BENEŠÍK, Martin, Jiří NOVÁČEK, Lubomír JANDA, Radka DOPITOVÁ, Lukáš ŽÍDEK, Jiří DOŠKAŘ, Vladislava RŮŽIČKOVÁ, Marek MOŠA and Roman PANTŮČEK. SH3b cell wall binding domain of bacteriophage 812 endolysin: Cloning, expression and structure determination. In Viruses of Microbes. From exploration to applications in the -omics era. EMBO Conference Series, Brussels, Belgium. 2012.
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Basic information
Original name SH3b cell wall binding domain of bacteriophage 812 endolysin: Cloning, expression and structure determination
Authors BENEŠÍK, Martin, Jiří NOVÁČEK, Lubomír JANDA, Radka DOPITOVÁ, Lukáš ŽÍDEK, Jiří DOŠKAŘ, Vladislava RŮŽIČKOVÁ, Marek MOŠA and Roman PANTŮČEK.
Edition Viruses of Microbes. From exploration to applications in the -omics era. EMBO Conference Series, Brussels, Belgium, 2012.
Other information
Original language English
Type of outcome Conference abstract
Field of Study Genetics and molecular biology
Country of publisher Belgium
Confidentiality degree is not subject to a state or trade secret
WWW URL
Organization unit Faculty of Science
Keywords in English Staphylococcus; bacteriophage; Myoviridae; endolysin; SH3b domain; NMR
Tags International impact, Reviewed
Changed by Changed by: prof. RNDr. Roman Pantůček, Ph.D., učo 842. Changed: 22/11/2012 11:34.
Abstract
Staphylococcus aureus is a major causative agent of human and animal diseases. The increasing number of pathogenic strains resistant to antimicrobial drugs is a serious public health problem that can be solved by applications of phage therapy as a suitable alternative to antibiotics treatment. Currently the research focus on the phage encoded antimicrobial proteins applicable to combat bacterial infections, such as phage endolysins that digest the cell wall of bacteria. In this study we focused on endolysin of staphylococcal bacteriophage 812, a member of SPO1-like viruses from family Myoviridae. Preliminary results of the NMR analysis confirmed the presence of the well defined structure of the studied construct, and provided the sequential assignment of all resonance frequencies along the peptide backbone allowing us to assess the presence of the secondary structure motifs.
Links
TA01010405, research and development projectName: Výzkum stafylokokových bakteriofágových mutant s širokým spektrem hostitelů (Acronym: TAČR/IMUNA-1)
Investor: Technology Agency of the Czech Republic
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