scholarly journals A model of the phage-encoded endolysin Psm, active against Clostridium perfringens, binding to the bacterial cell wall. Cell wall binding domains recognize the peptide side chains (cyan) of peptidoglycan to assist hydrolysis of the glycan backbone by the

2014 ◽  
Vol 92 (2) ◽  
pp. i-i
Keyword(s):  
Cell Wall ◽  
Clostridium Perfringens ◽  
Bacterial Cell ◽  
Bacterial Cell Wall ◽  
Side Chains ◽  
Binding Domains ◽  
Cell Wall Binding ◽  
Wall Cell ◽  
Hydrolysis Of

scholarly journals Thermophile Lytic Enzyme Fusion Proteins that Target Clostridium perfringens

Antibiotics ◽  
2019 ◽  
Vol 8 (4) ◽  
pp. 214 ◽  
Author(s):  
Steven M. Swift ◽  
Kevin P. Reid ◽  
David M. Donovan ◽  
Timothy G. Ramsay
Keyword(s):  
Cell Wall ◽  
Clostridium Perfringens ◽  
Animal Feed ◽  
Lytic Enzyme ◽  
Necrotic Enteritis ◽  
Lytic Enzymes ◽  
Thermostable Enzymes ◽  
Catalytic Domains ◽  
Binding Domains ◽  
Cell Wall Binding

Clostridium perfringens is a bacterial pathogen that causes necrotic enteritis in poultry and livestock, and is a source of food poisoning and gas gangrene in humans. As the agriculture industry eliminates the use of antibiotics in animal feed, alternatives to antibiotics will be needed. Bacteriophage endolysins are enzymes used by the virus to burst their bacterial host, releasing bacteriophage particles. This type of enzyme represents a potential replacement for antibiotics controlling C. perfringens. As animal feed is often heat-treated during production of feed pellets, thermostable enzymes would be preferred for use in feed. To create thermostable endolysins that target C. perfringens, thermophile endolysin catalytic domains were fused to cell wall binding domains from different C. perfringens prophage endolysins. Three thermostable catalytic domains were used, two from prophage endolysins from two Geobacillus strains, and a third endolysin from the deep-sea thermophilic bacteriophage Geobacillus virus E2 (GVE2). These domains harbor predicted L-alanine-amidase, glucosaminidase, and L-alanine-amidase activities, respectively and degrade the peptidoglycan of the bacterial cell wall. The cell wall binding domains were from C. perfringens prophage endolysins (Phage LYtic enzymes; Ply): PlyCP18, PlyCP10, PlyCP33, PlyCP41, and PlyCP26F. The resulting fifteen chimeric proteins were more thermostable than the native C. perfringens endolysins, and killed swine and poultry disease-associated strains of C. perfringens.

Inhibition of lysozyme by positively charged groups in the mucopeptide of the bacterial cell wall

1967 ◽  
Vol 167 (1009) ◽  
pp. 443-445 ◽  
Keyword(s):  
Cell Wall ◽  
Small Molecules ◽  
Bacterial Cell ◽  
Cell Walls ◽  
Bacterial Cell Wall ◽  
Amino Groups ◽  
Small Molecular Weight ◽  
Hydrolysis Of ◽  
Isolated Cell ◽  
Positively Charged

The elegant work that has been presented this afternoon has been concerned with the structure of lysozyme in relation to its action on model substrates of small molecular weight, or its inhibition by equally small molecules. The ‘natural’ substrate is presumably the mucopeptide of bacterial cell wall, which is a large, highly complex and insoluble molecule. A portion of a possible structure of a mucopeptide (Tipper & Strominger 1965) in this case from Staphylococcus aureus , is given in figure 51. Evidently in order to facilitate hydrolysis of the glycosidic links on C-1 of muramic acid (and, in the absence of O-acetyl groups, the enzyme is very good at this) lysozyme molecules must be able to approach closely to the relevant part of the polysaccharide backbone. One of the factors that appears to influence this approach of enzyme and substrate is the presence of positive charges on the mucopeptide. Isolated cell walls of Corynebacterium tritici were completely resistant to lysozyme, but could be made sensitive by the action of formamide at 150 °C for 15 min (Perkins 1965). It was found that this procedure did not remove more than 10% of the non-mucopeptide carbohydrate present, but it did formylate the free amino groups of diaminobutyric acid that occurred in the untreated wall. Acetylation by a mild procedure, followed by treatment with alkali to remove any O-acetyl groups, also caused the walls to become susceptible to dissolution by lysozyme.

scholarly journals Intramolecular synergism and bacterial lysis regulation can explain the complex multi-domain architecture of the bacteriophage endolysin PlySK1249

2020 ◽  
Author(s):  
Frank Oechslin ◽  
Carmen Menzi ◽  
Philippe Moreillon ◽  
Gregory Resch
Keyword(s):  
Cell Wall ◽  
Modular Forms ◽  
Bacterial Cell ◽  
Domain Architecture ◽  
Bacterial Cell Wall ◽  
Catalytic Domains ◽  
Cell Wall Binding ◽  
Bacterial Lysis ◽  
The Moment

AbstractEndolysins are peptidoglycan hydrolases produced at the end of the bacteriophage (phage) replication cycle to lyse the host cell. Gram-positive phages endolysins come in a variety of multi-modular forms that combine different catalytic domains and may have evolved to adapt to their bacterial hosts. However, the reason why phage can adopt endolysin with such complex multidomain architecture is for the moment not well understood.We used the Streptococcus dysgalactiae phage endolysin PlySK1249 as a model to study the implication of multi-domain architecture in phage-induced bacterial lysis and lysis regulation. The activity of the enzyme relied on a bacteriolytic amidase (Ami), a non-bacteriolytic L-Ala-D-Ala endopeptidase (CHAP) acting as a de-chaining enzyme and central LysM cell wall binding domain (CBD).Ami and CHAP synergized for peptidoglycan digestion and bacteriolysis in the native enzyme or when expressed individually and reunified in vitro. This cooperation could be modulated by bacterial cell wall-associated proteases, which specifically cleaved the two linkers connecting the different domains. While both catalytic domains were observed to act coordinately to optimize bacterial lysis, the CBD is expected to delay diffusion of the enzyme until proteolytic inactivation is achieved.As for certain autolysins, PlySK1249 cleavage by bacterial cell wall associated proteases might be an example of dual phage-bacterial regulation and mutual coevolution. In addition, understanding more thoroughly the multidomain interplay of PlySK1249 opens new perspectives on the ideal architecture of therapeutic antibacterial endolysins.

Role of bacterial cell wall proteinase in antihypertension

2002 ◽  
Vol 22 (1-2) ◽  
pp. 209-222 ◽  
Author(s):  
Bénédicte Flambard
Keyword(s):  
Cell Wall ◽  
Bacterial Cell ◽  
Bacterial Cell Wall
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