초록
Lipoteichoic acid (LTA) in the gram-positive bacterial cell wall acts as an immunomodulatory factor in host cells. The chemical structures vary among bacterial species and strains, and may be related to biological activities. In our previous work, much higher immunoglobulin A (IgA)-inducing activity was observed in cells of the Apilactobacillus genus (Apilactobacillus kosoi 10HT, Apilactobacillus apinorum JCM 30765T, and Apilactobacillus kunkeei JCM 16173T) than other lactic acid bacteria, and their LTA was responsible for the activity. In the present study, we elucidated the chemical structures of LTA from these Apilactobacillus strains to explore the structure-function relationship of the IgA-inducing activity. The 1H-nuclear magnetic resonance spectra suggested that their LTA structures were similar. All have a poly-glycerolphosphate main chain, which comprised 12 to 20 average number of the repeating units, with partial substitutions of glucose(α1-, glucosyl(α1-2)glucose(α1- (α-linked-kojibiose), and l-lysine at the C-2 hydroxy group of the glycerol residue. l-Lysine is a substituent never seen before in LTA, and is a probable characteristic of the Apilactobacillus genus. Removal of l-lysine residue from LTA by mild alkaline treatment decreased IgA induction in murine Peyer's patch experiments. The novel l-lysine residue in Apilactobacillus LTA plays a crucial role in the remarkably high IgA-inducing activity.