Purified Recombinant Phage Lysin LySMP: An Extensive Spectrum of Lytic Activity for Swine Streptococci

被引:40
作者
Wang, Y. [2 ]
Sun, J. H. [2 ]
Lu, C. P. [1 ,2 ]
机构
[1] Nanjing Agr Univ, Minist Agr, Key Lab Anim Dis Diagnost & Immunol, Nanjing 210095, Peoples R China
[2] Shanghai Jiao Tong Univ, Sch Agr & Biol, Dept Anim Sci, Shanghai 200240, Peoples R China
关键词
GROUP-B STREPTOCOCCI; ENZYME CPL-1; STAPHYLOCOCCUS-AUREUS; BACTERIOPHAGE; SUIS; MENINGITIS; PNEUMONIAE; THERAPY; IDENTIFICATION; ELIMINATION;
D O I
10.1007/s00284-009-9379-x
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Bacteriophage lysin has attracted considerable attentions as possible antimicrobial agents for solution of antibiotic resistance. SMP was a Streptococcus suis serotype 2 bacteriophage isolated from nasal swabs of healthy Bama minipigs. The putative SMP bacteriophage lysin, designated LySMP, was recombinantly expressed in Escherichia coli BL21, and chromatographically purified. Treated with 0.8% of beta-mercaptoethanol, LySMP exhibited an extensive lysin spectrum than those of whole phage against bacteria investigated. S. suis serotype 2, S. suis serotype 7 and S. suis serotype 9 strains were recovered from diseased pigs between 1998 and 2005 in China. Fifteen of seventeen strains of S. suis serotype 2 could be lysed, as well as S. suis serotype 7 and 9, Streptococcus equi ssp. zooepidemicus and Staphylococcus aureus. But E. coli and Salmonella enterica were not affected. Purified LySMP showed high degrading efficiency against PMSF or lysozyme treated cells comparing to PBS washed cells. Optimum pH and temperature conditions for the lysin were investigated by turbidity reduction assay. The lysin exerted efficient lysis activity at 37 degrees C, pH 5.2. The turbidity of bacterium investigated was observed to decrease by 1.2-68% in 30 min. Result indicated that putative LySMP could be a candidate antimicrobial agent in controlling S. suis infection.
引用
收藏
页码:609 / 615
页数:7
相关论文
共 31 条
[1]  
ARENDS JP, 1988, REV INFECT DIS, V10, P131
[2]  
Batas D, 1996, BIOTECHNOL BIOENG, V50, P16
[3]   Removal of group B streptococci colonizing the vagina and oropharynx of mice with a bacteriophage, lytic enzyme [J].
Cheng, Q ;
Nelson, D ;
Zhu, SW ;
Fischetti, VA .
ANTIMICROBIAL AGENTS AND CHEMOTHERAPY, 2005, 49 (01) :111-117
[4]   Mutagenesis of a bacteriophage lytic enzyme PlyGBS significantly increases its antibacterial activity against group B streptococci [J].
Cheng, Qi ;
Fischetti, Vincent A. .
APPLIED MICROBIOLOGY AND BIOTECHNOLOGY, 2007, 74 (06) :1284-1291
[5]   Synergistic killing of streptococcus pneumoniae with the bacteriophage lytic enzyme Cpl-1 and penicillin or gentamicin depends on the level of penicillin resistance [J].
Djurkovic, S ;
Loeffler, JA ;
Fischetti, VA .
ANTIMICROBIAL AGENTS AND CHEMOTHERAPY, 2005, 49 (03) :1225-1228
[6]   LambdaSa2 prophage endolysin requires Cpl-7-binding domains and amidase-5 domain for antimicrobial lysis of streptococci [J].
Donovan, David M. ;
Foster-Frey, Juli .
FEMS MICROBIOLOGY LETTERS, 2008, 287 (01) :22-33
[7]  
ELIZABETH DJ, 1975, J BACTERIOL, V124, P445
[8]   Bacteriophage lytic enzymes: novel anti-infectives [J].
Fischetti, VA .
TRENDS IN MICROBIOLOGY, 2005, 13 (10) :491-496
[9]   The pathogenesis of the meningitis caused by Streptococcus suis:: the unresolved questions [J].
Gottschalk, M ;
Segura, M .
VETERINARY MICROBIOLOGY, 2000, 76 (03) :259-272
[10]   Phage lytic enzyme Cpl-1 for antibacterial therapy in experimental pneumococcal meningitis [J].
Grandgirard, Denis ;
Loeffler, Jutta M. ;
Fischetti, Vincent A. ;
Leib, Stephen L. .
JOURNAL OF INFECTIOUS DISEASES, 2008, 197 (11) :1519-1522