N-Glycosylation in piroplasmids: diversity within simplicity

Autores
Florin Christensen, Mónica; Rodriguez, Anabel Elisa; Suárez, Carlos E.; Ueti, Massaro W.; Delgado, Fernando Oscar; Echaide, Ignacio Eduardo; Schnittger, Leonhard
Año de publicación
2021
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
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.
Fil: Florin Christensen, Mónica. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas. Instituto de Patobiología; Argentina
Fil: Rodriguez, Anabel Elisa. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas. Instituto de Patobiología Veterinaria - Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Patobiología Veterinaria; Argentina
Fil: Suárez, Carlos E.. Washington State University; Estados Unidos. United States Department of Agricultural-Agricultural Research Service. Animal Disease Research Unit; Estados Unidos
Fil: Ueti, Massaro W.. Washington State University; Estados Unidos. United States Department of Agricultural-Agricultural Research Service. Animal Disease Research Unit; Estados Unidos
Fil: Delgado, Fernando Oscar. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas. Instituto de Patobiología; Argentina
Fil: Echaide, Ignacio Eduardo. Instituto Nacional de Tecnología Agropecuaria; Argentina
Fil: Schnittger, Leonhard. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas. Instituto de Patobiología Veterinaria - Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Patobiología Veterinaria; Argentina
Materia
BABESIA
CYTAUXZOON
DOLICHOL
N-GLYCAN
PIROPLASMIDS
SUGAR NUCLEOTIDES
THEILERIA
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/162193
Acceder
id CONICETDig_cf336a7417fb950b0602dc374fffcc6f
oai_identifier_str oai:ri.conicet.gov.ar:11336/162193
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling N-Glycosylation in piroplasmids: diversity within simplicityFlorin Christensen, MónicaRodriguez, Anabel ElisaSuárez, Carlos E.Ueti, Massaro W.Delgado, Fernando OscarEchaide, Ignacio EduardoSchnittger, LeonhardBABESIACYTAUXZOONDOLICHOLN-GLYCANPIROPLASMIDSSUGAR NUCLEOTIDESTHEILERIAhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1N-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.Fil: Florin Christensen, Mónica. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas. Instituto de Patobiología; ArgentinaFil: Rodriguez, Anabel Elisa. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas. Instituto de Patobiología Veterinaria - Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Patobiología Veterinaria; ArgentinaFil: Suárez, Carlos E.. Washington State University; Estados Unidos. United States Department of Agricultural-Agricultural Research Service. Animal Disease Research Unit; Estados UnidosFil: Ueti, Massaro W.. Washington State University; Estados Unidos. United States Department of Agricultural-Agricultural Research Service. Animal Disease Research Unit; Estados UnidosFil: Delgado, Fernando Oscar. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas. Instituto de Patobiología; ArgentinaFil: Echaide, Ignacio Eduardo. Instituto Nacional de Tecnología Agropecuaria; ArgentinaFil: Schnittger, Leonhard. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas. Instituto de Patobiología Veterinaria - Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Patobiología Veterinaria; ArgentinaMultidisciplinary Digital Publishing Institute2021-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/162193Florin Christensen, Mónica; Rodriguez, Anabel Elisa; Suárez, Carlos E.; Ueti, Massaro W.; Delgado, Fernando Oscar; et al.; N-Glycosylation in piroplasmids: diversity within simplicity; Multidisciplinary Digital Publishing Institute; Pathogens; 10; 1; 1-2021; 1-142076-0817CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/2076-0817/10/1/50info:eu-repo/semantics/altIdentifier/doi/10.3390/pathogens10010050info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:12:03Zoai:ri.conicet.gov.ar:11336/162193instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-03 10:12:03.958CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv N-Glycosylation in piroplasmids: diversity within simplicity
title N-Glycosylation in piroplasmids: diversity within simplicity
spellingShingle N-Glycosylation in piroplasmids: diversity within simplicity
Florin Christensen, Mónica
BABESIA
CYTAUXZOON
DOLICHOL
N-GLYCAN
PIROPLASMIDS
SUGAR NUCLEOTIDES
THEILERIA
title_short 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_sort N-Glycosylation in piroplasmids: diversity within simplicity
dc.creator.none.fl_str_mv Florin Christensen, Mónica
Rodriguez, Anabel Elisa
Suárez, Carlos E.
Ueti, Massaro W.
Delgado, Fernando Oscar
Echaide, Ignacio Eduardo
Schnittger, Leonhard
author Florin Christensen, Mónica
author_facet Florin Christensen, Mónica
Rodriguez, Anabel Elisa
Suárez, Carlos E.
Ueti, Massaro W.
Delgado, Fernando Oscar
Echaide, Ignacio Eduardo
Schnittger, Leonhard
author_role author
author2 Rodriguez, Anabel Elisa
Suárez, Carlos E.
Ueti, Massaro W.
Delgado, Fernando Oscar
Echaide, Ignacio Eduardo
Schnittger, Leonhard
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv BABESIA
CYTAUXZOON
DOLICHOL
N-GLYCAN
PIROPLASMIDS
SUGAR NUCLEOTIDES
THEILERIA
topic BABESIA
CYTAUXZOON
DOLICHOL
N-GLYCAN
PIROPLASMIDS
SUGAR NUCLEOTIDES
THEILERIA
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv 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.
Fil: Florin Christensen, Mónica. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas. Instituto de Patobiología; Argentina
Fil: Rodriguez, Anabel Elisa. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas. Instituto de Patobiología Veterinaria - Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Patobiología Veterinaria; Argentina
Fil: Suárez, Carlos E.. Washington State University; Estados Unidos. United States Department of Agricultural-Agricultural Research Service. Animal Disease Research Unit; Estados Unidos
Fil: Ueti, Massaro W.. Washington State University; Estados Unidos. United States Department of Agricultural-Agricultural Research Service. Animal Disease Research Unit; Estados Unidos
Fil: Delgado, Fernando Oscar. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas. Instituto de Patobiología; Argentina
Fil: Echaide, Ignacio Eduardo. Instituto Nacional de Tecnología Agropecuaria; Argentina
Fil: Schnittger, Leonhard. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas. Instituto de Patobiología Veterinaria - Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Patobiología Veterinaria; Argentina
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.
publishDate 2021
dc.date.none.fl_str_mv 2021-01
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/162193
Florin Christensen, Mónica; Rodriguez, Anabel Elisa; Suárez, Carlos E.; Ueti, Massaro W.; Delgado, Fernando Oscar; et al.; N-Glycosylation in piroplasmids: diversity within simplicity; Multidisciplinary Digital Publishing Institute; Pathogens; 10; 1; 1-2021; 1-14
2076-0817
CONICET Digital
CONICET
url http://hdl.handle.net/11336/162193
identifier_str_mv Florin Christensen, Mónica; Rodriguez, Anabel Elisa; Suárez, Carlos E.; Ueti, Massaro W.; Delgado, Fernando Oscar; et al.; N-Glycosylation in piroplasmids: diversity within simplicity; Multidisciplinary Digital Publishing Institute; Pathogens; 10; 1; 1-2021; 1-14
2076-0817
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/2076-0817/10/1/50
info:eu-repo/semantics/altIdentifier/doi/10.3390/pathogens10010050
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Multidisciplinary Digital Publishing Institute
publisher.none.fl_str_mv Multidisciplinary Digital Publishing Institute
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.13397

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