Endolysin from Giant Bacteriophage Disrupts B. anthracis
نویسندگان
چکیده
منابع مشابه
A bacteriophage endolysin that eliminates intracellular streptococci
PlyC, a bacteriophage-encoded endolysin, lyses Streptococcus pyogenes (Spy) on contact. Here, we demonstrate that PlyC is a potent agent for controlling intracellular Spy that often underlies refractory infections. We show that the PlyC holoenzyme, mediated by its PlyCB subunit, crosses epithelial cell membranes and clears intracellular Spy in a dose-dependent manner. Quantitative studies using...
متن کاملA novel endolysin disrupts Streptococcus suis with high efficiency.
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 ...
متن کاملMutant of Lambda Bacteriophage Producing a Thermolabile Endolysin.
Campbell, Allan (University of Rochester, Rochester, N.Y.) and Alice del Campillo-Campbell. Mutant of lambda bacteriophage producing a thermolabile endolysin. J. Bacteriol. 85:1202-1207. 1963.-Endolysin from lambda bacteriophage and a temperature-sensitive mutant thereof was partially purified. The mutant enzyme was distinguishable from the wild type by its greater rate of inactivation by high ...
متن کاملAntimicrobial Activity of Bacteriophage Endolysin Produced in Nicotiana benthamiana Plants.
The increasing spread of antibiotic-resistant pathogens has raised the interest in alternative antimicrobial treatments. In our study, the functionally active gram-negative bacterium bacteriophage CP933 endolysin was produced in Nicotiana benthamiana plants by a combination of transient expression and vacuole targeting strategies, and its antimicrobial activity was investigated. Expression of t...
متن کاملLysis of staphylococcal mastitis pathogens by bacteriophage phi11 endolysin.
The Staphylococcus aureus bacteriophage phi11 endolysin has two peptidoglycan hydrolase domains (endopeptidase and amidase) and an SH3b cell wall-binding domain. In turbidity reduction assays, the purified protein can lyse untreated staphylococcal mastitis pathogens, Staphylococcus aureus and coagulase-negative staphylococci (Staphylococcus chronogenes, Staphylococcus epidermidis, Staphylococcu...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Microbe Magazine
سال: 2014
ISSN: 1558-7452,1558-7460
DOI: 10.1128/microbe.9.186.1