly resistant to physical and chemical conditions and present a problem in successful antimicrobial chemotherapy. However, the underlying mechanisms of B. mandrillaris transformation into cysts are not known. In this study, we examined the effects of exogenous sugars on B. mandrillaris encystment. The findings revealed that free exogenous galactose, but not other sugars, enhanced parasite differentiation into cysts, and apparently a galactose-binding protein is involved in B. mandrillaris encystment. Cytoskeletal re-arrangements and phosphatidylinositol 3-kinase (PI3K)-mediated pathways are involved in B. mandrillaris encystment based on inhibitor studies. Dual functionality of galactose-binding protein in B. mandrillaris pathogenesis and encystment is discussed further. |
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Authors:
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Ruqaiyyah Siddiqui; Edward L Jarroll; Naveed Ahmed Khan |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2009-09-18 |
Journal Detail:
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Title: Experimental parasitology Volume: 126 ISSN: 1090-2449 ISO Abbreviation: Exp. Parasitol. Publication Date: 2010 Sep |
Date Detail:
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Created Date: 2010-08-04 Completed Date: 2010-08-31 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0370713 Medline TA: Exp Parasitol Country: United States |
Other Details:
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Languages: eng Pagination: 22-7 Citation Subset: IM |
Copyright Information:
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Copyright 2009. Published by Elsevier Inc. |
Affiliation:
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School of Biological and Chemical Sciences, Birkbeck College, University of London, London, England, UK. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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1-Phosphatidylinositol 3-Kinase
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antagonists & inhibitors,
metabolism Amides / pharmacology Amoebozoa / drug effects, physiology* Brain / blood supply, cytology Calcium-Binding Proteins / physiology* Cells, Cultured Chromones / pharmacology Cytochalasin D / pharmacology Cytoskeleton / drug effects, physiology Endothelial Cells / parasitology Enzyme Inhibitors / pharmacology* Galactose / metabolism, pharmacology* Genistein / pharmacology Humans Monosaccharide Transport Proteins / physiology* Morpholines / pharmacology Periplasmic Binding Proteins / physiology* Protein Kinase Inhibitors / pharmacology Protein Tyrosine Phosphatases / antagonists & inhibitors Protein-Tyrosine Kinases / antagonists & inhibitors, metabolism Pyridines / pharmacology Signal Transduction / drug effects, physiology Vanadates / pharmacology rho-Associated Kinases / antagonists & inhibitors |
| Chemical | |
Reg. No./Substance:
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0/Amides; 0/Calcium-Binding Proteins; 0/Chromones; 0/Enzyme Inhibitors; 0/Monosaccharide Transport Proteins; 0/Morpholines; 0/Periplasmic Binding Proteins; 0/Protein Kinase Inhibitors; 0/Pyridines; 0/Vanadates; 0/galactose-binding protein; 138381-45-0/Y 27632; 154447-36-6/2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one; 22144-77-0/Cytochalasin D; 26566-61-0/Galactose; 446-72-0/Genistein; EC 2.7.1.137/1-Phosphatidylinositol 3-Kinase; EC 2.7.10.1/Protein-Tyrosine Kinases; EC 2.7.11.1/rho-Associated Kinases; EC 3.1.3.48/Protein Tyrosine Phosphatases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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