Serum IgM glycosylation associated with tuberculosis infection in mice

Tadahiro Kumagai, Ainhoa Palacios, Arturo Casadevall, M. Jesús García, Carlos Toro, Michael Tiemeyer, Rafael Prados-Rosales

Research output: Contribution to journalArticle

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.

Original languageEnglish (US)
Article numbere00684-18
JournalmSphere
Volume4
Issue number2
DOIs
StatePublished - Mar 1 2019

Fingerprint

Glycosylation
Mycobacterium tuberculosis
Immunoglobulin M
Tuberculosis
Glycoproteins
Mycobacterium Infections
Mycobacterium bovis
Infection
Serum
Polysaccharides
Mass Spectrometry
Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase
Lectins
Communicable Diseases
Digestion
Inflammation
Neoplasms

Keywords

  • Fucosylation
  • Glycans
  • IgM
  • Immunoglobulin M
  • Mice
  • Mycobacterium tuberculosis

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology

Cite this

Kumagai, T., Palacios, A., Casadevall, A., García, M. J., Toro, C., Tiemeyer, M., & Prados-Rosales, R. (2019). Serum IgM glycosylation associated with tuberculosis infection in mice. mSphere, 4(2), [e00684-18]. https://doi.org/10.1128/mSphere.00684-18

Serum IgM glycosylation associated with tuberculosis infection in mice. / Kumagai, Tadahiro; Palacios, Ainhoa; Casadevall, Arturo; García, M. Jesús; Toro, Carlos; Tiemeyer, Michael; Prados-Rosales, Rafael.

In: mSphere, Vol. 4, No. 2, e00684-18, 01.03.2019.

Research output: Contribution to journalArticle

Kumagai, T, Palacios, A, Casadevall, A, García, MJ, Toro, C, Tiemeyer, M & Prados-Rosales, R 2019, 'Serum IgM glycosylation associated with tuberculosis infection in mice', mSphere, vol. 4, no. 2, e00684-18. https://doi.org/10.1128/mSphere.00684-18
Kumagai T, Palacios A, Casadevall A, García MJ, Toro C, Tiemeyer M et al. Serum IgM glycosylation associated with tuberculosis infection in mice. mSphere. 2019 Mar 1;4(2). e00684-18. https://doi.org/10.1128/mSphere.00684-18
Kumagai, Tadahiro ; Palacios, Ainhoa ; Casadevall, Arturo ; García, M. Jesús ; Toro, Carlos ; Tiemeyer, Michael ; Prados-Rosales, Rafael. / Serum IgM glycosylation associated with tuberculosis infection in mice. In: mSphere. 2019 ; Vol. 4, No. 2.
@article{2fbe1a31e6374524961deef0d79dacb9,
title = "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 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.",
keywords = "Fucosylation, Glycans, IgM, Immunoglobulin M, Mice, Mycobacterium tuberculosis",
author = "Tadahiro Kumagai and Ainhoa Palacios and Arturo Casadevall and Garc{\'i}a, {M. Jes{\'u}s} and Carlos Toro and Michael Tiemeyer and Rafael Prados-Rosales",
year = "2019",
month = "3",
day = "1",
doi = "10.1128/mSphere.00684-18",
language = "English (US)",
volume = "4",
journal = "mSphere",
issn = "2379-5042",
publisher = "American Society for Microbiology",
number = "2",

}

TY - JOUR

T1 - Serum IgM glycosylation associated with tuberculosis infection in mice

AU - Kumagai, Tadahiro

AU - Palacios, Ainhoa

AU - Casadevall, Arturo

AU - García, M. Jesús

AU - Toro, Carlos

AU - Tiemeyer, Michael

AU - Prados-Rosales, Rafael

PY - 2019/3/1

Y1 - 2019/3/1

N2 - 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.

AB - 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.

KW - Fucosylation

KW - Glycans

KW - IgM

KW - Immunoglobulin M

KW - Mice

KW - Mycobacterium tuberculosis

UR - http://www.scopus.com/inward/record.url?scp=85063947065&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85063947065&partnerID=8YFLogxK

U2 - 10.1128/mSphere.00684-18

DO - 10.1128/mSphere.00684-18

M3 - Article

VL - 4

JO - mSphere

JF - mSphere

SN - 2379-5042

IS - 2

M1 - e00684-18

ER -