Babesia bovis contains an abundant parasite-specific protein-free glycerophosphatidylinositol and the genes predicted for its assembly
Autonomous glycosylphosphatidylinositol (GPI) molecules (also protein-free GPIs or free GPIs) have been reported to be particularly abundant in some parasitic protozoa and mediate strong immunomodulatory effects on the host immune system. In the work at hand we have investigated the existence of fre...
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todo:paper_03044017_v167_n2-4_p227_Rodriguez2023-10-03T15:20:33Z Babesia bovis contains an abundant parasite-specific protein-free glycerophosphatidylinositol and the genes predicted for its assembly Rodríguez, A.E. Couto, A. Echaide, I. Schnittger, L. Florin-Christensen, M. Babesia bovis Glycolipids Glycosylphosphatidylinositol GPI acyltransferase dolichol phosphate mannosyltransferase 1 glycosylphosphatidylinositol glycosylphosphatidylinositol mannosyltransferase 1 glycosylphosphatidylinositol mannosyltransferase 2 glycosyltransferase mannosamine mannosyltransferase transferase transferase GPI 1 transferase PIG L transferase PIG W unclassified drug animal cell article Babesia bovis babesiosis controlled study cow growth inhibition in vitro study lipid analysis lipid composition nonhuman phospholipid synthesis protein assembly thin layer chromatography Animals Babesia bovis Gene Expression Regulation Hexosamines Phosphatidylinositols Babesia bovis Bovinae Eukaryota Protozoa Suidae Autonomous glycosylphosphatidylinositol (GPI) molecules (also protein-free GPIs or free GPIs) have been reported to be particularly abundant in some parasitic protozoa and mediate strong immunomodulatory effects on the host immune system. In the work at hand we have investigated the existence of free GPIs in Babesia bovis. Comparative thin layer chromatographic analysis of the protein-free glycolipid fraction of in vitro cultured B. bovis merozoites and erythrocyte membranes demonstrated the presence of an abundant parasite-specific band. Its chemical analysis revealed a GPI species containing a chain of two mannose residues, N-glucosamine and non-acylated inositol. The lipid moiety linked to inositol was diacylglycerol. The total fatty acid composition showed predominantly long-carbon chain molecules (12% of C22:0 and 45% of C24:0). The potential of B. bovis to assemble the presented free GPI species was verified by the existence of seven genes in its genome that putatively encode the following GPI biosynthetic enzymes: PI N-acetyl-GlcN-transferase (PIG-A and GPI-1), N-acetyl-GlcN-PI-de-N-acetylase (PIG-L), acyltransferase (PIG-W), dolichyl-phosphate mannosyl transferase (DPM-1), GPI mannosyltransferase I (PIG-M), and GPI mannosyltransferase II (PIG-V). GPI biosynthesis is vital for the intraerythrocytic parasite stage as mannosamine, an inhibitor of GPI biosynthesis, impaired in vitro growth of B. bovis merozoites. Absence of the vast majority of N-glycan metabolism encoding genes in the B. bovis genome underscores that the growth inhibitory effect of mannosamine is attributable to its interference with GPI biosynthesis and not with assembly of N-linked oligosaccharides, as has been described for higher eukaryotes. Elucidation of the structure and biosynthesis of GPI may allow to facilitate the development of future immune interventions against bovine babesiosis. © 2009 Elsevier B.V. All rights reserved. Fil:Couto, A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Florin-Christensen, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_03044017_v167_n2-4_p227_Rodriguez |
| institution |
Universidad de Buenos Aires |
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I-28 |
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R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Babesia bovis Glycolipids Glycosylphosphatidylinositol GPI acyltransferase dolichol phosphate mannosyltransferase 1 glycosylphosphatidylinositol glycosylphosphatidylinositol mannosyltransferase 1 glycosylphosphatidylinositol mannosyltransferase 2 glycosyltransferase mannosamine mannosyltransferase transferase transferase GPI 1 transferase PIG L transferase PIG W unclassified drug animal cell article Babesia bovis babesiosis controlled study cow growth inhibition in vitro study lipid analysis lipid composition nonhuman phospholipid synthesis protein assembly thin layer chromatography Animals Babesia bovis Gene Expression Regulation Hexosamines Phosphatidylinositols Babesia bovis Bovinae Eukaryota Protozoa Suidae |
| spellingShingle |
Babesia bovis Glycolipids Glycosylphosphatidylinositol GPI acyltransferase dolichol phosphate mannosyltransferase 1 glycosylphosphatidylinositol glycosylphosphatidylinositol mannosyltransferase 1 glycosylphosphatidylinositol mannosyltransferase 2 glycosyltransferase mannosamine mannosyltransferase transferase transferase GPI 1 transferase PIG L transferase PIG W unclassified drug animal cell article Babesia bovis babesiosis controlled study cow growth inhibition in vitro study lipid analysis lipid composition nonhuman phospholipid synthesis protein assembly thin layer chromatography Animals Babesia bovis Gene Expression Regulation Hexosamines Phosphatidylinositols Babesia bovis Bovinae Eukaryota Protozoa Suidae Rodríguez, A.E. Couto, A. Echaide, I. Schnittger, L. Florin-Christensen, M. Babesia bovis contains an abundant parasite-specific protein-free glycerophosphatidylinositol and the genes predicted for its assembly |
| topic_facet |
Babesia bovis Glycolipids Glycosylphosphatidylinositol GPI acyltransferase dolichol phosphate mannosyltransferase 1 glycosylphosphatidylinositol glycosylphosphatidylinositol mannosyltransferase 1 glycosylphosphatidylinositol mannosyltransferase 2 glycosyltransferase mannosamine mannosyltransferase transferase transferase GPI 1 transferase PIG L transferase PIG W unclassified drug animal cell article Babesia bovis babesiosis controlled study cow growth inhibition in vitro study lipid analysis lipid composition nonhuman phospholipid synthesis protein assembly thin layer chromatography Animals Babesia bovis Gene Expression Regulation Hexosamines Phosphatidylinositols Babesia bovis Bovinae Eukaryota Protozoa Suidae |
| description |
Autonomous glycosylphosphatidylinositol (GPI) molecules (also protein-free GPIs or free GPIs) have been reported to be particularly abundant in some parasitic protozoa and mediate strong immunomodulatory effects on the host immune system. In the work at hand we have investigated the existence of free GPIs in Babesia bovis. Comparative thin layer chromatographic analysis of the protein-free glycolipid fraction of in vitro cultured B. bovis merozoites and erythrocyte membranes demonstrated the presence of an abundant parasite-specific band. Its chemical analysis revealed a GPI species containing a chain of two mannose residues, N-glucosamine and non-acylated inositol. The lipid moiety linked to inositol was diacylglycerol. The total fatty acid composition showed predominantly long-carbon chain molecules (12% of C22:0 and 45% of C24:0). The potential of B. bovis to assemble the presented free GPI species was verified by the existence of seven genes in its genome that putatively encode the following GPI biosynthetic enzymes: PI N-acetyl-GlcN-transferase (PIG-A and GPI-1), N-acetyl-GlcN-PI-de-N-acetylase (PIG-L), acyltransferase (PIG-W), dolichyl-phosphate mannosyl transferase (DPM-1), GPI mannosyltransferase I (PIG-M), and GPI mannosyltransferase II (PIG-V). GPI biosynthesis is vital for the intraerythrocytic parasite stage as mannosamine, an inhibitor of GPI biosynthesis, impaired in vitro growth of B. bovis merozoites. Absence of the vast majority of N-glycan metabolism encoding genes in the B. bovis genome underscores that the growth inhibitory effect of mannosamine is attributable to its interference with GPI biosynthesis and not with assembly of N-linked oligosaccharides, as has been described for higher eukaryotes. Elucidation of the structure and biosynthesis of GPI may allow to facilitate the development of future immune interventions against bovine babesiosis. © 2009 Elsevier B.V. All rights reserved. |
| format |
JOUR |
| author |
Rodríguez, A.E. Couto, A. Echaide, I. Schnittger, L. Florin-Christensen, M. |
| author_facet |
Rodríguez, A.E. Couto, A. Echaide, I. Schnittger, L. Florin-Christensen, M. |
| author_sort |
Rodríguez, A.E. |
| title |
Babesia bovis contains an abundant parasite-specific protein-free glycerophosphatidylinositol and the genes predicted for its assembly |
| title_short |
Babesia bovis contains an abundant parasite-specific protein-free glycerophosphatidylinositol and the genes predicted for its assembly |
| title_full |
Babesia bovis contains an abundant parasite-specific protein-free glycerophosphatidylinositol and the genes predicted for its assembly |
| title_fullStr |
Babesia bovis contains an abundant parasite-specific protein-free glycerophosphatidylinositol and the genes predicted for its assembly |
| title_full_unstemmed |
Babesia bovis contains an abundant parasite-specific protein-free glycerophosphatidylinositol and the genes predicted for its assembly |
| title_sort |
babesia bovis contains an abundant parasite-specific protein-free glycerophosphatidylinositol and the genes predicted for its assembly |
| url |
http://hdl.handle.net/20.500.12110/paper_03044017_v167_n2-4_p227_Rodriguez |
| work_keys_str_mv |
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