Complete Genome Sequence of Lactococcus lactis subsp. lactis G50 with Immunostimulating Activity, Isolated from Napier Grass

Nakano, Kazuma; Minami, Maiko; Shinzato, Misuzu; Shimoji, Makiko; Ashimine, Noriko; Shiroma, Akino; Ohki, Shun; Nakanishi, Tetsuhiro; Tamotsu, Hinako; Teruya, Kuniko; Satou, Kazuhito; Moriya, Naoko; Kimoto‐Nira, Hiromi; Kobayashi, Miho; Hagi, Tatsuro; Nomura, Masaru; Suzuki, Chise; Hirano, Takashi

doi:10.1128/genomea.00069-18

Cited by 4 publications

(4 citation statements)

References 16 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Several natural L. lactis isolates have been shown beneficial for health (Mercier-Bonin and Chapot-Chartier, 2017; Nakano et al, 2018). Recombinant L. lactis has also been proposed as a delivery vehicle for therapeutic molecules in the gastrointestinal tract (Carvalho et al, 2017), due to its anti-inflammatory (Nishitani et al, 2009; Bermudez-Humaran et al, 2013; Luerce et al, 2014; Ballal et al, 2015), anti-cancer (Roeffen et al, 2015) and anti-diabetes properties (Freudenberg et al, 2013; Agarwal et al, 2014).…”

Section: Discussionmentioning

confidence: 99%

A Short-Term Feeding of Dietary Casein Increases Abundance of Lactococcus lactis and Upregulates Gene Expression Involving Obesity Prevention in Cecum of Young Rats Compared With Dietary Chicken Protein

Fan

Song

et al. 2019

Front. Microbiol.

View full text Add to dashboard Cite

Casein and chicken are assessed to contain high quality proteins, which are essential for human health. Studies have shown that ingestion of the two dietary proteins resulted in distinct effects on physiology, liver transcriptome and gut microbiota. However, its underlying mechanism is not fully understood, in particular for a crosstalk between gut microbiota and host under a specific diet intervention. We fed young rats with a casein or a chicken protein-based diet (CHPD) for 7 days, and characterized cecal microbiota composition and cecal gene expression. We found that a short-term intervention with a casein-based diet (CAD) induced a higher relative abundance of beneficial bacterium Lactococcus lactis as well as Bifidobacterium pseudolongum, which upregulated galactose metabolism of the microbiome compared with a CHPD. The CAD also upregulated gene expression involved in obesity associated pathways (e.g., Adipoq and Irs1) in cecal tissue of rats. These genes and the bacterial taxon were reported to play an important role in protecting development of obesity. Furthermore, the differentially represented bacterial taxon L. lactis was positively associated with these differentially expressed genes in the gut tissue. Our results provide a new insight into the crosstalk between gut microbiota and host in response to dietary proteins, indicating a potential mechanism of obesity prevention function by casein.

show abstract

Section: Discussionmentioning

confidence: 99%

A Short-Term Feeding of Dietary Casein Increases Abundance of Lactococcus lactis and Upregulates Gene Expression Involving Obesity Prevention in Cecum of Young Rats Compared With Dietary Chicken Protein

Fan

Song

et al. 2019

Front. Microbiol.

View full text Add to dashboard Cite

show abstract

“…Analysis of the G50 genome sequence [ 19 ] may help reveal the cell-surface proteins that contribute to the activity of G50. Here, we detected a cell-surface protein by reaction of L .…”

Section: Introductionmentioning

confidence: 99%

Cell-surface protein YwfG of Lactococcus lactis binds to α-1,2-linked mannose

et al. 2023

Self Cite

View full text Add to dashboard Cite

Lactococcus lactis strains are used as starter cultures in the production of fermented dairy and vegetable foods, but the species also occurs in other niches such as plant material. Lactococcus lactis subsp. lactis G50 (G50) is a plant-derived strain and potential candidate probiotics. Western blotting of cell-wall proteins using antibodies generated against whole G50 cells detected a 120-kDa protein. MALDI-TOF MS analysis identified it as YwfG, a Leu-Pro-any-Thr-Gly cell-wall-anchor-domain–containing protein. Based on a predicted domain structure, a recombinant YwfG variant covering the N-terminal half (aa 28–511) of YwfG (YwfG28−511) was crystallized and the crystal structure was determined. The structure consisted of an L-type lectin domain, a mucin-binding protein domain, and a mucus-binding protein repeat. Recombinant YwfG variants containing combinations of these domains (YwfG28–270, YwfG28–336, YwfG28−511, MubR4) were prepared and their interactions with monosaccharides were examined by isothermal titration calorimetry; the only interaction observed was between YwfG28–270, which contained the L-type lectin domain, and d-mannose. Among four mannobioses, α-1,2-mannobiose had the highest affinity for YwfG28–270 (dissociation constant = 34 μM). YwfG28–270 also interacted with yeast mannoproteins and yeast mannan. Soaking of the crystals of YwfG28–511 with mannose or α-1,2-mannobiose revealed that both sugars bound to the L-type lectin domain in a similar manner, although the presence of the mucin-binding protein domain and the mucus-binding protein repeat within the recombinant protein inhibited the interaction between the L-type lectin domain and mannose residues. Three of the YwfG variants (except MubR4) induced aggregation of yeast cells. Strain G50 also induced aggregation of yeast cells, which was abolished by deletion of ywfG from G50, suggesting that surface YwfG contributes to the interaction with yeast cells. These findings provide new structural and functional insights into the interaction between L. lactis and its ecological niche via binding of the cell-surface protein YwfG with mannose.

show abstract

“…; https://doi.org/10.1101/2022.08. 19.504583 doi: bioRxiv preprint Lactobacilli are known to possess surface-layers (S-layers) proteins [7] that are involved in the adhesion of the cells to the host epithelium or to extracellular matrix components and in the modulating the host immune response [3]. For example, knockout of the S-layer protein A in Lactobacillus acidophilus significantly reduces binding of the mutant to DC-SIGN, a dendritic cell (DC)-specific receptor, and the S-layer protein A is involved in the modulation of DC and T-cell functions [8].…”

Section: Introductionmentioning

confidence: 99%

“…Analysis of the G50 genome sequence [19] may help reveal the cell-surface proteins that contribute to the activity of G50. Here, we detected a cell-surface protein by reaction of L. lactis strains with anti-G50 antibody.…”

Section: Introductionmentioning

confidence: 99%

Cell-surface protein YwfG ofLactococcus lactisbinds to α-1,2-linked mannose

Tsuchiya

Fujimoto

Inagaki

et al. 2022

Preprint

Self Cite

View full text Add to dashboard Cite

Lactococcus lactis strains are used as starter cultures in the production of fermented dairy and vegetable foods, but the species also occurs in other niches such as plant material. Lactococcus lactis subsp. lactis G50 (G50) is a plant-derived strain and potential candidate probiotics. Western blotting of cell-surface proteins using antibodies generated against whole G50 cells identified a 120-kDa protein. MALDI-TOF MS analysis identified it as YwfG, a Leu-Pro-any-Thr-Gly cell wall anchor domain–containing protein. Based on a predicted structure, a recombinant protein covering the N-terminal half (aa 28–511) of YwfG (YwfG28−511) was crystallized and the crystal structure was determined. The structure consisted of an L-type lectin domain, a mucin-binding protein domain, and a mucus-binding protein repeat. Recombinant proteins containing combinations of these domains were prepared and their interactions with monosaccharides were examined by isothermal titration calorimetry; the only interaction observed was between the L-type lectin domain and D-mannose. Among four mannobioses, α1,2-mannobiose had the highest affinity for the L-type lectin domain (dissociation constant = 34 μM). The L-type lectin domain also interacted with yeast mannoproteins and yeast cells. Soaking of the crystals of YwfG28−511 with mannose or α1,2-mannobiose revealed that both sugars bound to the L-type lectin domain in a similar manner, although the presence of the mucin-binding protein domain and the mucus-binding protein repeat within the recombinant protein inhibited the interaction between the L-type lectin domain and mannose. These findings provide new structural and functional insights into the interaction between L. lactis and its ecological niche via binding of the cell-surface protein YwfG with mannose.

show abstract

Complete Genome Sequence of Lactococcus lactis subsp. lactis G50 with Immunostimulating Activity, Isolated from Napier Grass

Cited by 4 publications

References 16 publications

A Short-Term Feeding of Dietary Casein Increases Abundance of Lactococcus lactis and Upregulates Gene Expression Involving Obesity Prevention in Cecum of Young Rats Compared With Dietary Chicken Protein

A Short-Term Feeding of Dietary Casein Increases Abundance of Lactococcus lactis and Upregulates Gene Expression Involving Obesity Prevention in Cecum of Young Rats Compared With Dietary Chicken Protein

Cell-surface protein YwfG of Lactococcus lactis binds to α-1,2-linked mannose

Cell-surface protein YwfG ofLactococcus lactisbinds to α-1,2-linked mannose

Contact Info

Product

Resources

About