The Pore-Forming Haemolysins of Bacillus Cereus: A Review

Ramarao, Nalini; Sanchis, Vincent

doi:10.3390/toxins5061119

Cited by 145 publications

(125 citation statements)

References 102 publications

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“…Among these factors, some, such as phospholipases, destroy the cell membrane by enzymatic activity while others, such as certain hemolysins and enterotoxins, lyse the cells by pore formation [34]. The virulence factors described in this section are the protein toxins expressed in both B. cereus and B. thuringiensis (Table 29.1), identified either by experimental evidence or by similarity to other known virulence factors.…”

Section: Toxins Of B Cereus Slmentioning

confidence: 98%

Bacillus cereus phospholipases, enterotoxins, and other hemolysins

Lindbäck

Granum

2015

The Comprehensive Sourcebook of Bacterial Protein Toxins

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Section: Toxins Of B Cereus Slmentioning

confidence: 98%

Bacillus cereus phospholipases, enterotoxins, and other hemolysins

Lindbäck

Granum

2015

The Comprehensive Sourcebook of Bacterial Protein Toxins

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“…B. cereus is a human pathogen that causes diarrheal or emetic-type illnesses and is considered the third most important cause of collective food poisoning incidents in Europe (29,30). L. monocytogenes is a facultative intracellular foodborne pathogen that can cause listeriosis in animals and humans, especially immunocompromised individuals (31).…”

Section: Discussionmentioning

confidence: 99%

Three Novel Lantibiotics, Ticins A1, A3, and A4, Have Extremely Stable Properties and Are Promising Food Biopreservatives

Xin

Zheng

et al. 2015

Appl Environ Microbiol

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Lantibiotics are antimicrobial peptides with potential applications as the next generation of antimicrobials in the food industry and/or the pharmaceutical industry. Nisin has successfully been used as a food preservative for over 40 years, but its major drawback is its limited stability under neutral and alkaline pH conditions. To identify alternatives with better biochemical properties, we screened more than 100 strains of the Bacillus cereus group. Three novel lantibiotics, ticins A1 (4,062.98 Da), A3 (4,048.96 Da), and A4 (4,063.02 Da), which were highly thermostable (121°C for 30 min) and extremely pH tolerant (pH 2.0 to 9.0), were identified in Bacillus thuringiensis BMB3201. They all showed potent antimicrobial activities against all tested Gram-positive bacteria and greater activities than those of nisin A against Bacillus cereus and Listeria monocytogenes, two important foodborne pathogens. These three novel lantibiotics, with their extremely stable properties and potent antimicrobial activities, have the potential for use as biopreservatives. Bacteriocins are ribosomally synthesized antimicrobial peptides produced by various bacteria that are active against other bacteria either of the same species (narrow spectrum) or across genera (broad spectrum) (1). They are classified into two groups: posttranslationally modified bacteriocins and unmodified or cyclic bacteriocins (2). Lantibiotics (lanthipeptides) are the best-characterized modified bacteriocins, and their modifications include the formation of meso-lanthionine and 3-methyllanthionine residues, as well as dehydrated amino acids (Dha and Dhb) (3). Lanthionine (Lan) consists of two alanine residues cross-linked via a thioether linkage; 3-methyllanthionine (MeLan) contains one additional methyl group. Lanthipeptides are classified into four classes depending on their biosynthetic enzymes. For class I lanthipeptides, dehydration is carried out by a LanB dehydratase, and cyclization is catalyzed by a LanC cyclase. Class II lanthipeptides are modified by LanM lanthionine synthetases, which have an N-terminal dehydration domain and a C-terminal cyclization domain. For class III and IV lanthipeptides, the dehydration and cyclization reactions are catalyzed by multifunctional enzymes (RamC/LabKC or LanL).In the past decade, research on bacteriocins or lantibiotics has focused primarily on lactic acid bacteria (LAB), primarily because of their potential applications as preservatives in the food industry and/or as viable alternatives to antibiotics in medicine (2, 4). These bacteriocins also have several desirable properties that make them suitable for food preservation, as follows: (i) they are generally recognized as safe (GRAS), (ii) they are nontoxic to eukaryotic cells, (iii) they can be inactivated by digestive proteases, (iv) they are pH and heat tolerant, (v) they have a relatively broad antimicrobial spectrum against many Gram-positive foodborne pathogenic and spoilage bacteria, (vi) they show a bactericidal mode of action and no cross-resistance w...

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“…cereus toxins often cause severe food poisoning, accompanied by diarrhea [1]. This is the primary rea son for active research on toxins produced by B. cereus and its closest relative, B. thuringiensis.…”

mentioning

confidence: 99%

Effect of Bacillus cereus hemolysin II on hepatocyte cells

Kholodkov

Budarina

Andreeva-Kovalevskaya

et al. 2015

Appl Biochem Microbiol

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We investigated the efficiency of increasing the permeability (permeabilization) of cell membranes in primary liver cells by Bacillus cereus hemolysin II. An assessment of the degree of permeabilization was car ried out by measuring the fluorescence intensity of various low molecular weight dyes, which enter through pores into hepatocyte cells cultivated with hemolysin. We uncovered a high efficacy of hemolysin HlyII action on hepatocyte cell walls, which exceeded the effect of nonionic detergent, digitonin, which is commonly employed for pore formation in various cell membranes. Our results also point to the reversibility of mem brane permeabilization in primary hepatocytes. The data obtained in this study can be utilized for assessments of pore forming activity, in studies of hepatic mechanisms of action, and also the determination of the liver toxicity for different low molecular weight drugs.

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The Pore-Forming Haemolysins of Bacillus Cereus: A Review

Cited by 145 publications

References 102 publications

Bacillus cereus phospholipases, enterotoxins, and other hemolysins

Bacillus cereus phospholipases, enterotoxins, and other hemolysins

Three Novel Lantibiotics, Ticins A1, A3, and A4, Have Extremely Stable Properties and Are Promising Food Biopreservatives

Effect of Bacillus cereus hemolysin II on hepatocyte cells

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