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Yasushi Kawai,
Joni Kusnadi,
Rober Kemperman,
Jan Kok,
Yoshiyuki Ito,
Mikiko Endo,
Kensuke Arakawa, Hideaki Uchida,
Junko Nishimura,
Haruki Kitazawa,
Tadao Saito
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ABSTRACT: Gassericin A, produced by Lactobacillus gasseri LA39, is a hydrophobic circular bacteriocin. The DNA region surrounding the gassericin A structural gene, gaaA, was sequenced, and seven open reading frames (ORFs) of 3.5 kbp (gaaBCADITE) were found with possible functions in gassericin A production, secretion, and immunity. The deduced products of the five consecutive ORFs gaaADITE have homology to those of genes involved in butyrivibriocin AR10 production, although the genetic arrangements are different in the two circular bacteriocin genes. GaaI is a small, positively charged hydrophobic peptide of 53 amino acids containing a putative transmembrane segment. Heterologous expression and homologous expression of GaaI in Lactococcus lactis subsp. cremoris MG1363 and L. gasseri JCM1131(T), respectively, were studied. GaaI-expressing strains exhibited at least sevenfold-higher resistance to gassericin A than corresponding control strains, indicating that gaaI encodes an immunity peptide for gassericin A. Comparison of GaaI to peptides with similar characteristics found in the circular bacteriocin gene loci is discussed.
Applied and environmental microbiology 01/2009; 75(5):1324-30. · 3.69 Impact Factor
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Hideaki Uchida,
Yasushi Kawai,
Hideki Kinoshita,
Haruki Kitazawa,
Koh Miura,
Kenichi Shiiba,
Akira Horii,
Katsunori Kimura,
Naoki Taketomo,
Munehiro Oda,
Takaji Yajima,
Tadao Saito
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ABSTRACT: Twenty lactobacilli isolated from human feces were studied for binding to the human blood type B-antigen [Galalpha1-3 (Fucalpha1-2) Gal-] and H-antigen (Fucalpha1-2Gal-] expressed sugar chains in human intestinal mucosa. We found two strains, L. gasseri OLL2755 and L. gasseri OLL2877 that firmly adhere to human B-antigen, and we found L. gasseri OLL2827 bound to the H-antigen.
Bioscience Biotechnology and Biochemistry 01/2007; 70(12):3073-6. · 1.28 Impact Factor
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Hideaki Uchida,
Hideki Kinoshita,
Yasushi Kawai,
Haruki Kitazawa,
Koh Miura,
Kenichi Shiiba,
Akira Horii,
Katsunori Kimura,
Naoki Taketomo,
Munehiro Oda,
Takaji Yajima,
Tadao Saito
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ABSTRACT: Adherent lactic acid bacteria (LAB) in the human intestine were investigated using the surface plasmon resonance technique with the biosensor BIACORE-1000. Ninety-three LAB strains were isolated from human feces and evaluated for binding to human blood type-A antigen [GalNAcalpha1-3 (Fucalpha1-2) Gal-: A-trisaccharide] expressed in the intestinal mucosa. Eleven strains showed strong adherence to an A-trisaccharide biotinyl polymer (BP) probe, and slightly or no adherence to a B-trisaccharide BP probe. Four strains with high adherence (high A/B ratio) were selected and their surface layer proteins (SLPs) were evaluated for A-antigen ligand binding using BIACORE. The SLP from L. brevis strain OLL2772 showed a single band at ca. 48 kDa by SDS-PAGE analysis and it had a very strong adherence to the human A-antigen, as shown using an anti-A lectin blocking technique. A partial N-terminal sequence of the band showed strong homology to an S-layer protein of L. brevis ATCC8287T. The probiotic LAB binds to human blood type-A antigen expressed in the intestinal mucosa which may aid in colonization of the gut.
Research in Microbiology 10/2006; 157(7):659-65. · 2.76 Impact Factor
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ABSTRACT: A new binding assay to investigate the mechanism of adhesion of lactic acid bacteria to the human intestine was established by the surface plasmon resonance technique using a biosensor BIACORE1000. Cells of 26 strains of the Lactobacillus acidophilus group as analytes were eluted onto a sensor chip on which were immobilized biotinylated A-trisaccharide polymer probes having human A-type antigen [(GalNAcalpha1-3(Fucalpha1-2)Gal)-] or human colonic mucin of blood type A (HCM-A) as ligands. In the first screening, high adhesive affinity to the A-trisaccharide BP-probe was observed in L. acidophilus OLL2769, L. crispatus JCM8778, LA205 and LA206. In the second screening, which used HCM-A, only L. acidophilus OLL2769 and L. crispatus JCM8778 were selected as adhesive strains with specific binding ability to human A-antigen. The results indicated that some strains of the L. acidophilus group could recognize and bind the sugar chain of A-antigen structure on HCM.
Bioscience Biotechnology and Biochemistry 06/2004; 68(5):1004-10. · 1.28 Impact Factor
