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A novel endolysin disrupts Streptococcus suis with high efficiency.
Ji, Wenhui; Huang, Qingqing; Sun, Liang; Wang, Hengan; Yan, Yaxian; Sun, Jianhe.
Affiliation
  • Ji W; Shanghai Key Laboratory of Veterinary Biotechnology, School of Agriculture and Biology, Shanghai Jiao Tong University, Key Laboratory of Urban Agriculture (South), Ministry of Agriculture, Shanghai 200240, China.
  • Huang Q; Shanghai Key Laboratory of Veterinary Biotechnology, School of Agriculture and Biology, Shanghai Jiao Tong University, Key Laboratory of Urban Agriculture (South), Ministry of Agriculture, Shanghai 200240, China.
  • Sun L; School of Veterinary Medicine, Gansu Agricultural University, Lanzhou, Gansu 730070, China.
  • Wang H; Shanghai Key Laboratory of Veterinary Biotechnology, School of Agriculture and Biology, Shanghai Jiao Tong University, Key Laboratory of Urban Agriculture (South), Ministry of Agriculture, Shanghai 200240, China.
  • Yan Y; Shanghai Key Laboratory of Veterinary Biotechnology, School of Agriculture and Biology, Shanghai Jiao Tong University, Key Laboratory of Urban Agriculture (South), Ministry of Agriculture, Shanghai 200240, China.
  • Sun J; Shanghai Key Laboratory of Veterinary Biotechnology, School of Agriculture and Biology, Shanghai Jiao Tong University, Key Laboratory of Urban Agriculture (South), Ministry of Agriculture, Shanghai 200240, China sunjhe@sjtu.edu.cn.
FEMS Microbiol Lett ; 362(24): fnv205, 2015 Dec.
Article in En | MEDLINE | ID: mdl-26534896
ABSTRACT
Streptococcus suis serotype 2 (S. suis 2) is a zoonotic pathogen that exhibits high-level resistance and multi-drug resistance to classic antibiotics and causes serious human casualties and heavy economic losses in the swine industry worldwide. Therefore, alternative therapies or novel antibacterial agents need to be developed to combat this pathogen. A novel endolysin derived from the S. suis temperate phage phi7917, termed Ly7917, was identified, which had broad lytic activity against S. suis type 1, 2, 7 and 9. Ly7917 consisted of an N-terminal cysteine, histidine-dependent amidohydrolases/peptidase catalytic domain and C-terminal SH3b cell wall binding domain. The endolysin maintained activity at high pH and its catalytic activity could be improved by addition of 10 µM 1.5 mM Ca(2+). In animal studies, 90% of BALB/c mice challenged with typical virulent strain HA9801 of S. suis 2 were protected by Ly7917 treatment. The bacterial load in the blood of HA9801-challenged mice was efficiently reduced almost 50% by Ly7917 while that of penicillin-G-treated mice kept almost unchanged. Our data suggest that Ly7917 may be an alternative therapeutic agent for infections caused by virulent S. suis strains.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Endopeptidases / Streptococcus suis / Streptococcus Phages Limits: Animals / Humans Language: En Journal: FEMS Microbiol Lett Year: 2015 Document type: Article Affiliation country:

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Endopeptidases / Streptococcus suis / Streptococcus Phages Limits: Animals / Humans Language: En Journal: FEMS Microbiol Lett Year: 2015 Document type: Article Affiliation country: