Draft Genome Sequences of Lactococcus lactis Strains MS22314, MS22333, MS22336, and MS22337, Isolated from Fermented Camel Milk in Ethiopia

Bragason, Esben; Svendsen, Christina Aaby; Guya, Mitiku Eshetu; Berhe, Tesfemariam; Hansen, Egon Bech

doi:10.1128/mra.00862-20

Cited by 4 publications

(4 citation statements)

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“…It was recently demonstrated that proteolysis is the bottleneck for acidification of camel milk with commercially available dairy starter cultures ( Berhe et al, 2018 ). LAB strains able to acidify camel milk have been isolated ( Abdelgadir et al, 2008 ; Drici, 2008 ; Drici et al, 2010 ; Gabed et al, 2015 ; Fugl et al, 2017 ) and several of these have been genome sequenced ( Drici, 2008 ; Gabed et al, 2015 ; Bragason et al, 2020 ).…”

Section: Introductionmentioning

confidence: 99%

Modeled Structure of the Cell Envelope Proteinase of Lactococcus lactis

Hansen

Marcatili

2020

Front. Bioeng. Biotechnol.

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The cell envelope proteinase (CEP) of Lactococcus lactis is a large extracellular protease covalently linked to the peptidoglycan of the cell wall. Strains of L. lactis are typically auxotrophic for several amino acids and in order to grow to high cell densities in milk they need an extracellular protease. The structure of the entire CEP enzyme is difficult to determine experimentally due to the large size and due to the attachment to the cell surface. We here describe the use of a combination of structure prediction tools to create a structural model for the entire CEP enzyme of Lactococcus lactis. The model has implications for how the bacterium interacts with casein micelles during growth in milk, and it has implications regarding the energetics of the proteolytic system. Our model for the CEP indicates that the catalytic triad is activated through a structural change caused by interaction with the substrate. The CEP of L. lactis might become a useful model for the mode of action for enzymes belonging to the large class of S8 proteinases with a PA (protease associated) domain and a downstream fibronectin like domain.

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Section: Introductionmentioning

confidence: 99%

Modeled Structure of the Cell Envelope Proteinase of Lactococcus lactis

Hansen

Marcatili

2020

Front. Bioeng. Biotechnol.

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“…We have previously published the genome sequences of L. lactis MS22314, MS22333, MS22336 and MS22337 (Bragason et al, 2020), where annotation of the contigs showed that MS22333 were the only strain without any genes coding for antibiotic resistance. Starter cultures containing resistance genes can possibly be a critical source of spreading antibiotic resistance, and studies have found multiple starter cultures with resistance genes (Kastner et al, 2006;Katla, Kruse, Johnsen, & Herikstad, 2001).…”

Section: Discussionmentioning

confidence: 99%

“…Originally, the strains MS22314, MS22333, MS22336 and MS22337 were isolated from spontaneous fermented camel milk in Ethiopia (Fugl et al, 2017). Genome sequences of the strains can be accessed at the Genbank under BioSample numbers: SAMN13701540, SAMN13701541, 76 SAMN13701542, SAMN13701543 (Bragason, Svendsen, Guya, Berhe, & Hansen, 2020). The cultures were grown for 24 h at 30 °C in M17 broth (Oxoid, Thermo Scientific, Hampshire, UK) containing 0.5% lactose.…”

Section: Bacterial Strainsmentioning

confidence: 99%

Antimicrobial activity of novel Lactococcus lactis strains against Salmonella Typhimurium DT12, Escherichia coli O157:H7 VT− and Klebsiella pneumoniae in raw and pasteurised camel milk

Bragason

Berhe

Dashe

et al. 2020

International Dairy Journal

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The present study investigated inhibition of multiple food related pathogens in raw and pasteurised camel milk during fermentation with four novel Lactococcus lactis strains. All pathogens alone in camel milk reached 8.0 log(CFU mL -1 ). When the pathogens were cultivated with L. lactis MS22333 or MS22337 they were reduced between 0.9-6.0 log(CFU mL -1 ). L. lactis MS22314 and MS22336 showed no antimicrobial activity.Bad hygiene and lack of cooling facilities have resulted in spontaneously fermented African camel milk with high incidence of contaminants. Starter cultures promote food safety by controlling the fermentation. Commercial cultures developed for bovine milk acidify poorly in camel milk and cultures optimized for camel milk with inhibitory effects against pathogens are therefore needed.To our knowledge, we have for the first time demonstrated that some L. lactis strains isolated from camel milk can inhibit the growth of food related pathogens in both raw and pasteurised camel milk.

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“…It was recently demonstrated that proteolysis is the bottleneck for acidification of camel milk with commercially available dairy starter cultures (Berhe et al, 2018). LAB strains able to acidify camel milk have been isolated (Abdelgadir et al, 2008;Drici, 2008;Drici et al, 2010;Gabed et al, 2015;Fugl et al, 2017) and several of these have been genome sequenced (Drici, 2008;Gabed et al, 2015;Bragason et al, 2020).…”

Section: Introductionmentioning

confidence: 99%

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Draft Genome Sequences of Lactococcus lactis Strains MS22314, MS22333, MS22336, and MS22337, Isolated from Fermented Camel Milk in Ethiopia

Abstract: The genome sequences of four Lactococcus lactis strains isolated from fermented camel milk were sequenced using paired-end Illumina MiSeq reads. The genome size of each strain was about 2.6 Mb, and three of the strains were annotated with tet(S) coding for tetracycline resistance.

Cited by 4 publications

References 10 publications

Modeled Structure of the Cell Envelope Proteinase of Lactococcus lactis

Modeled Structure of the Cell Envelope Proteinase of Lactococcus lactis

Antimicrobial activity of novel Lactococcus lactis strains against Salmonella Typhimurium DT12, Escherichia coli O157:H7 VT− and Klebsiella pneumoniae in raw and pasteurised camel milk

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