Serum IgM Glycosylation Associated with Tuberculosis Infection in Mice

ABSTRACT 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 glycosylatio...

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Autores principales:	Tadahiro Kumagai, Ainhoa Palacios, Arturo Casadevall, M. Jesús García, Carlos Toro, Michael Tiemeyer, Rafael Prados-Rosales
Formato:	article
Lenguaje:	EN
Publicado:	American Society for Microbiology 2019
Materias:	IgM Mycobacterium tuberculosis fucosylation glycans immunoglobulin M mice Microbiology QR1-502
Acceso en línea:	https://doaj.org/article/1c6d8067a5e341608122edaf43ec763a
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spelling	oai:doaj.org-article:1c6d8067a5e341608122edaf43ec763a2021-11-15T15:22:22ZSerum IgM Glycosylation Associated with Tuberculosis Infection in Mice10.1128/mSphere.00684-182379-5042https://doaj.org/article/1c6d8067a5e341608122edaf43ec763a2019-04-01T00:00:00Zhttps://journals.asm.org/doi/10.1128/mSphere.00684-18https://doaj.org/toc/2379-5042ABSTRACT 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. IMPORTANCE We demonstrate that M. tuberculosis infection influenced host protein glycosylation in a mouse model. The mechanism by which infection modifies glycans in serum proteins is not understood. Investigation of the regulation of such modifications by M. tuberculosis opens a new field that could lead to the discovery of novel biomarkers. Validation of such findings in human samples will reveal the clinical relevance of these findings.Tadahiro KumagaiAinhoa PalaciosArturo CasadevallM. Jesús GarcíaCarlos ToroMichael TiemeyerRafael Prados-RosalesAmerican Society for MicrobiologyarticleIgMMycobacterium tuberculosisfucosylationglycansimmunoglobulin MmiceMicrobiologyQR1-502ENmSphere, Vol 4, Iss 2 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	IgM Mycobacterium tuberculosis fucosylation glycans immunoglobulin M mice Microbiology QR1-502
spellingShingle	IgM Mycobacterium tuberculosis fucosylation glycans immunoglobulin M mice Microbiology QR1-502 Tadahiro Kumagai Ainhoa Palacios Arturo Casadevall M. Jesús García Carlos Toro Michael Tiemeyer Rafael Prados-Rosales Serum IgM Glycosylation Associated with Tuberculosis Infection in Mice
description	ABSTRACT 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. IMPORTANCE We demonstrate that M. tuberculosis infection influenced host protein glycosylation in a mouse model. The mechanism by which infection modifies glycans in serum proteins is not understood. Investigation of the regulation of such modifications by M. tuberculosis opens a new field that could lead to the discovery of novel biomarkers. Validation of such findings in human samples will reveal the clinical relevance of these findings.
format	article
author	Tadahiro Kumagai Ainhoa Palacios Arturo Casadevall M. Jesús García Carlos Toro Michael Tiemeyer Rafael Prados-Rosales
author_facet	Tadahiro Kumagai Ainhoa Palacios Arturo Casadevall M. Jesús García Carlos Toro Michael Tiemeyer Rafael Prados-Rosales
author_sort	Tadahiro Kumagai
title	Serum IgM Glycosylation Associated with Tuberculosis Infection in Mice
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
publisher	American Society for Microbiology
publishDate	2019
url	https://doaj.org/article/1c6d8067a5e341608122edaf43ec763a
work_keys_str_mv	AT tadahirokumagai serumigmglycosylationassociatedwithtuberculosisinfectioninmice AT ainhoapalacios serumigmglycosylationassociatedwithtuberculosisinfectioninmice AT arturocasadevall serumigmglycosylationassociatedwithtuberculosisinfectioninmice AT mjesusgarcia serumigmglycosylationassociatedwithtuberculosisinfectioninmice AT carlostoro serumigmglycosylationassociatedwithtuberculosisinfectioninmice AT michaeltiemeyer serumigmglycosylationassociatedwithtuberculosisinfectioninmice AT rafaelpradosrosales serumigmglycosylationassociatedwithtuberculosisinfectioninmice
_version_	1718427995905982464

Serum IgM Glycosylation Associated with Tuberculosis Infection in Mice

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