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Galectin-2 Agglutinates Helicobacter pylori via Lipopolysaccharide Containing H Type I Under Weakly Acidic Conditions.
Sasaki, Takaharu; Oyama, Midori; Kubota, Mao; Isshiki, Yasunori; Takeuchi, Tomoharu; Tanaka, Toru; Tanikawa, Takashi; Tamura, Mayumi; Arata, Yoichiro; Hatanaka, Tomomi.
Affiliation
  • Sasaki T; Faculty of Pharmacy and Pharmaceutical Sciences, Josai University, 1-1 Keyakidai, Sakado, Saitama 350-0295, Japan.
  • Oyama M; Faculty of Pharmacy and Pharmaceutical Sciences, Josai University, 1-1 Keyakidai, Sakado, Saitama 350-0295, Japan.
  • Kubota M; Faculty of Pharmacy and Pharmaceutical Sciences, Josai University, 1-1 Keyakidai, Sakado, Saitama 350-0295, Japan.
  • Isshiki Y; Faculty of Pharmacy and Pharmaceutical Sciences, Josai University, 1-1 Keyakidai, Sakado, Saitama 350-0295, Japan.
  • Takeuchi T; Faculty of Pharmacy and Pharmaceutical Sciences, Josai University, 1-1 Keyakidai, Sakado, Saitama 350-0295, Japan.
  • Tanaka T; School of Pharmacy, Aichi Gakuin University, 1-100 Kusumoto-cho, Chikusa-ku, Nagoya, Aichi 464-8650, Japan.
  • Tanikawa T; Faculty of Pharmacy and Pharmaceutical Sciences, Josai University, 1-1 Keyakidai, Sakado, Saitama 350-0295, Japan.
  • Tamura M; Faculty of Pharmacy and Pharmaceutical Sciences, Josai University, 1-1 Keyakidai, Sakado, Saitama 350-0295, Japan.
  • Arata Y; Faculty of Pharmaceutical Sciences, Teikyo University, 2-11-1 Kaga, Itabashi-ku, Tokyo 173-8605, Japan.
  • Hatanaka T; Faculty of Pharmaceutical Sciences, Teikyo University, 2-11-1 Kaga, Itabashi-ku, Tokyo 173-8605, Japan.
Int J Mol Sci ; 25(16)2024 Aug 10.
Article de En | MEDLINE | ID: mdl-39201412
ABSTRACT
Galectins are ß-galactoside-binding animal lectins involved in various biological functions, such as host defense. Galectin-2 and -3 are members of the galectin family that are expressed in the stomach, including the gastric mucosa and surface mucous cells. Galectin-3 exhibits aggregation and bactericidal activity against Helicobacter pylori in a ß-galactoside-dependent manner. We previously reported that galectin-2 has the same activity under neutral pH conditions. In this study, the H. pylori aggregation activity of galectin-2 was examined under weakly acidic conditions, in which H. pylori survived. Galectin-2 agglutinated H. pylori even at pH 6.0, but not at pH 5.0, correlating with its structural stability, as determined using circular dichroism. Additionally, galectin-2 binding to the lipopolysaccharide (LPS) of H. pylori cultured under weakly acidic conditions was investigated using affinity chromatography and Western blotting. Galectin-2 could bind to H. pylori LPS containing H type I, a Lewis antigen, in a ß-galactoside-dependent manner. In contrast, galectin-3 was structurally more stable than galectin-2 under acidic conditions and bound to H. pylori LPS containing H type I and Lewis X. In conclusion, galectin-2 and -3 might function cooperatively in the defense against H. pylori in the stomach under different pH conditions.
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Texte intégral: 1 Collection: 01-internacional Base de données: MEDLINE Sujet principal: Lipopolysaccharides / Helicobacter pylori / Galectine 2 Limites: Humans Langue: En Journal: Int J Mol Sci Année: 2024 Type de document: Article Pays d'affiliation: Japon Pays de publication: Suisse

Texte intégral: 1 Collection: 01-internacional Base de données: MEDLINE Sujet principal: Lipopolysaccharides / Helicobacter pylori / Galectine 2 Limites: Humans Langue: En Journal: Int J Mol Sci Année: 2024 Type de document: Article Pays d'affiliation: Japon Pays de publication: Suisse