Journal of Microbiology

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Carbohydrate-binding specificities of potential probiotic Lactobacillus strains in porcine jejunal (IPEC-J2) cells and porcine mucin: Valerie Diane Valeriano , Bernadette B. Bagon , Marilen P. Balolong , Dae-Kyung Kang; J. Microbiol. 2016;54(7):510-519. Published online June 28, 2016; DOI: https://doi.org/10.1007/s12275-016-6168-7

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Bacterial lectins are carbohydrate-binding adhesins that recognize glycoreceptors in the gut mucus and epithelium of hosts. In this study, the contribution of lectin-like activities to adhesion of Lactobacillus mucosae LM1 and Lactobacillus johnsonii PF01, which were isolated from swine intestine, were compared to those of the commercial probiotic Lactobacillus rhamnosus GG. Both LM1 and PF01 strains have been reported to have good adhesion ability to crude intestinal mucus of pigs. To confirm this, we quantified their adhesion to porcine gastric mucin and intestinal porcine enterocytes isolated from the jejunum of piglets (IPEC-J2). In addition, we examined their carbohydrate-binding specificities by suspending bacterial cells in carbohydrate solutions prior to adhesion assays. We found that the selected carbohydrates affected the adherences of LM1 to IPEC-J2 cells and of LGG to mucin. In addition, compared to adhesion to IPEC-J2 cells, adhesion to mucin by both LM1 and LGG was characterized by enhanced specific recognition of glycoreceptor components such as galactose, mannose, and N-acetylglucosamine. Hydrophobic interactions might make a greater contribution to adhesion of PF01. A similar adhesin profile between a probiotic and a pathogen, suggest a correlation between shared pathogen–probiotic glycoreceptor recognition and the ability to exclude enteropathogens such as Escherichia coli K88 and Salmonella Typhimurium KCCM 40253. These findings extend our understanding of the mechanisms of the intestinal adhesion and pathogen-inhibition abilities of probiotic Lactobacillus strains.

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rpoS mutation relieves biosynthesis of flagella in hns mutants of salmonella typhimurium UK1: Cho, Mi Ook , Bang, Ile Soo , Hong, Seong Karp , Bang, Seong Ho , Park, Yong Keun; J. Microbiol. 1998;36(3):184-188.

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Abstract: The biosynthesis and function of flagella is positively regulated by the cyclic AMP-catabolite activator protein (cAMP-CAP) complex and the nucleoid protein H-NS. In this report, we show that nonmotile Salmonella typhimurium hns mutants could recover its motility by introducing the rpoSmutation. In a swarm plate assay, rpoS/hns double mutants could woim while hns mutants could not. This regeneration of motility resulted from the flagella synthesis. Transmission electron microscopy analysis showed the capability of rpoS/hns double mutants for flagella synthesis. And rpoS mutation derepressed the transcription of flhD, the flagella master gene, in hns mutants.

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