Proteomic Analysis of Therapeutically Important Bacteriophage 812 by Combination of Electrophoresis and Mass Spectrometry
| Autoři | |
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| Rok publikování | 2003 |
| Druh | Článek ve sborníku |
| Konference | Proceedings of the 51st Annual Conference on Mass Spectrometry and Allied Topics |
| Fakulta / Pracoviště MU | |
| Citace | |
| Obor | Genetika a molekulární biologie |
| Klíčová slova | MALDI; staphylococcal bacteriophage; proteome |
| Popis | The alarming increase in antibiotic-resistant bacteria has renewed interest in bacteriophage therapy of various human infections, such as postoperative staphylococcal wound infections or anthrax. Genetic engineering has been previously applied for obtaining phage mutants with the desired host specificity. However, the genomic sequence similarity of the different phages is generally low, and identification of proteins with the same function in various phages based solely on the DNA sequence is often impossible. Furthermore, amino acid modifications, such as variants and post-translational modifications of the predicted proteins cannot be deduced from the DNA sequence. In this work, we propose new approaches to the analysis of the phage proteins, especially low abundant proteins, such as lytic enzymes. SDS gel electrophoresis was used for the protein separation followed by tryptic digestion and ESI or MALDI analysis. Additionally, protein and peptide separations were performed with capillary electrophoresis (CE) and a new universal interface has been developed to couple CE with MALDI MS. |
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