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Open AccessArticle

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

1
Department of Infectious Disease, College of Pharmaceutical Sciences, Matsuyama University, 4-2 Bunkyo-cho, Matsuyama, Ehime 790-8578, Japan
2
Laboratory of Food Microbiology and Hygiene, Graduate School of Biosphere Science, Hiroshima University, 1-4-4 Kagamiyama-cho, Higashihiroshima, Hiroshima 739-8528, Japan
3
Laboratory of Food Microbiology and Hygiene, Graduate School of Integrated Sciences for Life, Hiroshima University, 1-4-4 Kagamiyama, Higashihiroshima, Hiroshima 739-8528, Japan
4
Laboratory of Food Microbiology, Graduate School of Human Life Sciences Food and Nutritional Sciences, Jumonji University, 2-1-28, Kansawa, Niiza, Saitama 352-8510, Japan
*
Author to whom correspondence should be addressed.
These authors should be considered joint first authors.
Academic Editor: Hugo Oliveira
Antibiotics 2021, 10(3), 245; https://doi.org/10.3390/antibiotics10030245
Received: 6 January 2021 / Revised: 24 February 2021 / Accepted: 25 February 2021 / Published: 1 March 2021
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. View Full-Text
Keywords: endolysin; amidase; Clostridium perfringens; bacterial cell wall; peptidoglycan endolysin; amidase; Clostridium perfringens; bacterial cell wall; peptidoglycan
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MDPI and ACS Style

Sekiya, H.; Okada, M.; Tamai, E.; Shimamoto, T.; Shimamoto, T.; Nariya, H. A Putative Amidase Endolysin Encoded by Clostridium perfringens St13 Exhibits Specific Lytic Activity and Synergizes with the Muramidase Endolysin Psm. Antibiotics 2021, 10, 245. https://doi.org/10.3390/antibiotics10030245

AMA Style

Sekiya H, Okada M, Tamai E, Shimamoto T, Shimamoto T, Nariya H. A Putative Amidase Endolysin Encoded by Clostridium perfringens St13 Exhibits Specific Lytic Activity and Synergizes with the Muramidase Endolysin Psm. Antibiotics. 2021; 10(3):245. https://doi.org/10.3390/antibiotics10030245

Chicago/Turabian Style

Sekiya, Hiroshi; Okada, Maho; Tamai, Eiji; Shimamoto, Toshi; Shimamoto, Tadashi; Nariya, Hirofumi. 2021. "A Putative Amidase Endolysin Encoded by Clostridium perfringens St13 Exhibits Specific Lytic Activity and Synergizes with the Muramidase Endolysin Psm" Antibiotics 10, no. 3: 245. https://doi.org/10.3390/antibiotics10030245

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