Isolation of the Bacillus subtilis antimicrobial peptide subtilosin from the dairy product-derived Bacillus amyloliquefaciens

Sutyak, Katia E.; Wirawan, Ruth E.; Aroutcheva, Alla; Chikindas, Michael L.

doi:10.1111/j.1365-2672.2007.03626.x

Cited by 175 publications

(144 citation statements)

References 32 publications

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“…The only fully characterised bacteriocin from B. amyloliquefaciens was found to correspond to subtilosin A, a bacteriocin previously reported in B. subtilis [24]. However, genetic evidence suggests that this results rather from an intra-species horizontal transfer of gene (HGT) than from a mechanism selected by evolution.…”

Section: Discussionmentioning

confidence: 76%

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Antilisterial Activity on Poultry Meat of Amylolysin, a Bacteriocin from Bacillus amyloliquefaciens GA1

Halimi

Dortu

Arias

et al. 2010

Probiotics & Antimicro. Prot.

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This paper describes the production, the purification and the antilisterial activity of amylolysin, a novel bacteriocin from B. amyloliquefaciens GA1. The strain genome was first analysed using PCR techniques for the presence of gene clusters that direct the synthesis of characterised bacteriocins from B. amyloliquefaciens and the closely related B. subtilis. Our results suggest that amylolysin corresponds to a novel bacteriocin. The effect of amylolysin on the growth of different isolates of Listeria monocytogenes was evaluated in poultry meat during 21 days of storage at 4°C. A potent antilisterial effect was observed for all the indicator strains tested, demonstrating that amylolysin is a novel bacteriocin that could be used as a food preservative.

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Section: Discussionmentioning

confidence: 76%

“…These include subtilin from B. subtilis [17], megacin A-216 from B. megaterium [16], cerein 7 from B. cereus [4] and subtilosin A, produced by some strains of both B. subtilis and B. amyloliquefaciens [3,4,24]. Some of these substances have been successfully tested as food preservatives in dairy products [4].…”

Section: Introductionmentioning

confidence: 99%

Antilisterial Activity on Poultry Meat of Amylolysin, a Bacteriocin from Bacillus amyloliquefaciens GA1

Halimi

Dortu

Arias

et al. 2010

Probiotics & Antimicro. Prot.

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“…The lipopeptides could also induce the plant defence responses to conquer the pathogens . Moreover, some peptides were also reported to be able to inhibit the pathogen growth, such as lantibiotics, bacteriocin, and LCI protein (Sutyak et al 2008;Herzner et al 2011;Meng et al 2012;Arguelles Arias et al 2013;Scholz et al 2014;Rasimus-Sahari et al 2015). The good stability and inhibitory activities of the peptides pointed out their potential in the plant protection and food preservation.…”

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confidence: 99%

Purification and characterisation of a fungicidal peptide from Bacillus amyloliquefaciens NCPSJ7

Jun-hua¹,

Zhao²,

Qiu³

et al. 2017

Czech J. Food Sci.

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Wang J., Zhao S., Qiu J., Zhou Q., Liu X., Xin X., Guo D., Yudina T.G., Wang Y., Sun H., Chen X., Chen L. (2017): Purification and characterisation of a fungicidal peptide from Bacillus amyloliquefaciens NCPSJ7. Czech J. Food Sci., 35: 113-121.Bacillus amyloliquefaciens NCPSJ7 could secrete extracellular antimicrobial substances, showing potent antifungal activities. An active peptide AFP3 was isolated from the fermentation supernatant. After chromatography, the purified peptide was tested for the fungicidal activity, molecular mass, and stability. The results indicated that the peptide with a molecular mass of around 3.3 kDa, showed discernible inhibition of the pathogen Fusarium oxysporum f.sp. niveum with the minimum fungicidal concentration of 31 µg/ml. It also exhibited excellent inhibition of some representative pathogenic fungi at a low concentration. Moreover, the peptide remained active at a wide range of temperatures and pH. Ion Na + may even increase the antifungal activities. At the same time, the peptide could well tolerate the treatment with trypsin. Electron microscopy was used to investigate the effect of the peptide on the pathogens. The peptide inhibited the growth of pathogens by disrupting the integrity of the hyphal membranes, resulting in their lysis. The potent fungicidal activities and stability made the peptide be a candidate for a biopreservative.

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“…Subtilosin A is a 35-amino-acid bacteriocin originally isolated from Bacillus subtilis by Babasaki et al (2) but was also found in Bacillus atrophaeus (26) and Bacillus amyloliquefaciens isolated from a dairy product (29). It is a unique macrocyclic bacteriocin in part due to its having an anionic nature unlike many other membrane-targeting cationic bacteriocins.…”

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confidence: 99%

Isolation of a Variant of Subtilosin A with Hemolytic Activity

et al. 2009

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Bacillus subtilis produces an anionic bacteriocin called subtilosin A that possesses antibacterial activity against certain gram-positive bacteria. In this study, we uncovered a hemolytic mutant of B. subtilis that produces an altered form of subtilosin A. The mutant bacteriocin, named subtilosin A1, has a replacement of threonine at position 6 with isoleucine. In addition to the hemolytic activity, subtilosin A1 was found to exhibit enhanced antimicrobial activity against specific bacterial strains. The B. subtilis albB mutant that does not produce a putative immunity peptide was more sensitive to both subtilosin A and subtilosin A1. A spontaneous suppressor mutation of albB that restored resistance to subtilosin A and subtilosin A1 was obtained. The sbr (subtilosin resistance) mutation conferring the resistance is not linked to the sboA-alb locus. The sbr mutation does not increase the resistance of B. subtilis to other cell envelope-targeted antimicrobial agents, indicating that the mutation specifically confers the resistance to subtilosins. The findings suggest possible bioengineering approaches for obtaining anionic bacteriocins with enhanced and/or altered bactericidal activity. Furthermore, future identification of the subtilosin-resistant mutation could provide insights into the mechanism of subtilosin A activity.Bacteria produce a variety of secondary metabolites, such as antibiotics and bacteriocins. Bacteriocins are proteinaceous antimicrobial substances that are often distinguished from traditional antibiotics by their narrow range of activity against closely related bacteria. However, bacteriocins produced by gram-positive bacteria show a relatively broader spectrum than those from gram-negative bacteria (reviewed in references 14 and 22). Various gram-positive bacteria produce small bacteriocins that are ribosomally synthesized peptides but that are often heavily modified during posttranslational processing. The target of these bacteriocins is primarily the cytoplasmic membrane, where they create pores through which ions can pass, leading eventually to cell death.Subtilosin A is a 35-amino-acid bacteriocin originally isolated from Bacillus subtilis by Babasaki et al. (2) but was also found in Bacillus atrophaeus (26) and Bacillus amyloliquefaciens isolated from a dairy product (29). It is a unique macrocyclic bacteriocin in part due to its having an anionic nature unlike many other membrane-targeting cationic bacteriocins. Subtilosin A is formed from its precursor by proteolytic cleavage of the N-terminal leader peptide and cyclization through covalent linkage between the N-terminal asparagine and the C-terminal glycine. Structure analysis of subtilosin A by 1 H nuclear magnetic resonance (NMR) spectrometry suggested the formation of thioether bonds between Cys4/Phe31, Cys7/ Thr28, and Cys13/Phe22, but the actual sites of connection were unknown (15). Subsequent isotopic labeling and multidimensional NMR analysis demonstrated unprecedented crosslinking between sulfurs of the cysteines and the ␣ ca...

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Isolation of the Bacillus subtilis antimicrobial peptide subtilosin from the dairy product-derived Bacillus amyloliquefaciens

Abstract: This is the first report of intra-species horizontal gene transfer for subtilosin and the first fully characterized bacteriocin isolated from B. amyloliquefaciens. Finally, this is the first report on subtilosin's activity against bacterial vaginosis-associated pathogens.

Cited by 175 publications

References 32 publications

Antilisterial Activity on Poultry Meat of Amylolysin, a Bacteriocin from Bacillus amyloliquefaciens GA1

Antilisterial Activity on Poultry Meat of Amylolysin, a Bacteriocin from Bacillus amyloliquefaciens GA1

Purification and characterisation of a fungicidal peptide from Bacillus amyloliquefaciens NCPSJ7

Isolation of a Variant of Subtilosin A with Hemolytic Activity

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