Journal of Animal Science and Technology
Korean Society of Animal Science and Technology
Article

Development and characterization of endolysin SALys78925 with antimicrobial activity against Streptococcus agalactiae

Sohyeon Yoon1, Joonbeom Moon1, Hanbeen Kim1,2, Jakyeom Seo1,*
1Department of Animal Science, Life and Industry Convergence Research Institute, Pusan National University, Miryang 50463, Korea.
2Faculty of Land and Food Systems, The University of British Columbia, Vancouver 248-2357, Canada.
*Corresponding Author: Jakyeom Seo, Department of Animal Science, Life and Industry Convergence Research Institute, Pusan National University, Miryang 50463, Korea, Republic of. Phone: +82-55-350-5513. E-mail: jseo81@pusan.ac.kr.

© Copyright 2025 Korean Society of Animal Science and Technology. This is an Open-Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Received: Feb 04, 2025; Revised: Mar 26, 2025; Accepted: Apr 08, 2025

Published Online: Apr 23, 2025

Abstract

<italic>Streptococcus agalactiae</italic> is one of the pathogens in bovine mastitis, which contributes to substantial economic losses in the dairy industry. Endolysins are bacteriophage-encoded peptidoglycan degrading hydrolases, and they have become a novel weapon for selective elimination of target bacteria. This study aimed to identify endolysin with specific lytic activity against <italic>S. agalactiae</italic>, characterize the endolysin SALys78925, and evaluate its efficacy against related pathogens. The whole genome sequence of <italic>S. agalactiae </italic>strain was obtained from the National Center for Biotechnology Information database, and the putative gene for <italic>SALys78925</italic> was retrieved from their genomes. <italic>SALys78925</italic> was overexpressed in <italic>Escherichia coli</italic> BL21 (DE3) using pET system. The optimal conditions of SALys78925 were determined by assessing lytic activity under various ranges of pH, NaCl concentration, temperature, metal ions, and dosage. <italic>In silico</italic> analysis revealed that SALys78925 possesses a modular structure that comprises an N-terminal enzymatically active domain (Peptidase_M23) and a C-terminal cell wall binding domain (Zoocin A target recognition domain). SALys78925 exhibited maximal lytic activity against <italic>S. agalactiae</italic> KCCM 40417 at pH 9.0 and 37℃, but the activity decreased in a salt dose-dependent manner. The addition of Mn²⁺ enhanced SALys78925 activity, whereas Zn²⁺ reduced it by approximately 80%. Antimicrobial spectrum analysis revealed that SALys78925 exhibited varying degrees of lytic activity against multiple bacterial species, demonstrating potent lysis of <italic>S. agalactiae</italic> and lysis of <italic>Streptococcus parauberis</italic> and <italic>Enterococcus faecalis</italic>. These findings suggest that SALys78925 could be a promising candidate for preventing bovine mastitis in the dairy industry and beyond, offering a potential alternative to conventional antimicrobial treatments.

Keywords: endolysin; peptidoglycan hydrolase; Streptococcus agalactiae; bovine mastitis; antimicrobial agent