Brevibacillus laterosporus, a Pathogen of Invertebrates and a Broad-Spectrum Antimicrobial Species

Ruiu, Luca

doi:10.3390/insects4030476

Cited by 119 publications

(89 citation statements)

References 78 publications

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“…In addition to B. cereus and B. thuringiensis, vip1 and vip2 genes have also been found in other bacterial species, such as Lysinibacillus sphaericus (formerly Bacillus sphaericus) and Brevibacillus laterosporus (17,18). Studies on the distribution of vip1 and vip2 genes have shown that they are found in ϳ10% of B. thuringiensis strains (7,(19)(20)(21)(22).…”

Section: The Binary Vip1/vip2 Toxinmentioning

confidence: 99%

Bacterial Vegetative Insecticidal Proteins (Vip) from Entomopathogenic Bacteria

Chakroun

Banyuls

Bel

et al. 2016

Microbiol Mol Biol Rev

260

261

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SUMMARYEntomopathogenic bacteria produce insecticidal proteins that accumulate in inclusion bodies or parasporal crystals (such as the Cry and Cyt proteins) as well as insecticidal proteins that are secreted into the culture medium. Among the latter are the Vip proteins, which are divided into four families according to their amino acid identity. The Vip1 and Vip2 proteins act as binary toxins and are toxic to some members of the Coleoptera and Hemiptera. The Vip1 component is thought to bind to receptors in the membrane of the insect midgut, and the Vip2 component enters the cell, where it displays its ADP-ribosyltransferase activity against actin, preventing microfilament formation. Vip3 has no sequence similarity to Vip1 or Vip2 and is toxic to a wide variety of members of the Lepidoptera. Its mode of action has been shown to resemble that of the Cry proteins in terms of proteolytic activation, binding to the midgut epithelial membrane, and pore formation, although Vip3A proteins do not share binding sites with Cry proteins. The latter property makes them good candidates to be combined with Cry proteins in transgenic plants (Bacillus thuringiensis-treated crops [Bt crops]) to prevent or delay insect resistance and to broaden the insecticidal spectrum. There are commercially grown varieties of Bt cotton and Bt maize that express the Vip3Aa protein in combination with Cry proteins. For the most recently reported Vip4 family, no target insects have been found yet.

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Section: The Binary Vip1/vip2 Toxinmentioning

confidence: 99%

Bacterial Vegetative Insecticidal Proteins (Vip) from Entomopathogenic Bacteria

Chakroun

Banyuls

Bel

et al. 2016

Microbiol Mol Biol Rev

260

261

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“…The biocontrol potential of this bacterial species in agriculture is not limited to invertebrate pests (insects in different orders, nematodes and mollusks) but also includes phytopathogenic bacteria and fungi11. This broad-spectrum of activity is associated with a wide variety of molecules, including proteins and antibiotics, it produces.…”

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confidence: 99%

Spore surface proteins of Brevibacillus laterosporus are involved in insect pathogenesis

Marche

Mura

Falchi

et al. 2017

Sci Rep

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Outer spore envelope proteins of pathogenic bacteria often present specific virulence factors and tools to evade the defence system of their hosts. Brevibacillus laterosporus, a pathogen of invertebrates and an antimicrobial-producing species, is characterised by a unique spore coat and canoe-shaped parasporal body (SC-CSPB) complex surrounding the core spore. In the present study, we identified and characterised major proteins of the SC-CSPB complex of B. laterosporus, and we investigated their entomopathogenic role. Employing a proteomic approach and a B. laterosporus-house fly study model, we found four highly conserved proteins (ExsC, CHRD, CpbA and CpbB) that function as insect virulence factors. CpbA was associated with a significantly higher mortality of flies and greater relative gene expression levels during sporulation, compared to the other SC-CSPB proteins. Taken together, we suggest that spore surface proteins are a part of a complex set of toxins and virulence factors that B. laterosporus employs in its pathogenicity against flies.

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“…Many bioactive compounds have been isolated from Brevibacillus spp. since then, including new antibacterial, antifungal, and anti-invertebrate agents (8,9). For instance, extracellular neutral protease that controls nematode growth was obtained from a Brevibacillus sp.…”

mentioning

confidence: 99%

Isolation and Structural Elucidation of Brevibacillin, an Antimicrobial Lipopeptide from Brevibacillus laterosporus That Combats Drug-Resistant Gram-Positive Bacteria

Huang

Yuan

et al. 2016

Appl Environ Microbiol

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A new environmental bacterial strain exhibited strong antimicrobial characteristics against methicillin-resistant Staphylococcus aureus, vancomycin-resistant strains of Enterococcus faecalis and Lactobacillus plantarum, and other Gram-positive bacteria. The producer strain, designated OSY-I 1 , was determined to be Brevibacillus laterosporus via morphological, biochemical, and genetic analyses. The antimicrobial agent was extracted from cells of OSY-I 1 with isopropanol, purified by high-performance liquid chromatography, and structurally analyzed using mass spectrometry (MS) and nuclear magnetic resonance (NMR). The MS and NMR results, taken together, uncovered a linear lipopeptide consisting of 13 amino acids and an N-terminal C 6 fatty acid (FA) chain, 2-hydroxy-3-methylpentanoic acid. The lipopeptide (FA-Dhb-Leu-Orn-Ile-Ile-Val-Lys-Val-Val-Lys-Tyr-Leu-valinol, where Dhb is ␣,␤-didehydrobutyric acid and valinol is 2-amino-3-methyl-1-butanol) has a molecular mass of 1,583.0794 Da and contains three modified amino acid residues: ␣,␤-didehydrobutyric acid, ornithine, and valinol. The compound, designated brevibacillin, was determined to be a member of a cationic lipopeptide antibiotic family. In addition to its potency against drugresistant bacteria, brevibacillin also exhibited low MICs (1 to 8 g/ml) against selected foodborne pathogenic and spoilage bacteria, such as Listeria monocytogenes, Bacillus cereus, and Alicyclobacillus acidoterrestris. Purified brevibacillin showed no sign of degradation when it was held at 80°C for 60 min, and it retained at least 50% of its antimicrobial activity when it was held for 22 h under acidic or alkaline conditions. On the basis of these findings, brevibacillin is a potent antimicrobial lipopeptide which is potentially useful to combat drug-resistant bacterial pathogens and foodborne pathogenic and spoilage bacteria. U nregulated access to antibiotics is one of the main reasons for the spread of antibiotic-resistant pathogens and their resistance genes through migration, travel, and trade (1). It was reported that in Europe alone, 25,000 patients die annually because of bacterial infections which cannot be treated with common antibiotics (2). Examples of antibiotic-resistant bacteria are methicillin-resistant Staphylococcus aureus (MRSA), vancomycin-resistant Enterococcus spp., carbapenem-resistant Mycobacterium tuberculosis, and highly virulent multidrug-resistant Clostridium difficile strains (2-5). Therefore, the discovery and development of new antimicrobial agents are of paramount importance. Despite their natural scarcity, new antimicrobial agents can be discovered by subjecting microorganisms that potentially produce such agents to screening and isolation processes (6, 7).The current study led to the discovery of a new strain of Brevibacillus sp. with promising antimicrobial activity. The genus Brevibacillus was established in 1996 on the basis of a genetic reclassification of strains previously recognized to be Bacillus brevis (8). Many bioactive compounds have been...

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Brevibacillus laterosporus, a Pathogen of Invertebrates and a Broad-Spectrum Antimicrobial Species

Cited by 119 publications

References 78 publications

Bacterial Vegetative Insecticidal Proteins (Vip) from Entomopathogenic Bacteria

Bacterial Vegetative Insecticidal Proteins (Vip) from Entomopathogenic Bacteria

Spore surface proteins of Brevibacillus laterosporus are involved in insect pathogenesis

Isolation and Structural Elucidation of Brevibacillin, an Antimicrobial Lipopeptide from Brevibacillus laterosporus That Combats Drug-Resistant Gram-Positive Bacteria

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