Proteomic characterization of the polyvalent staphylophage 812
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| Year of publication | 2006 |
| Type | Conference abstract |
| MU Faculty or unit | |
| Citation | |
| Description | 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. |
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