DOŠKAŘ, Jiří, Luděk EYER, Roman PANTŮČEK, Vladislava RŮŽIČKOVÁ, Hana KONEČNÁ, Zbyněk ZDRÁHAL, Lenka HERNYCHOVÁ and Jan PREISLER. Proteomic characterization of the polyvalent staphylophage 812. In 12th International Symposium on Staphylococci & Staphylococcal Infections. 2006.
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Basic information
Original name Proteomic characterization of the polyvalent staphylophage 812
Name in Czech Proteomic characterization of the polyvalent staphylophage 812
Authors DOŠKAŘ, Jiří (203 Czech Republic, guarantor), Luděk EYER (203 Czech Republic), Roman PANTŮČEK (203 Czech Republic), Vladislava RŮŽIČKOVÁ (203 Czech Republic), Hana KONEČNÁ (203 Czech Republic), Zbyněk ZDRÁHAL (203 Czech Republic), Lenka HERNYCHOVÁ (203 Czech Republic) and Jan PREISLER (203 Czech Republic).
Edition 12th International Symposium on Staphylococci & Staphylococcal Infections, 2006.
Other information
Original language English
Type of outcome Conference abstract
Field of Study Genetics and molecular biology
Country of publisher Netherlands
Confidentiality degree is not subject to a state or trade secret
RIV identification code RIV/00216224:14310/06:00015836
Organization unit Faculty of Science
Keywords in English Staphylococcus aureus; medical microbiology; molecular diagnostics; phage therapy; proteomics
Tags medical microbiology, Molecular diagnostics, phage therapy, proteomics, Staphylococcus aureus
Tags International impact, Reviewed
Changed by Changed by: prof. Mgr. Jan Preisler, Ph.D., učo 45329. Changed: 8/4/2010 10:15.
Bacteriophage 812 is a polyvalent phage with very broad host range in the genus Staphylococcus, which makes it a suitable candidate for phage therapy of staphylococcal infections. The genomes of polyvalent staphylococcal phages exceed 125 kbp and include about 200 putative open reading frames. Our study was focused on characterization of the phage proteome, especially on identification of phage virion proteins. Combination of both one- and two-dimensional electrophoreses (1-DE and 2-DE) followed by peptide mass fingerprinting using MALDI-TOF mass spectrometry, led to the identification of 24 virion proteins of the phage 812. Twenty of them were not identified by proteome analysis of closely related staphylococcal phages K and G1 yet. Although the phage proteome is much simpler compared to that of cellular organisms, using 2-DE in addition to 1-DE significantly increased the number of identified proteins. Fifteen proteins were assigned unambiguously to the head-tail genome module; the remaining nine proteins are encoded by genes of the left or right arms of the phage genome. As expected, the most abundant proteins in the electrophoretic patterns are the major capsid protein, the major tail sheath protein and proteins identical to ORF 50 and ORF 95 of the phage K, although their function is only putative. Twenty new identified proteins set the basis for a detailed analysis of the phage virion structure and are a prerequisite for their efficient and safe application in phage therapy.
Abstract (in Czech)
GA203/03/0515, research and development projectName: Integrovaná analýza genomu a proteomu terapeuticky významných bakteriofágů kombinací elektroforézy a hmotnostní spektrometrie
Investor: Czech Science Foundation, Standard Projects
MSM0021622415, plan (intention)Name: Molekulární podstata buněčných a tkáňových regulací
Investor: Ministry of Education, Youth and Sports of the CR, Research Intents
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