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Data set on the antibacterial effects of the hydro-alcoholic extract of Ferula assafoetida plant on Listeria monocytogenes.

ABSTRACT: The aim of the collection of the present dataset is to show the antibacterial effects of the hydro-alcoholic extract of Ferula assafoetida plant on Listeria monocytogenes. Firstly, the Ferula assafoetida herb was collected from investigated hills in Gonabad, Khorasan province, Iran. After botanical and pharmocognosy investigation, the hydro-alcoholic extract of this herb was produced using percolation method. Then, its antimicrobial effects, Minimum Inhibitory Concentration (MIC) and Minimum Bactericidal Concentration (MBC), were investigated using Disc Diffusion Method and Macro Dilution Method vs. Listeria Monocytogenes, serotypes 4a and 4b, respectively. Also, Ampicillin (10?µg/disc) was used as a reference antimicrobial material. The data showed that MIC and MBC of the Ferula assafoetida extract on Listeria monocytogenes was 7.25?µg/ml and 12.50?µg/ml, respectively. Moreover, the average diameter of the inhibitory zone of extracted hydrolcoholic from Ferula Alliacea plant over Listeria monocytogenes 4a and 4b (30?g/ml) were 16.35 2.5 and 15.87 3.1?mm, respectively, and in order for ampicillin was 24.31 2.45 and 24.31 2.45?mm. The hydro-alcoholic extract produced from Ferula assafoetida can be used as the antibacterial for Listeria Monocytogenes.

SUBMITTER: Akhlaghi M

PROVIDER: S-EPMC6129725 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature

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Data set on the antibacterial effects of the hydro-alcoholic extract of Ferula assafoetida plant on Listeria monocytogenes.

Akhlaghi Maliheh M Abbasi Morteza M Safari Yahya Y Amiri Reza R Yoosefpour Nasrin N

Data in brief 20180828

The aim of the collection of the present dataset is to show the antibacterial effects of the hydro-alcoholic extract of Ferula assafoetida plant on Listeria monocytogenes. Firstly, the Ferula assafoetida herb was collected from investigated hills in Gonabad, Khorasan province, Iran. After botanical and pharmocognosy investigation, the hydro-alcoholic extract of this herb was produced using percolation method. Then, its antimicrobial effects, Minimum Inhibitory Concentration ...[more]

PMID: 30211257

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Project description:BACKGROUND: Bacterial penicillin-binding proteins (PBPs) can be visualized by their ability to bind radiolabeled or fluorescent ?-lactam derivatives both whole cells and membrane/cell enriched fractions. Analysis of the Listeria monocytogenes genome sequence predicted ten genes coding for putative PBPs, but not all of their products have been detected in studies using radiolabeled antibiotics, thus hindering their characterization. Here we report the positive identification of the full set of L. monocytogenes PBPs and the characteristics of the hitherto undescribed PBPD2 (Lmo2812). RESULTS: Eight L. monocytogenes PBPs were identified by the binding of fluorescent ?-lactam antibiotic derivatives Boc-FL, Boc-650 and Amp-Alexa430 to proteins in whole cells or membrane/cell wall extracts. The gene encoding a ninth PBP (Lmo2812) was cloned and expressed in Escherichia coli as a His-tagged protein. The affinity purified recombinant protein had DD-carboxypeptidase activity and preferentially degraded low-molecular-weight substrates. L. monocytogenes mutants lacking the functional Lmo2812 enzyme were constructed and, compared to the wild-type, the cells were longer and slightly curved with bent ends.Protein Lmo1855, previously designated PBPD3, did not bind any of the antibiotic derivatives tested, similarly to the homologous enterococcal protein VanY. CONCLUSIONS: Nine out of the ten putative L. monocytogenes PBP genes were shown to encode proteins that bind derivatives of ?-lactam antibiotics, thus enabling their positive identification. PBPD2 (Lmo2812) was not visualized in whole cell extracts, most probably due to its low abundance, but it was shown to bind Boc-FL after recombinant overexpression and purification. Mutants lacking Lmo2812 and another low molecular mass (LMM) PBP, PBP5 (PBPD1)--both with DD-carboxypeptidase activity--displayed only slight morphological alterations, demonstrating that they are dispensable for cell survival and probably participate in the latter stages of peptidoglycan synthesis. Since Lmo2812 preferentially degrades low-molecular- mass substrates, this may indicate a role in cell wall turnover.

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Data set on the antibacterial effects of the hydro-alcoholic extract of Ferula assafoetida plant on Listeria monocytogenes.

Publications

Data set on the antibacterial effects of the hydro-alcoholic extract of <i>Ferula assafoetida</i> plant on <i>Listeria monocytogenes</i>.

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