Food applications of bacterial cell wall hydrolases

Callewaert, Lien; Walmagh, Maarten; Michiels, Chris W.; Lavigne, Rob

doi:10.1016/j.copbio.2010.10.012

Cited by 84 publications

(68 citation statements)

References 67 publications

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“…Bacterial lytic systems, involving endolysins released by holins from the bacterial cytoplasm during phage infection, are effective food preservatives (90). These systems have been used for pathogen control in human food sources, including fish, milk, cheese, eggs, and poultry (91)(92)(93). They similarly should be useful antibacterial agents in animal feed stocks.…”

Section: Use Of Holins For Therapeutic Purposes In Medicinementioning

confidence: 99%

Holins in Bacteria, Eukaryotes, and Archaea: Multifunctional Xenologues with Potential Biotechnological and Biomedical Applications

2015

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bHolins form pores in the cytoplasmic membranes of bacteria for the primary purpose of releasing endolysins that hydrolyze the cell wall and induce cell death. Holins are encoded within bacteriophage genomes, where they promote cell lysis for virion release, and within bacterial genomes, where they serve a diversity of potential or established functions. These include (i) release of gene transfer agents, (ii) facilitation of programs of differentiation such as those that allow sporulation and spore germination, (iii) contribution to biofilm formation, (iv) promotion of responses to stress conditions, and (v) release of toxins and other proteins. There are currently 58 recognized families of holins and putative holins with members exhibiting between 1 and 4 transmembrane ␣-helical spanners, but many more families have yet to be discovered. Programmed cell death in animals involves holin-like proteins such as Bax and Bak that may have evolved from bacterial holins. Holin homologues have also been identified in archaea, suggesting that these proteins are ubiquitous throughout the three domains of life. Phage-mediated cell lysis of dualmembrane Gram-negative bacteria also depends on outer membrane-disrupting "spanins" that function independently of, but in conjunction with, holins and endolysins. In this minireview, we provide an overview of their modes of action and the first comprehensive summary of the many currently recognized and postulated functions and uses of these cell lysis systems. It is anticipated that future studies will result in the elucidation of many more such functions and the development of additional applications.

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Section: Use Of Holins For Therapeutic Purposes In Medicinementioning

confidence: 99%

Holins in Bacteria, Eukaryotes, and Archaea: Multifunctional Xenologues with Potential Biotechnological and Biomedical Applications

2015

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“…It has been reported that the endolysin, a phage-encoded peptidoglycan hydrolase, generally shows a broader lytic spectrum than the phage (39)(40)(41)(42)(43). Moreover, the development of resistance against endolysins has not been reported (44)(45)(46)(47). Therefore, we chose the endolysin of PBC1 (LysPBC1) as an alternative or complementary antimicrobial against B. cereus and tested its lytic activity.…”

Section: Resultsmentioning

confidence: 99%

Bacteriophage PBC1 and Its Endolysin as an Antimicrobial Agent against Bacillus cereus

Kong

Ryu

2015

Appl Environ Microbiol

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Bacillus cereus is an opportunistic human pathogen responsible for food poisoning and other, nongastrointestinal infections. Due to the emergence of multidrug-resistant B. cereus strains, the demand for alternative therapeutic options is increasing. To address these problems, we isolated and characterized a Siphoviridae virulent phage, PBC1, and its lytic enzymes. PBC1 showed a very narrow host range, infecting only 1 of 22 B. cereus strains. Phylogenetic analysis based on the major capsid protein revealed that PBC1 is more closely related to the Bacillus clarkii phage BCJA1c and phages of lactic acid bacteria than to the phages infecting B. cereus. Whole-genome comparison showed that the late-gene region, including the terminase gene, structural genes, and holin gene of PBC1, is similar to that from B. cereus temperate phage 250, whereas their endolysins are different. Compared to the extreme host specificity of PBC1, its endolysin, LysPBC1, showed a much broader lytic spectrum, albeit limited to the genus Bacillus. The catalytic domain of LysPBC1 when expressed alone also showed Bacillus-specific lytic activity, which was lower against the B. cereus group but higher against the Bacillus subtilis group than the full-length protein. Taken together, these results suggest that the virulent phage PBC1 is a useful component of a phage cocktail to control B. cereus, even with its exceptionally narrow host range, as it can kill a strain of B. cereus that is not killed by other phages, and that LysPBC1 is an alternative biocontrol agent against B. cereus. Bacillus cereus is a spore-forming, opportunistic Gram-positive bacterium that is widely distributed in the environment. Because B. cereus produces emetic toxin and enterotoxins, it causes food poisoning, including vomiting and diarrhea, particularly after the consumption of rice-based dishes (1). The Centers for Disease and Control and Prevention (CDC) reported that B. cereus outbreaks account for 2 to 5% of food-borne diseases in the United States (2). In addition to food poisoning, B. cereus is also associated with potentially fatal non-gastrointestinal tract infections due to the various types of toxins, including phospholipases, proteases, and hemolysins, produced during growth (3). For these reasons, there is an urgent need to control B. cereus. Since B. cereus is generally resistant to beta-lactam antibiotics and several strains of B. cereus are also resistant to erythromycin, tetracycline, and fluoroquinolones (1, 4), the demand for alternative methods to control B. cereus has grown (3).Bacteriophages, natural killers of bacteria, have gained increasing attention in the past few decades, particularly in light of emerging antibiotic resistance (5, 6). Bacteriophages are much more specific than antibiotics, so they have minimal impact on commensal bacteria other than the host. Although bacteria can develop resistance to their viral predators, finding a new phage that can kill resistant bacteria is not difficult, because the phage itself continually evolves again...

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“…Knowledge of how the PGB domain binds and recognizes cortex PG can be extrapolated to other PG hydrolases and lyases, and could ultimately help in the design of inhibitors that interfere with spore PG degradation. This knowledge could also be exploited in biotechnology applications such as the use of PGB domains for the detection and removal of foodborne pathogens (Callewaert et al, 2011).…”

Section: Discussionmentioning

confidence: 99%

Functional analysis of SleC from Clostridium difficile: an essential lytic transglycosylase involved in spore germination

et al. 2014

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Clostridium difficile is the most common cause of enteric disease and presents a major burden on healthcare systems globally due in part to the observed rapid rise in antibiotic resistance. The ability of C. difficile to form endospores is a key feature in the organism’s pathogenesis and transmission, and contributes greatly to its resilient nature. Endospores are highly resistant to disinfection, allowing them to persist on hospital surfaces. In order for the organism to cause disease, the spores must germinate and revert to a vegetative form. While spore germination in Bacillus spp. is well understood, very little is known about this process in Clostridia. Here we report the characterization of SleC (CD0551) from C. difficile 630. Bioinformatic analysis of SleC indicated a multi-domained protein possessing a peptidoglycan-binding (PGB) domain, a SpoIID/LytB domain and an undefined N-terminal region. We have confirmed that SleC is an exo-acting lytic transglycosylase with the catalytic activity localized to the N-terminal region. Additionally, we have shown that both the N-terminal catalytic domain and the C-terminal PGB domain require muramyl-δ-lactam for substrate binding. As with carbohydrate-binding modules from cellulases and xylanases, the PGB domain may be responsible for increasing the processivity of SleC by concentrating the enzyme at the surface of the substrate.

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Food applications of bacterial cell wall hydrolases

Cited by 84 publications

References 67 publications

Holins in Bacteria, Eukaryotes, and Archaea: Multifunctional Xenologues with Potential Biotechnological and Biomedical Applications

Holins in Bacteria, Eukaryotes, and Archaea: Multifunctional Xenologues with Potential Biotechnological and Biomedical Applications

Bacteriophage PBC1 and Its Endolysin as an Antimicrobial Agent against Bacillus cereus

Functional analysis of SleC from Clostridium difficile: an essential lytic transglycosylase involved in spore germination

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