Negligible elongation of mucin glycans with Gal β1-3 units distinguishes the laminated layer of Echinococcus multilocularis from that of Echinococcus granulosus
Autor: | Sylvia Dematteis, Uriel Koziol, Marco Navatta, Gerardo Lin, Guillermo Moyna, Carolina Fontana, Alvaro Díaz, Fernando Ferreira, Klaus Brehm, Lucía del Puerto, Romina Rovetta |
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Rok vydání: | 2016 |
Předmět: |
0301 basic medicine
Glycan Magnetic Resonance Spectroscopy Biology Echinococcus multilocularis Gene Expression Regulation Enzymologic Mice 03 medical and health sciences chemistry.chemical_compound Polysaccharides Tandem Mass Spectrometry parasitic diseases Glycosyltransferase Animals Data Mining Echinococcus granulosus Peritoneal Cavity Mice Inbred BALB C Genome Reverse Transcriptase Polymerase Chain Reaction Mucin Mucins Glycosyltransferases biology.organism_classification Glycome In vitro 030104 developmental biology Infectious Diseases chemistry Biochemistry Larva Spectrometry Mass Matrix-Assisted Laser Desorption-Ionization Galactose Chromatography Gel biology.protein Parasitology Gerbillinae Transcriptome |
Zdroj: | International Journal for Parasitology. 46:311-321 |
ISSN: | 0020-7519 |
DOI: | 10.1016/j.ijpara.2015.12.009 |
Popis: | The larval stages of the cestodes Echinococcus multilocularis and Echinococcus granulosus cause the important zoonoses known as larval echinococcoses. These larvae are protected by a unique, massive, mucin-based structure known as the laminated layer. The mucin glycans of the E. granulosus laminated layer are core 1- or core 2-based O-glycans in which the core Galpβ1-3 residue can initiate a chain comprising one to three additional Galpβ1-3 residues, a motif not known in mammalian carbohydrates. This chain can be capped with a Galpα1-4 residue, and can be ramified with GlcNAcpβ1-6 residues. These, as well as the GlcNAcpβ1-6 residue in core 2, can be decorated with the Galpα1-4Galpβ1-4 disaccharide. Here we extend our analysis to the laminated layer of E. multilocularis, showing that the non-decorated cores, together with Galpβ1-3(Galpα1-4Galpβ1-4GlcNAcpβ1-6)GalNAc, comprise over 96% of the glycans in molar terms. This simple laminated layer glycome is exhibited by E. multilocularis grown either in vitro or in vivo. Interestingly, all the differences with the complex laminated layer glycome found in E. granulosus may be explained in terms of strongly reduced activity in E. multilocularis of a putative glycosyltransferase catalysing the elongation with Galpβ1-3. Comparative inter-species analysis of available genomic and transcriptomic data suggested a candidate for this enzyme, amongst more than 20 putative (non-core 1) Gal/GlcNAc β1-3 transferases present in each species as a result of a taeniid-specific gene expansion. The candidate gene was experimentally verified to be transcribed at much higher levels in the larva of E. granulosus than that of E. multilocularis. |
Databáze: | OpenAIRE |
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