Functional role of surface layer proteins of<i> Lactobacillus acidophilus</i> L-92 in stress tolerance and binding to host cell proteins
-
- WAKAI Taketo
- Core Technology Laboratories, Asahi Quality and Innovations, Ltd., 5-11-10 Fuchinobe, Chuo-ku, Sagamihara-shi, Kanagawa, Japan
-
- KANO Chie
- Core Technology Laboratories, Asahi Quality and Innovations, Ltd., 5-11-10 Fuchinobe, Chuo-ku, Sagamihara-shi, Kanagawa, Japan
-
- KARSENS Harma
- Department of Molecular Genetics, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Linnaeusborg, Nijenborgh 7, Groningen, The Netherlands
-
- KOK Jan
- Department of Molecular Genetics, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Linnaeusborg, Nijenborgh 7, Groningen, The Netherlands
-
- YAMAMOTO Naoyuki
- School of Life Science and Technology, Tokyo Institute of Technology, 4259 Nagatsuta-cho, Midori-ku, Yokohama-shi, Kanagawa, Japan
この論文をさがす
抄録
<p>Lactobacillus acidophilus surface layer proteins (SLPs) self-assemble into a monolayer that is non-covalently bound to the outer surface of the cells. There they are in direct contact with the environment, environmental stressors and gut components of the host in which the organism resides. The role of L. acidophilus SLPs is not entirely understood, although SLPs seem to be essential for bacterial growth. We constructed three L. acidophilus L-92 strains, each expressing a mutant of the most abundant SLP, SlpA. Each carried a 12-amino acid c-myc epitope substitution at a different position in the protein. A strain was also obtained that expressed the SlpA paralog SlpB from an originally silent slpB gene. All four strains behaved differently with respect to growth under various stress conditions, such as the presence of salt, ox gall or ethanol, suggesting that SlpA affects stress tolerance in L. acidophilus L-92. Also, the four mutants showed differential in vitro binding ability to human host cell proteins such as uromodulin or dendritic cell (DC)-specific intercellular adhesion molecule-3 grabbing non-integrin (DC-SIGN). Furthermore, co-culture of murine immature DCs with a mutant strain expressing one of the recombinant SlpA proteins changed the concentrations of the cytokines IL-10 and IL-12. Our data suggest that SlpA and SlpB of L. acidophilus participate in bacterial stress tolerance and binding to uromodulin or DC-SIGN, possibly leading to effective immune-modification.</p>
収録刊行物
-
- Bioscience of Microbiota, Food and Health
-
Bioscience of Microbiota, Food and Health 40 (1), 33-42, 2021
BMFH出版会
- Tweet
キーワード
詳細情報 詳細情報について
-
- CRID
- 1391694356257937920
-
- NII論文ID
- 130007966543
-
- ISSN
- 21863342
-
- 本文言語コード
- en
-
- データソース種別
-
- JaLC
- Crossref
- CiNii Articles
-
- 抄録ライセンスフラグ
- 使用不可