Activation of the toll-like receptor 2 signaling pathway by GAPDH from bacterial strain RD055328

Author:

Kurata Atsushi1ORCID,Takeuchi Shimpei1,Fujiwara Ryo1,Tamura Kento1,Imai Tomoya2,Yamasaki-Yashiki Shino3ORCID,Onuma Hiroki1,Fukuta Yasuhisa1,Shirasaka Norifumi1,Uegaki Koichi14ORCID

Affiliation:

1. Department of Applied Biological Chemistry, Faculty of Agriculture, Kindai University , Nakamachi, Nara , Japan

2. Research Institute for Sustainable Humanosphere, Kyoto University , Uji, Kyoto , Japan

3. Department of Life Science and Biotechnology, Faculty of Chemistry, Materials and Bioengineering, Kansai University , Suita, Osaka , Japan

4. Agricultural Technology and Innovation Research Institute, Kindai University , Nakamachi, Nara, Japan

Abstract

ABSTRACT We characterized the membrane vesicle fraction (RD-MV fraction) from bacterial strain RD055328, which is related to members of the genus Companilactobacillus and Lactiplantibacillus plantarum. RD-MVs and glyceraldehyde 3-phosphate dehydrogenase (GAPDH) were detected in the RD-MV fraction. Immunoglobulin A (IgA) was produced by Peyer's patch cells following the addition of the RD-MV fraction. In the presence of the RD-MV fraction, RAW264 cells produced the pro-inflammatory cytokine IL-6. Recombinant GAPDH probably induced the production of IL-6 by RAW264 cells via superficial toll-like receptor 2 (TLR2) recognition. A confocal laser scanning microscopy image analysis indicated that RD-MVs and GAPDH were taken up by RAW264 cells. GAPDH wrapped around RAW264 cells. We suggest that GAPDH from strain RD055328 enhanced the production of IgA by acquired immune cells via the production of IL-6 by innate immune cells through TLR2 signal transduction.

Funder

JSPS

Analysis and Development System for Advanced Materials

Kyoto University

Publisher

Oxford University Press (OUP)

Subject

Organic Chemistry,Molecular Biology,Applied Microbiology and Biotechnology,General Medicine,Biochemistry,Analytical Chemistry,Biotechnology

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