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RISS 인기검색어
- 검색키워드
- 저자 : Valerie Diane Valeriano (검색결과 5 건)
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Valeriano, Valerie Diane V.,Oh, Ju Kyoung,Bagon, Bernadette B.,Kim, Heebal,Kang, Dae-Kyung Elsevier 2019 Genomics Vol.111 No.1
<P><B>Abstract</B></P> <P> <I>Lactobacillus mucosae</I> is currently of interest as putative probiotics due to their metabolic capabilities and ability to colonize host mucosal niches. <I>L. mucosae</I> LM1 has been studied in its functions in cell adhesion and pathogen inhibition, <I>etc.</I> It demonstrated unique abilities to use energy from carbohydrate and non-carbohydrate sources. Due to these functions, we report the first complete genome sequence of an <I>L. mucosae</I> strain, <I>L</I>. <I>mucosae</I> LM1. Analysis of the pan-genome in comparison with closely-related <I>Lactobacillus</I> species identified a complete glycogen metabolism pathway, as well as folate biosynthesis, complementing previous proteomic data on the LM1 strain. It also revealed common and unique niche-adaptation genes among the various <I>L. mucosae</I> strains. The aim of this study was to derive genomic information that would reveal the probable mechanisms underlying the probiotic effect of <I>L. mucosae</I> LM1, and provide a better understanding of the nature of <I>L. mucosae</I> sp.</P> <P><B>Highlights</B></P> <P> <UL> <LI> Comparative analysis of the complete genome of <I>L. mucosae</I> LM1 with those of other <I>L. mucosae</I> strains was performed. </LI> <LI> It identified complete glycogen metabolism and folate biosynthesis pathway, complementing previous proteomic data on LM1. </LI> <LI> It also revealed common and unique niche-adaptation genes among the various <I>L. mucosae</I> strains. </LI> </UL> </P>
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Valerie Diane Valeriano,BAGON BERNADETTE,Marilen P. Balolong,Dae-Kyung Kang 한국미생물학회 2016 The journal of microbiology Vol.54 No.7
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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Pajarillo, Edward Alain B.,Kim, Sang Hoon,Lee, Ji-Yoon,Valeriano, Valerie Diane V.,Kang, Dae-Kyung Korean Society for Food Science of Animal Resource 2015 한국축산식품학회지 Vol.35 No.5
Lactobacillus mucosae is a natural resident of the gastrointestinal tract of humans and animals and a potential probiotic bacterium. To understand the global protein expression profile and metabolic features of L. mucosae LM1 in the early stationary phase, the QExactive<sup>TM</sup> Hybrid Quadrupole-Orbitrap Mass Spectrometer was used. Characterization of the intracellular proteome identified 842 proteins, accounting for approximately 35% of the 2,404 protein-coding sequences in the complete genome of L. mucosae LM1. Proteome quantification using QExactive<sup>TM</sup> Orbitrap MS detected 19 highly abundant proteins (> 1.0% of the intracellular proteome), including CysK (cysteine synthase, 5.41%) and EF-Tu (elongation factor Tu, 4.91%), which are involved in cell survival against environmental stresses. Metabolic pathway annotation of LM1 proteome using the Kyoto Encyclopedia of Genes and Genomes (KEGG) database showed that half of the proteins expressed are important for basic metabolic and biosynthetic processes, and the other half might be structurally important or involved in basic cellular processes. In addition, glycogen biosynthesis was activated in the early stationary phase, which is important for energy storage and maintenance. The proteogenomic data presented in this study provide a suitable reference to understand the protein expression pattern of lactobacilli in standard conditions
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Edward Alain B. Pajarillo,Sang Hoon Kim,Ji-yoon Lee,Valerie Diane V. Valeriano,Dae-kyung Kang 한국축산식품학회 2015 한국축산식품학회지 Vol.35 No.5
Lactobacillus mucosae is a natural resident of the gastrointestinal tract of humans and animals and a potential probiotic bacterium. To understand the global protein expression profile and metabolic features of L. mucosae LM1 in the early stationary phase, the QExactive ™ Hybrid Quadrupole-Orbitrap Mass Spectrometer was used. Characterization of the intracellular proteome identified 842 proteins, accounting for approximately 35% of the 2,404 protein-coding sequences in the complete genome of L. mucosae LM1. Proteome quantification using QExactive™ Orbitrap MS detected 19 highly abundant proteins (> 1.0% of the intracellular proteome), including CysK (cysteine synthase, 5.41%) and EF-Tu (elongation factor Tu, 4.91%), which are involved in cell survival against environmental stresses. Metabolic pathway annotation of LM1 proteome using the Kyoto Encyclopedia of Genes and Genomes (KEGG) database showed that half of the proteins expressed are important for basic metabolic and biosynthetic processes, and the other half might be structurally important or involved in basic cellular processes. In addition, glycogen biosynthesis was activated in the early stationary phase, which is important for energy storage and maintenance. The proteogenomic data presented in this study provide a suitable reference to understand the protein expression pattern of lactobacilli in standard conditions.
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