N-Glycosylation in piroplasmids : Diversity within simplicity
N-glycosylation has remained mostly unexplored in Piroplasmida, an order of tick-transmitted pathogens of veterinary and medical relevance. Analysis of 11 piroplasmid genomes revealed three distinct scenarios regarding N-glycosylation: Babesia sensu stricto (s.s.) species add one or two N-acetylgluc...
| Autores principales: | , , , , , , |
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| Formato: | Artículo |
| Lenguaje: | Inglés |
| Publicado: |
MDPI
2021
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| Materias: | |
| Acceso en línea: | http://hdl.handle.net/20.500.12123/9115 https://www.mdpi.com/2076-0817/10/1/50 https://doi.org/10.3390/pathogens10010050 |
| _version_ | 1855484333751533568 |
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| author | Florin-Christensen, Mónica Rodriguez, Anabel Elisa Suarez, Carlos Esteban Ueti, Massaro W. Delgado, Fernando Oscar Echaide, Ignacio Eduardo Schnittger, Leonhard |
| author_browse | Delgado, Fernando Oscar Echaide, Ignacio Eduardo Florin-Christensen, Mónica Rodriguez, Anabel Elisa Schnittger, Leonhard Suarez, Carlos Esteban Ueti, Massaro W. |
| author_facet | Florin-Christensen, Mónica Rodriguez, Anabel Elisa Suarez, Carlos Esteban Ueti, Massaro W. Delgado, Fernando Oscar Echaide, Ignacio Eduardo Schnittger, Leonhard |
| author_sort | Florin-Christensen, Mónica |
| collection | INTA Digital |
| description | N-glycosylation has remained mostly unexplored in Piroplasmida, an order of tick-transmitted pathogens of veterinary and medical relevance. Analysis of 11 piroplasmid genomes revealed three distinct scenarios regarding N-glycosylation: Babesia sensu stricto (s.s.) species add one or two N-acetylglucosamine (NAcGlc) molecules to proteins; Theileria equi and Cytauxzoon felis add (NAcGlc)2-mannose, while B. microti and Theileria s.s. synthesize dolichol-P-P-NAcGlc and dolichol-P-P-(NAcGlc)2 without subsequent transfer to proteins. All piroplasmids possess the gene complement needed for the synthesis of the N-glycosylation substrates, dolichol-P and sugar nucleotides. The oligosaccharyl transferase of Babesia species, T. equi and C. felis, is predicted to be composed of only two subunits, STT3 and Ost1. Occurrence of short N-glycans in B. bovis merozoites was experimentally demonstrated by fluorescence microscopy using a NAcGlc-specific lectin. In vitro growth of B. bovis was significantly impaired by tunicamycin, an inhibitor of N-glycosylation, indicating a relevant role for N-glycosylation in this pathogen. Finally, genes coding for N-glycosylation enzymes and substrate biosynthesis are transcribed in B. bovis blood and tick stages, suggesting that this pathway is biologically relevant throughout the parasite life cycle. Elucidation of the role/s exerted by N-glycans will increase our understanding of these successful parasites, for which improved control measures are needed. |
| format | Artículo |
| id | INTA9115 |
| institution | Instituto Nacional de Tecnología Agropecuaria (INTA -Argentina) |
| language | Inglés |
| publishDate | 2021 |
| publishDateRange | 2021 |
| publishDateSort | 2021 |
| publisher | MDPI |
| publisherStr | MDPI |
| record_format | dspace |
| spelling | INTA91152021-04-16T16:49:50Z N-Glycosylation in piroplasmids : Diversity within simplicity Florin-Christensen, Mónica Rodriguez, Anabel Elisa Suarez, Carlos Esteban Ueti, Massaro W. Delgado, Fernando Oscar Echaide, Ignacio Eduardo Schnittger, Leonhard Piroplasmea Babesia Theileria Cytauxzoon Glicosidos Glycosides N-glycosylation has remained mostly unexplored in Piroplasmida, an order of tick-transmitted pathogens of veterinary and medical relevance. Analysis of 11 piroplasmid genomes revealed three distinct scenarios regarding N-glycosylation: Babesia sensu stricto (s.s.) species add one or two N-acetylglucosamine (NAcGlc) molecules to proteins; Theileria equi and Cytauxzoon felis add (NAcGlc)2-mannose, while B. microti and Theileria s.s. synthesize dolichol-P-P-NAcGlc and dolichol-P-P-(NAcGlc)2 without subsequent transfer to proteins. All piroplasmids possess the gene complement needed for the synthesis of the N-glycosylation substrates, dolichol-P and sugar nucleotides. The oligosaccharyl transferase of Babesia species, T. equi and C. felis, is predicted to be composed of only two subunits, STT3 and Ost1. Occurrence of short N-glycans in B. bovis merozoites was experimentally demonstrated by fluorescence microscopy using a NAcGlc-specific lectin. In vitro growth of B. bovis was significantly impaired by tunicamycin, an inhibitor of N-glycosylation, indicating a relevant role for N-glycosylation in this pathogen. Finally, genes coding for N-glycosylation enzymes and substrate biosynthesis are transcribed in B. bovis blood and tick stages, suggesting that this pathway is biologically relevant throughout the parasite life cycle. Elucidation of the role/s exerted by N-glycans will increase our understanding of these successful parasites, for which improved control measures are needed. Instituto de Patobiología Fil: Florin-Christensen, Mónica. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Patobiología; Argentina Fil: Florin-Christensen, Mónica. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Fil: Rodriguez, Anabel Elisa. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Patobiología; Argentina Fil: Rodriguez, Anabel Elisa. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Fil: Suarez, Carlos Esteban. Washington State University. College of Veterinary Medicine. Department of Veterinary Microbiology and Pathology; Estados Unidos Fil: Suarez, Carlos Esteban. United States Department of Agricultural-Agricultural Research Service. Animal Disease Research Unit; Estados Unidos Fil: Ueti, Massaro W. Washington State University. College of Veterinary Medicine. Department of Veterinary Microbiology and Pathology; Estados Unidos Fil: Ueti, Massaro W. United States Department of Agricultural-Agricultural Research Service. Animal Disease Research Unit; Estados Unidos Fil: Delgado, Fernando Oscar. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Patobiología; Argentina Fil: Delgado, Fernando Oscar. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Fil: Echaide, Ignacio Eduardo. Instituto Nacional de Tecnología Agropecuaria (INTA). Estación Experimental Agropecuaria Rafaela; Argentina Fil: Schnittger, Leonhard. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Patobiología; Argentina Fil: Schnittger, Leonhard. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina 2021-04-16T16:41:07Z 2021-04-16T16:41:07Z 2021-01 info:ar-repo/semantics/artículo info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://hdl.handle.net/20.500.12123/9115 https://www.mdpi.com/2076-0817/10/1/50 2076-0817 https://doi.org/10.3390/pathogens10010050 eng info:eu-repograntAgreement/INTA/2019-PD-E5-I102-001/2019-PD-E5-I102-001/AR./Desarrollo de vacunas y tecnologías para mejorar las estrategias profilácticas y terapéuticas de las enfermedades que afectan la producción animal y la salud pública info:eu-repograntAgreement/INTA/2019-PD-E5-I105-001/2019-PD-E5-I105-001/AR./Patógenos animales: su interacción con el hospedador y el medio ambiente. Impacto en productividad, ecosistemas, sanidad animal y salud pública en el marco “Una Salud” info:eu-repograntAgreement/INTA/2019-PE-E5-I109-001/2019-PE-E5-I109-001/AR./Convocatoria: Estudios para el control de enfermedades subtropicales y/o transmitidas por vectores (Tristeza Bovina, Garrapatas, Miasis, Tripanosomiasis, Lengua Azul y la info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by-nc-sa/4.0/ Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0) application/pdf MDPI Pathogens 10 (1) : 50 (Enero 2021) |
| spellingShingle | Piroplasmea Babesia Theileria Cytauxzoon Glicosidos Glycosides Florin-Christensen, Mónica Rodriguez, Anabel Elisa Suarez, Carlos Esteban Ueti, Massaro W. Delgado, Fernando Oscar Echaide, Ignacio Eduardo Schnittger, Leonhard N-Glycosylation in piroplasmids : Diversity within simplicity |
| title | N-Glycosylation in piroplasmids : Diversity within simplicity |
| title_full | N-Glycosylation in piroplasmids : Diversity within simplicity |
| title_fullStr | N-Glycosylation in piroplasmids : Diversity within simplicity |
| title_full_unstemmed | N-Glycosylation in piroplasmids : Diversity within simplicity |
| title_short | N-Glycosylation in piroplasmids : Diversity within simplicity |
| title_sort | n glycosylation in piroplasmids diversity within simplicity |
| topic | Piroplasmea Babesia Theileria Cytauxzoon Glicosidos Glycosides |
| url | http://hdl.handle.net/20.500.12123/9115 https://www.mdpi.com/2076-0817/10/1/50 https://doi.org/10.3390/pathogens10010050 |
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