Immunomodulatory Functions of Glycolipids from Pathogens.

BMDC generation BMDC/T cell co-culture Glycolipid extraction Myeloid cell activation assay ROS production assay Reporter cell assay

Journal

Methods in molecular biology (Clifton, N.J.)
ISSN: 1940-6029
Titre abrégé: Methods Mol Biol
Pays: United States
ID NLM: 9214969

Informations de publication

Date de publication:
2023
Historique:
entrez: 31 12 2022
pubmed: 1 1 2023
medline: 4 1 2023
Statut: ppublish

Résumé

The cell envelopes of pathogens comprise a wealth of unique glycolipids, which are important modulators of the host immune responses during infection and in some cases have been used as adjuvants. Despite this abundant basic knowledge, the identities of the host immune receptors for mycobacterial lipids have long been elusive (Ishikawa et al., Trends Immunol 38:66-76, 2017). We describe the method of how to isolate glycolipids from microorganisms and how to analyze the glycolipids' potential to activate reporter cells and bone marrow-derived dendritic cells (BMDCs), such as surface marker expression and reactive oxygen species (ROS) production. Additionally, we outline an in vitro BMDC/T cell coculture model to investigate functional consequences of leukocyte activation, such as cytokine production. In this chapter, we provide a guide for extracting glycolipids from microorganisms and how to use them to activate leukocytes. We also present methods on how to generate and activate reporter cells, as well as BMDCs and how to set up BMDC/T cell cocultures. We further outline how to generate samples and how to analyze the immunomodulatory effect glycolipid exposure has on these cells, via flow cytometry, ROS production assays and ELISA.

Identifiants

pubmed: 36587068
doi: 10.1007/978-1-0716-2910-9_3
doi:

Substances chimiques

Glycolipids 0
Reactive Oxygen Species 0
Adjuvants, Immunologic 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

23-31

Informations de copyright

© 2023. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.

Références

Ishikawa E, Mori D, Yamasaki S (2017) Recognition of mycobacterial lipids by immune receptors. Trends Immunol 38:66–76
doi: 10.1016/j.it.2016.10.009
Chiffoleau E (2018) C-type lectin-like receptors as emerging orchestrators of sterile inflammation represent potential therapeutic targets. Front Immunol 9:227
doi: 10.3389/fimmu.2018.00227
Yamasaki S, Ishikawa E, Sakuma M et al (2008) Mincle is an ITAM-coupled activating receptor that senses damaged cells. Nat Immunol 9:1179–1188
doi: 10.1038/ni.1651
Vartabedian VF, Savage PB, Peyton L (2016) The processing and presentation of lipids and glycolipids to the immune system. Immunol Rev 272:109–119
doi: 10.1111/imr.12431
Ishikawa E, Ishikawa T, Morita YS et al (2009) Direct recognition of the mycobacterial glycolipid, trehalose dimycolate, by C-type lectin Mincle. J Exp Med 206:2879–2888
doi: 10.1084/jem.20091750
Ishikawa T, Itoh F, Yoshida S et al (2013) Identification of distinct ligands for the C-type lectin receptors Mincle and Dectin-2 in the pathogenic fungus Malassezia. Cell Host Microbe 13:477–488
doi: 10.1016/j.chom.2013.03.008
Toyonaga K, Torigoe S, Motomura Y et al (2016) C-type lectin receptor DCAR recognizes mycobacterial Phosphatidyl-inositol Mannosides to promote a Th1 response during infection. Immunity 45:1245–1257
doi: 10.1016/j.immuni.2016.10.012
Miyake Y, Toyonaga K, Mori D et al (2013) C-type lectin MCL is an FcRγ-coupled receptor that mediates the adjuvanticity of mycobacterial cord factor. Immunity 38:1050–1062
doi: 10.1016/j.immuni.2013.03.010
Yonekawa A, Saijo S, Hoshino Y et al (2014) Dectin-2 is a direct receptor for mannose-capped lipoarabinomannan of mycobacteria. Immunity 41:402–413
doi: 10.1016/j.immuni.2014.08.005
Folch J, Lees M, Stanley GHS (1956) A simple method for the isolation and purification of total lipides from animal tissues. J Biol Chem 226:497–509
doi: 10.1016/S0021-9258(18)64849-5

Auteurs

Carla Guenther (C)

Tampere Institute for Advanced Study, Faculty of Medicine and Health Technology, University of Tampere, Tampere, Finland.
Department of Molecular Immunology, Research Institute for Microbial Diseases, Osaka University, Suita, Osaka, Japan.
Laboratory of Molecular Immunology, Immunology Frontier Research Center, Osaka University, Suita, Osaka, Japan.

Miyuki Watanabe (M)

Department of Molecular Immunology, Research Institute for Microbial Diseases, Osaka University, Suita, Osaka, Japan.
Laboratory of Molecular Immunology, Immunology Frontier Research Center, Osaka University, Suita, Osaka, Japan.

Sho Yamasaki (S)

Department of Molecular Immunology, Research Institute for Microbial Diseases, Osaka University, Suita, Osaka, Japan. yamasaki@biken.osaka-u.ac.jp.
Laboratory of Molecular Immunology, Immunology Frontier Research Center, Osaka University, Suita, Osaka, Japan. yamasaki@biken.osaka-u.ac.jp.
Center for Infectious Disease Education and Research (CiDER), Osaka University, Osaka, Japan. yamasaki@biken.osaka-u.ac.jp.
Division of Molecular Immunology, Medical Mycology Research Center, Chiba University, Chiba, Japan. yamasaki@biken.osaka-u.ac.jp.

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