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Purification and Characterization of Bacteriocin Produced by Weissella confusa A3 of Dairy Origin.

Goh HF, Philip K - PLoS ONE (2015)

Bottom Line: Reduction of activity was shown after treatment with proteinase K, trypsin and peptidase that confirmed the proteinaceous nature of the compound.Bacterial cell treated with the bacteriocin also showed significant morphological changes under transmission electron microscope.No virulence and disease related genes can be detected from the genome of the strain.

View Article: PubMed Central - PubMed

Affiliation: Microbiology Division, Institute of Biological Sciences, Faculty of Science, University of Malaya, 50603, Kuala Lumpur, Malaysia.

ABSTRACT
A dramatic increase in bacterial resistance towards currently available antibiotics has raised worldwide concerns for public health. Therefore, antimicrobial peptides (AMPs) have emerged as a promisingly new group of therapeutic agents for managing infectious diseases. The present investigation focusses on the isolation and purification of a novel bacteriocin from an indigenous sample of cow milk and it's mode of action. The bacteriocin was isolated from Weissella confusa A3 that was isolated from the sample and was shown to have inhibitory activity towards pathogenic bacteria namely Bacillus cereus, Escherichia coli, Pseudomonas aeruginosa and Micrococcus luteus. The bacteriocin was shown to be heat stable and functioned well at low pH (2 to 6). Reduction of activity was shown after treatment with proteinase K, trypsin and peptidase that confirmed the proteinaceous nature of the compound. MALDI-TOF analysis of the sample gave a mass approximating 2.7 kDa. The membrane of the bacteria was disrupted by the bacteriocin causing SYTOX® green dye to enter the cell and bind to the bacterial DNA giving fluorescence signal. Bacterial cell treated with the bacteriocin also showed significant morphological changes under transmission electron microscope. No virulence and disease related genes can be detected from the genome of the strain.

No MeSH data available.


Related in: MedlinePlus

Subsystem feature of the genome sequence of W. confusa A3 analysed with RAST server.The red box indicated absence of genes in toxins and superantigens and virulence, disease and defense genes.
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pone.0140434.g008: Subsystem feature of the genome sequence of W. confusa A3 analysed with RAST server.The red box indicated absence of genes in toxins and superantigens and virulence, disease and defense genes.

Mentions: The bacteria genome was analyzed with RAST server for virulence, disease and defense subsystems. It was conclusively observed that the W. confusa strain used in our study did not harbour any genes related to toxins and production of superantigens. Virulence, disease and defense genes were also not detected from the genome of the bacteria (Fig 8). For gene encoding bacteriocin production, possible colicin V production protein was detected from the genome. The gene encoding possible colicin V production was translated into amino acid sequence and searched with UniProt (http://www.uniprot.org/blast/) showing the amino acid sequence to be 100% identical to colicin V from W. confusa LBAE C39-2. It can therefore be established that the bacteria is safe for use in the food industry.


Purification and Characterization of Bacteriocin Produced by Weissella confusa A3 of Dairy Origin.

Goh HF, Philip K - PLoS ONE (2015)

Subsystem feature of the genome sequence of W. confusa A3 analysed with RAST server.The red box indicated absence of genes in toxins and superantigens and virulence, disease and defense genes.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4608715&req=5

pone.0140434.g008: Subsystem feature of the genome sequence of W. confusa A3 analysed with RAST server.The red box indicated absence of genes in toxins and superantigens and virulence, disease and defense genes.
Mentions: The bacteria genome was analyzed with RAST server for virulence, disease and defense subsystems. It was conclusively observed that the W. confusa strain used in our study did not harbour any genes related to toxins and production of superantigens. Virulence, disease and defense genes were also not detected from the genome of the bacteria (Fig 8). For gene encoding bacteriocin production, possible colicin V production protein was detected from the genome. The gene encoding possible colicin V production was translated into amino acid sequence and searched with UniProt (http://www.uniprot.org/blast/) showing the amino acid sequence to be 100% identical to colicin V from W. confusa LBAE C39-2. It can therefore be established that the bacteria is safe for use in the food industry.

Bottom Line: Reduction of activity was shown after treatment with proteinase K, trypsin and peptidase that confirmed the proteinaceous nature of the compound.Bacterial cell treated with the bacteriocin also showed significant morphological changes under transmission electron microscope.No virulence and disease related genes can be detected from the genome of the strain.

View Article: PubMed Central - PubMed

Affiliation: Microbiology Division, Institute of Biological Sciences, Faculty of Science, University of Malaya, 50603, Kuala Lumpur, Malaysia.

ABSTRACT
A dramatic increase in bacterial resistance towards currently available antibiotics has raised worldwide concerns for public health. Therefore, antimicrobial peptides (AMPs) have emerged as a promisingly new group of therapeutic agents for managing infectious diseases. The present investigation focusses on the isolation and purification of a novel bacteriocin from an indigenous sample of cow milk and it's mode of action. The bacteriocin was isolated from Weissella confusa A3 that was isolated from the sample and was shown to have inhibitory activity towards pathogenic bacteria namely Bacillus cereus, Escherichia coli, Pseudomonas aeruginosa and Micrococcus luteus. The bacteriocin was shown to be heat stable and functioned well at low pH (2 to 6). Reduction of activity was shown after treatment with proteinase K, trypsin and peptidase that confirmed the proteinaceous nature of the compound. MALDI-TOF analysis of the sample gave a mass approximating 2.7 kDa. The membrane of the bacteria was disrupted by the bacteriocin causing SYTOX® green dye to enter the cell and bind to the bacterial DNA giving fluorescence signal. Bacterial cell treated with the bacteriocin also showed significant morphological changes under transmission electron microscope. No virulence and disease related genes can be detected from the genome of the strain.

No MeSH data available.


Related in: MedlinePlus