Serum IgM glycosylation associated with tuberculosis infection in mice

Changes in serum glycans discriminate between disease statuses in cancer. A similar connection has not been established in the context of infectious diseases such as tuberculosis (TB). The inflammation arising from infection by Mycobacterium tuberculosis may affect host protein glycosylation,thereby...

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Detalles Bibliográficos
Autores: Kumagai, Tadahiro, Palacios, Ainhoa, Casadevall, Arturo, García García, María Jesús, Toro, Carlos, Tiemeyer, Michael, Prados Rosales, Rafael Carlos
Tipo de recurso: artículo
Fecha de publicación:2019
País:España
Institución:Universidad Autónoma de Madrid
Repositorio:Biblos-e Archivo. Repositorio Institucional de la UAM
Idioma:inglés
OAI Identifier:oai:repositorio.uam.es:10486/688809
Acceso en línea:http://hdl.handle.net/10486/688809
https://dx.doi.org/10.1128/mSphere.00684-18
Access Level:acceso abierto
Palabra clave:Fucosylation
Glycans
IgM
Immunoglobulin M
Mice
Mycobacterium tuberculosis
Medicina
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spelling Serum IgM glycosylation associated with tuberculosis infection in miceKumagai, TadahiroPalacios, AinhoaCasadevall, ArturoGarcía García, María JesúsToro, CarlosTiemeyer, MichaelPrados Rosales, Rafael CarlosFucosylationGlycansIgMImmunoglobulin MMiceMycobacterium tuberculosisMedicinaChanges in serum glycans discriminate between disease statuses in cancer. A similar connection has not been established in the context of infectious diseases such as tuberculosis (TB). The inflammation arising from infection by Mycobacterium tuberculosis may affect host protein glycosylation,thereby providing information about disease status in TB. A mouse model of infection was used to study glycoprotein N-glycosylation in serum. Following digestion of serum glycoproteins with peptide-N-glycosidase F (PNGase F), released glycans were permethylated and analyzed by multidimensional mass spectrometry (MS). Conditions included naive or Mycobacterium bovis BCG-vaccinated animals, which were either uninfected or infected with M. tuberculosis. MS results were validated by lectin blotting. We found that both glycoprotein fucosylation and sialylation were particularly sensitive to M. tuberculosis infection. We observed that M. tuberculosis infection elevates serum IgM levels and induces changes in glycosylation that could inform about the disease.Glycomic and glycoproteomic analyses were supported by grants from NIH (P41GM103490 and P01HL107151) to M.T. R.P.-R. is supported in part by NIH/NIAID grant AI115091. R.P.-R. is furthermore a Ramon y Cajal fellow from the Spanish Ministry of Economy and Competitiveness. R.P.-R. is also supported by the Spanish Ministry of Economy and Competitiveness (grant SAF2016-77433-R). R.P.-R. acknowledges support from CICbioGUNE through the Severo Ochoa Excellence Accreditation (SEV-2016-0644)American Society for MicrobiologyDepartamento de Medicina Preventiva y Salud Pública y MicrobiologíaFacultad de Medicina20192019-03-01research articlehttp://purl.org/coar/resource_type/c_2df8fbb1VoRhttp://purl.org/coar/version/c_970fb48d4fbd8a85info:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10486/688809https://dx.doi.org/10.1128/mSphere.00684-18reponame:Biblos-e Archivo. Repositorio Institucional de la UAMinstname:Universidad Autónoma de MadridInglésengopen accesshttp://purl.org/coar/access_right/c_abf2info:eu-repo/semantics/openAccessoai:repositorio.uam.es:10486/6888092026-06-23T12:46:27Z
dc.title.none.fl_str_mv Serum IgM glycosylation associated with tuberculosis infection in mice
title Serum IgM glycosylation associated with tuberculosis infection in mice
spellingShingle Serum IgM glycosylation associated with tuberculosis infection in mice
Kumagai, Tadahiro
Fucosylation
Glycans
IgM
Immunoglobulin M
Mice
Mycobacterium tuberculosis
Medicina
title_short Serum IgM glycosylation associated with tuberculosis infection in mice
title_full Serum IgM glycosylation associated with tuberculosis infection in mice
title_fullStr Serum IgM glycosylation associated with tuberculosis infection in mice
title_full_unstemmed Serum IgM glycosylation associated with tuberculosis infection in mice
title_sort Serum IgM glycosylation associated with tuberculosis infection in mice
dc.creator.none.fl_str_mv Kumagai, Tadahiro
Palacios, Ainhoa
Casadevall, Arturo
García García, María Jesús
Toro, Carlos
Tiemeyer, Michael
Prados Rosales, Rafael Carlos
author Kumagai, Tadahiro
author_facet Kumagai, Tadahiro
Palacios, Ainhoa
Casadevall, Arturo
García García, María Jesús
Toro, Carlos
Tiemeyer, Michael
Prados Rosales, Rafael Carlos
author_role author
author2 Palacios, Ainhoa
Casadevall, Arturo
García García, María Jesús
Toro, Carlos
Tiemeyer, Michael
Prados Rosales, Rafael Carlos
author2_role author
author
author
author
author
author
dc.contributor.none.fl_str_mv Departamento de Medicina Preventiva y Salud Pública y Microbiología
Facultad de Medicina
dc.subject.none.fl_str_mv Fucosylation
Glycans
IgM
Immunoglobulin M
Mice
Mycobacterium tuberculosis
Medicina
topic Fucosylation
Glycans
IgM
Immunoglobulin M
Mice
Mycobacterium tuberculosis
Medicina
description Changes in serum glycans discriminate between disease statuses in cancer. A similar connection has not been established in the context of infectious diseases such as tuberculosis (TB). The inflammation arising from infection by Mycobacterium tuberculosis may affect host protein glycosylation,thereby providing information about disease status in TB. A mouse model of infection was used to study glycoprotein N-glycosylation in serum. Following digestion of serum glycoproteins with peptide-N-glycosidase F (PNGase F), released glycans were permethylated and analyzed by multidimensional mass spectrometry (MS). Conditions included naive or Mycobacterium bovis BCG-vaccinated animals, which were either uninfected or infected with M. tuberculosis. MS results were validated by lectin blotting. We found that both glycoprotein fucosylation and sialylation were particularly sensitive to M. tuberculosis infection. We observed that M. tuberculosis infection elevates serum IgM levels and induces changes in glycosylation that could inform about the disease.
publishDate 2019
dc.date.none.fl_str_mv 2019
2019-03-01
dc.type.none.fl_str_mv research article
http://purl.org/coar/resource_type/c_2df8fbb1
VoR
http://purl.org/coar/version/c_970fb48d4fbd8a85
dc.type.openaire.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv http://hdl.handle.net/10486/688809
https://dx.doi.org/10.1128/mSphere.00684-18
url http://hdl.handle.net/10486/688809
https://dx.doi.org/10.1128/mSphere.00684-18
dc.language.none.fl_str_mv Inglés
eng
language_invalid_str_mv Inglés
language eng
dc.rights.none.fl_str_mv open access
http://purl.org/coar/access_right/c_abf2
dc.rights.openaire.fl_str_mv info:eu-repo/semantics/openAccess
rights_invalid_str_mv open access
http://purl.org/coar/access_right/c_abf2
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv American Society for Microbiology
publisher.none.fl_str_mv American Society for Microbiology
dc.source.none.fl_str_mv reponame:Biblos-e Archivo. Repositorio Institucional de la UAM
instname:Universidad Autónoma de Madrid
instname_str Universidad Autónoma de Madrid
reponame_str Biblos-e Archivo. Repositorio Institucional de la UAM
collection Biblos-e Archivo. Repositorio Institucional de la UAM
repository.name.fl_str_mv
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