Characteristics for phage-encoded cell wall hydrolase of LysSAP27 to reduce staphylococcal food poisoning

2021 ◽  
Author(s):  
Do-won Park ◽  
Young-Duck Lee ◽  
Jong-Hyun Park
Keyword(s):  
Cell Wall ◽  
Food Poisoning ◽  
Cell Wall Hydrolase

scholarly journals A Putative Amidase Endolysin Encoded by Clostridium perfringens St13 Exhibits Specific Lytic Activity and Synergizes with the Muramidase Endolysin Psm

Antibiotics ◽  
2021 ◽  
Vol 10 (3) ◽  
pp. 245
Author(s):  
Hiroshi Sekiya ◽  
Maho Okada ◽  
Eiji Tamai ◽  
Toshi Shimamoto ◽  
Tadashi Shimamoto ◽  
...  
Keyword(s):  
Cell Wall ◽  
Clostridium Perfringens ◽  
Antimicrobial Agents ◽  
Catalytic Domain ◽  
Food Poisoning ◽  
Binding Activity ◽  
Lytic Activity ◽  
Intestinal Bacterium ◽  
Terminal Domain ◽  
Cell Wall Binding

Clostridium perfringens is an often-harmful intestinal bacterium that causes various diseases ranging from food poisoning to life-threatening fulminant disease. Potential treatments include phage-derived endolysins, a promising family of alternative antimicrobial agents. We surveyed the genome of the C. perfringens st13 strain and identified an endolysin gene, psa, in the phage remnant region. Psa has an N-terminal catalytic domain that is homologous to the amidase_2 domain, and a C-terminal domain of unknown function. psa and gene derivatives encoding various Psa subdomains were cloned and expressed in Escherichia coli as N-terminal histidine-tagged proteins. Purified His-tagged full-length Psa protein (Psa-his) showed C. perfringens-specific lytic activity in turbidity reduction assays. In addition, we demonstrated that the uncharacterized C-terminal domain has cell wall-binding activity. Furthermore, cell wall-binding measurements showed that Psa binding was highly specific to C. perfringens. These results indicated that Psa is an amidase endolysin that specifically lyses C. perfringens; the enzyme’s specificity is highly dependent on the binding of the C-terminal domain. Moreover, Psa was shown to have a synergistic effect with another C. perfringens-specific endolysin, Psm, which is a muramidase that cleaves peptidoglycan at a site distinct from that targeted by Psa. The combination of Psa and Psm may be effective in the treatment and prevention of C. perfringens infections.

scholarly journals Identification and Characterization of a Peptidoglycan Hydrolase, MurA, of Listeria monocytogenes, a Muramidase Needed for Cell Separation

2003 ◽  
Vol 185 (23) ◽  
pp. 6801-6808 ◽  
Author(s):  
Shannon A. Carroll ◽  
Torsten Hain ◽  
Ulrike Technow ◽  
Ayub Darji ◽  
Philippos Pashalidis ◽  
...  
Keyword(s):  
Cell Wall ◽  
Listeria Monocytogenes ◽  
Cell Separation ◽  
Bacterial Species ◽  
Surface Protein ◽  
Wild Type ◽  
Terminal Domain ◽  
Cell Wall Hydrolase ◽  
Characteristic Features ◽  
Type Gene

ABSTRACT A novel cell wall hydrolase encoded by the murA gene of Listeria monocytogenes is reported here. Mature MurA is a 66-kDa cell surface protein that is recognized by the well-characterized L. monocytogenes-specific monoclonal antibody EM-7G1. MurA displays two characteristic features: (i) an N-terminal domain with homology to muramidases from several gram-positive bacterial species and (ii) four copies of a cell wall-anchoring LysM repeat motif present within its C-terminal domain. Purified recombinant MurA produced in Escherichia coli was confirmed to be an authentic cell wall hydrolase with lytic properties toward cell wall preparations of Micrococcus lysodeikticus. An isogenic mutant with a deletion of murA that lacked the 66-kDa cell wall hydrolase grew as long chains during exponential growth. Complementation of the mutant strain by chromosomal reintegration of the wild-type gene restored expression of this murein hydrolase activity and cell separation levels to those of the wild-type strain. Studies reported herein suggest that the MurA protein is involved in generalized autolysis of L. monocytogenes.

scholarly journals Factors Contributing to Heat Resistance of Clostridium perfringens Endospores

2008 ◽  
Vol 74 (11) ◽  
pp. 3328-3335 ◽  
Author(s):  
Benjamin Orsburn ◽  
Stephen B. Melville ◽  
David L. Popham
Keyword(s):  
Cell Wall ◽  
Heat Resistance ◽  
Clostridium Perfringens ◽  
Food Poisoning ◽  
High Heat ◽  
Relative Importance ◽  
High Heat Resistance ◽  
Factors Affecting ◽  
Cooking Process ◽  
Determining Factors

ABSTRACT The endospores formed by strains of type A Clostridium perfringens that produce the C. perfringens enterotoxin (CPE) are known to be more resistant to heat and cold than strains that do not produce this toxin. The high heat resistance of these spores allows them to survive the cooking process, leading to a large number of food-poisoning cases each year. The relative importance of factors contributing to the establishment of heat resistance in this species is currently unknown. The present study examines the spores formed by both CPE+ and CPE− strains for factors known to affect heat resistance in other species. We have found that the concentrations of DPA and metal ions, the size of the spore core, and the protoplast-to-sporoplast ratio are determining factors affecting heat resistance in these strains. While the overall thickness of the spore peptidoglycan was found to be consistent in all strains, the relative amounts of cortex and germ cell wall peptidoglycan also appear to play a role in the heat resistance of these strains.

scholarly journals Antimicrobial Activity of Exebacase (Lysin CF-301) against the Most Common Causes of Infective Endocarditis

2019 ◽  
Vol 63 (10) ◽  
Author(s):  
Aubrey Watson ◽  
Jun Taek Oh ◽  
Karen Sauve ◽  
Patricia A. Bradford ◽  
Cara Cassino ◽  
...  
Keyword(s):  
Antimicrobial Activity ◽  
Cell Wall ◽  
Infective Endocarditis ◽  
Broth Microdilution ◽  
Coagulase Negative Staphylococci ◽  
Content Type ◽  
Microdilution Method ◽  
Cell Wall Hydrolase ◽  
Broth Microdilution Method ◽  
Common Causes

ABSTRACT Exebacase, a recombinantly produced lysin (cell wall hydrolase), and comparator antibiotics were tested by the broth microdilution method against strain sets of Staphylococcus and Streptococcus spp., which are the most common causes of infective endocarditis in humans. Exebacase was active against all Staphylococcus spp. tested, including S. aureus and coagulase-negative staphylococci (MIC50/90, 0.5/1 μg/ml). Activity against Streptococcus spp. was variable, with S. pyogenes, S. agalactiae, and S. dysgalactiae (MIC50/90, 1/2 μg/ml) among the most susceptible.

scholarly journals Nucleotide sequence and regulation of a new putative cell wall hydrolase gene, cwlD, which affects germination in Bacillus subtilis. .

1995 ◽  
Vol 177 (19) ◽  
pp. 5582-5589 ◽  
Author(s):  
J Sekiguchi ◽  
K Akeo ◽  
H Yamamoto ◽  
F K Khasanov ◽  
J C Alonso ◽  
...  
Keyword(s):  
Cell Wall ◽  
Bacillus Subtilis ◽  
Nucleotide Sequence ◽  
Cell Wall Hydrolase
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