Analysis of Intracellular Trafficking of Cholera Toxin B Subunits Depending on Ganglioside GM1 in Tissue-Resident Macrophages.

Izumi Sasaki, Shiori Kaji, Naoko Wakaki-Nishiyama, Tsuneyasu Kaisho

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Article in Methods in molecular biology (Clifton, N.J.), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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4 authors.

Izumi SasakiDepartment of Immunology, Institute of Advanced Medicine, Wakayama Medical University, Wakayama, Wakayama, Japan. izumisas@wakayama-med.ac.jp.

Shiori KajiSecond Department of Internal Medicine, Wakayama Medical University, Wakayama, Wakayama, Japan.

Naoko Wakaki-NishiyamaDepartment of Immunology, Institute of Advanced Medicine, Wakayama Medical University, Wakayama, Wakayama, Japan.

Tsuneyasu KaishoDepartment of Immunology, Institute of Advanced Medicine, Wakayama Medical University, Wakayama, Wakayama, Japan.

Funding

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6 · The paper itself

Abstract

Cholera toxin (CT) is a bacterial exotoxin secreted by Vibrio cholerae. CT is comprised of one toxic A subunit (CTA) and five nontoxic B subunits (CTB). CTB is required for internalization of CT through binding with a membrane glycolipid ganglioside GM1. Previously, we clarified that CTB could induce production of proinflammatory cytokine interleukin-1β (IL-1β) from murine resident peritoneal macrophages (RPMs) in synergy with lipopolysaccharide (LPS) through a ganglioside GM1-dependent manner. Then, CTB was incorporated into endoplasmic reticulum (ER) depending on GM1 and activate ER stress sensor, inositol-requiring enzyme 1 alpha (IRE1α). IRE1α was required for both ER stress responses and IL-1β production in CTB- plus LPS-stimulated RPMs. These findings indicate that ganglioside GM1 functions not only for cell-surface receptor for CTB but also for cross talk with the ER stress sensor, IRE1α, in RPMs. Here, we describe the protocols for analysis of intracellular trafficking of CTB depending on ganglioside GM1 in RPMs.

Indexed as

Cholera ToxinG(M1) GangliosideMacrophagesMacrophages, PeritonealAnimalsEndoplasmic ReticulumEndoplasmic Reticulum StressEndoribonucleasesInterleukin-1betaLipopolysaccharidesMiceProtein Serine-Threonine KinasesProtein TransportCholera ToxinEndoribonucleasesErn1 protein, mouseG(M1) GangliosideInterleukin-1betaLipopolysaccharidesProtein Serine-Threonine KinasesCholera toxinGanglioside GM1Resident peritoneal macrophages

Identifiers

PMID42613525

DOI10.1007/978-1-0716-1971-1_9

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