Document Detail


Balamuthia mandrillaris: role of galactose in encystment and identification of potential inhibitory targets.
MedLine Citation:
PMID:  19766634     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
Ruqaiyyah Siddiqui; Edward L Jarroll; Naveed Ahmed Khan
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2009-09-18
Journal Detail:
Title:  Experimental parasitology     Volume:  126     ISSN:  1090-2449     ISO Abbreviation:  Exp. Parasitol.     Publication Date:  2010 Sep 
Date Detail:
Created Date:  2010-08-04     Completed Date:  2010-08-31     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0370713     Medline TA:  Exp Parasitol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  22-7     Citation Subset:  IM    
Copyright Information:
Copyright 2009. Published by Elsevier Inc.
Affiliation:
School of Biological and Chemical Sciences, Birkbeck College, University of London, London, England, UK.
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MeSH Terms
Descriptor/Qualifier:
1-Phosphatidylinositol 3-Kinase / 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:
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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