Manganese privation induced transcriptional upregulation of the class IIa bacteriocin plantaricin 423 in Lactobacillus plantarum 423

Author(s):  
Ross Vermeulen ◽  
Shelly Deane ◽  
Leon Dicks ◽  
Johann Rohwer ◽  
Anton Du Preez van Staden

Plantaricin 423 is produced by Lactobacillus plantarum 423 using the pla biosynthetic operon located on the 8188 bp plasmid, pPLA4. As with many class IIa bacteriocin operons, the pla operon encodes biosynthetic genes ( plaA : precursor peptide, plaB : immunity, plaC : accessory and plaD : ABC transporter) but does not encode local regulatory genes. Little is known about the regulatory mechanisms involved in the expression of the apparently regulationless class IIa bacteriocins such as plantaricin 423. In this study, phylogenetic analysis of class IIa immunity proteins indicated that at least three distinct clades exist, which were then used to subgroup the class IIa operons. It became evident that the absence of classical quorum sensing genes on mobile bacteriocin encoding elements is a predisposition of the subgroup which includes plantaricin 423, pediocin AcH/PA-1, divercin V41, enterocin A, leucocin-A and -B, mesentericin Y105 and sakacin G. Further analysis of the subgroup suggested that the regulation of these class IIa operons may be linked to transition metal homeostasis in the host. By using a fluorescent promoter-reporter system in Lactobacillus plantarum 423, transcriptional regulation of plantaricin 423 was shown to be upregulated in response to manganese privation. IMPORTANCE Lactic acid bacteria hold huge industrial application and economic value, especially bacteriocinogenic strains which further aids in the exclusion of specific foodborne pathogens. Since bacteriocinogenic strains are sought after it is equally important to understand the mechanism of bacteriocin regulation. This is currently an understudied aspect of class IIa operons. Our research suggests the existence of a previously undescribed mode of class IIa bacteriocin regulation, whereby bacteriocin expression is linked to management of the producer’s transition metal homeostasis. This delocalized metalloregulatory model may fundamentally affect the selection of culture conditions for bacteriocin expression and change our understanding of class IIa bacteriocin gene transfer dynamics in a given microbiome.

Author(s):  
Andrew G. Turner ◽  
Cheryl-lynn Y. Ong ◽  
Mark J. Walker ◽  
Karrera Y. Djoko ◽  
Alastair G. McEwan

2012 ◽  
Vol 518-523 ◽  
pp. 5468-5471
Author(s):  
Shi Ru Jia ◽  
Zhen Ding ◽  
Ning Tan ◽  
Nan Wang ◽  
Pei Pei Han ◽  
...  

Nostoc flagelliforme is a kind of terrestrial cyanobacterium with high economic value. Dissociated cells, which separated from a natural colony of N. flagelliforme, could be cultivated heterotrophically in the darkness on xylose and glucose under fed-batch culture conditions. Growth and extracellular polysaccharides (EPS) production in different cultures are investigated. At harvest time, the cultures contain 1.215 g•L-1 of biomass and 122.5 mg•L-1 of EPS respectively. The gravimetric EPS production rate is 17.5 mg•g-1•day-1, which is 1.65 times higher than previously reported results for heterotrophic Nostoc flagelliforme grown on xylose batch culture.


2017 ◽  
Vol 37 ◽  
pp. 26-32 ◽  
Author(s):  
Claire M. Weekley ◽  
Chuan He

2009 ◽  
Vol 12 (3) ◽  
pp. 347-357 ◽  
Author(s):  
Marinus Pilon ◽  
Christopher M Cohu ◽  
Karl Ravet ◽  
Salah E Abdel-Ghany ◽  
Frederic Gaymard

EcoSal Plus ◽  
2009 ◽  
Vol 3 (2) ◽  
Author(s):  
Dietrich H. Nies ◽  
Gregor Grass

2020 ◽  
Author(s):  
Rosario Castro-Rodríguez ◽  
María Reguera ◽  
Viviana Escudero ◽  
Patricia Gil-Díez ◽  
Julia Quintana ◽  
...  

ABSTRACTYellow Stripe-Like (YSL) proteins are a family of plant transporters typically involved in transition metal homeostasis. The substrate of three of the four YSL clades (clades I, II, and IV) are metal complexes with non-proteinogenic amino acid nicotianamine or its derivatives. No such transport capabilities have been shown for any member of the remaining clade (clade III), which is able to translocate short peptides across the membranes instead. The connection between clade III YSL members and metal homeostasis might have been masked by the functional redundancy characteristic of this family. This might have been circumvented in legumes through neofunctionalization of YSLs to ensure a steady supply of transition metals for symbiotic nitrogen fixation in root nodules. To test this possibility, Medicago truncatula clade III transporter MtYSL7 has been studied both when the plant was fertilized with ammonium nitrate or when nitrogen had to be provided by endosymbiotic rhizobia within the root nodules. MtYSL7 is a plasma membrane protein expressed in the vasculature and in the nodule cortex. This protein is able to transport short peptides into the cytosol, although none with known metal homeostasis roles. Reducing MtYSL7 expression levels resulted in diminished nitrogen fixation rates. In addition, nodules of mutant lines lacking YSL7 accumulated more copper and iron, the later the likely result of increased expression in roots of iron uptake and delivery genes. The available data is indicative of a role of MtYSL7, and likely other clade III YSLs, in transition metal homeostasis.ONE SENTENCE SUMMARYMedicago truncatula YSL7 is a peptide transporter required for symbiotic nitrogen fixation in legume nodules, likely controlling transition metal allocation to these organs.


2020 ◽  
Vol 2020 ◽  
pp. 1-17
Author(s):  
Mahreen Ul Hassan ◽  
Hina Nayab ◽  
Farheen Shafique ◽  
Mike P. Williamson ◽  
Taghreed Saud Almansouri ◽  
...  

Probiotic bacteria are of utmost importance owing to their extensive utilisation in dairy products and in the prevention of various intestinal diseases. The objective of this study was to assess the probiotic properties of bacteriocin-producing isolates of Lactobacillus helveticus and Lactobacillus plantarum isolated from traditional Pakistani yoghurt. In this study, ten bacteriocin-producing isolates were selected to screen for the probiotic property. The isolates showed resistance to acidic pH (6-6.5), bile salt (0.01-1%), and 1-7% NaCl salt and showed good growth at acidic pH and antibacterial activity against ten different foodborne pathogens. Interestingly, these isolates were proved to be effective against Actinobacter baumannii but least effective against Klebsiella pneumoniae and Pseudomonas aeruginosa. A few isolates were found to be resistant to some antibiotics like vancomycim, gentamycin, erythromycin, streptomycin, and clindamycin. Our results provide strong evidence in favour of traditional Pakistani yoghurts as a potential source of bacteriocin-producing bacteria with an added benefit of the probiotic property. Specifically, LBh5 was considered a good probiotic isolate as compared to other isolates used in the study. Further extensive research should be done on isolation and characterisation of probiotic isolates from local fermented foods, and then, these isolates should be used in the development of probiotic enriched food supplements in Pakistan.


2020 ◽  
Vol 16 ◽  
Author(s):  
Mohanasrinivasan V. ◽  
Mounika Ranga ◽  
Jannatul Firdous Siddique ◽  
Nivetha Anbalagan ◽  
Subathradevi C.

Abstract:: Bacteriocins are antimicrobial peptides synthesized ribosomally which can be used as bio-preservative reducing the risk of chemical preservative’s effect and also replacing the thermal treatments. This study aims to isolate, purify the an-tibacterial protein from Lactobacillus plantarum KY449289 and to assess its bio preservative potential. In this study, twenty strains were isolated from a yogurt sample and preliminary characterization was carried out, such as morphological, bio-chemical, and molecular levels as a preliminary assay. The characterized strains were assessed for the antibacterial activity by well diffusion assay, whereas all twenty strains were shown to have a antibacterial activity against foodborne pathogens, among which two strains VITMM04 and VITMM05 shows the highest zone of inhibition of 15 mm and 10 mm respectively against Listeria monocytogenes. The potent isolate VITMM05 solely showed a broad spectrum antibacterial activity against the pathogens. These strains were further subjected to optimization, purification, and application studies. A high increase in the inhibition zone was recorded with an optimum temperature of 35°C and its activity was found to be stable up to 85°C, optimum pH 6, and 5 mM of EDTA as an enhancer surfactant. On subjected to RP-HPLC, the purified sample showed a dis-tinct peak at 2.192 min corresponding to the peak at 2.192 min for standard bacteriocin The six-fold purified bacteriocin was effective in controlling 87% of the microbial population with 20mm zone of inhibiton against the Listeria monocytogenes and this shows the effective role of purified bacteriocin in inhibiting bacterial growth in a greater extent.


2021 ◽  
pp. 159-178
Author(s):  
Yamshi Arif ◽  
Priyanka Singh ◽  
Husna Siddiqui ◽  
Romana Naaz ◽  
Shamsul Hayat

Microbiology ◽  
2004 ◽  
Vol 150 (8) ◽  
pp. 2663-2668 ◽  
Author(s):  
Manilduth Ramnath ◽  
Safia Arous ◽  
Anne Gravesen ◽  
John W. Hastings ◽  
Yann Héchard

Sensitivity to class IIa bacteriocins from lactic acid bacteria was recently associated with the mannose phosphotransferase system (PTS) permease, , in Listeria monocytogenes. To assess the involvement of this protein complex in class IIa bacteriocin activity, the mptACD operon, encoding , was heterologously expressed in an insensitive species, namely Lactococcus lactis, using the NICE double plasmid system. Upon induction of the cloned operon, the recombinant Lc. lactis became sensitive to leucocin A. Pediocin PA-1 and enterocin A also showed inhibitory activity against Lc. lactis cultures expressing mptACD. Furthermore, the role of the three genes of the mptACD operon was investigated. Derivative plasmids containing various combinations of these three genes were made from the parental mptACD plasmid by divergent PCR. The results showed that expression of mptC alone is sufficient to confer sensitivity to class IIa bacteriocins in Lc. lactis.


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