| Literature DB >> 19401597 |
Francesco Doro1, Sabrina Liberatori, Manuel J Rodríguez-Ortega, Cira D Rinaudo, Roberto Rosini, Marirosa Mora, Maria Scarselli, Emrah Altindis, Romina D'Aurizio, Maria Stella, Immaculada Margarit, Domenico Maione, John L Telford, Nathalie Norais, Guido Grandi.
Abstract
Safe recombinant vaccines, based on a small number of antigenic proteins, are emerging as the most attractive, cost-effective solution against infectious diseases. In the present work, we confirmed previous data from our laboratory showing that whole viable bacterial cell treatment with proteases followed by the identification of released peptides by mass spectrometry is the method of choice for the rapid and reliable identification of vaccine candidates in Gram-positive bacteria. When applied to the Group B Streptococcus COH1 strain, 43 surface-associated proteins were identified, including all the protective antigens described in the literature as well as a new protective antigen, the cell wall-anchored protein SAN_1485 belonging to the serine-rich repeat protein family. This strategy overcomes the difficulties so far encountered in the identification of novel vaccine candidates and speeds up the entire vaccine discovery process by reducing the number of recombinant proteins to be tested in the animal model.Entities:
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Year: 2009 PMID: 19401597 PMCID: PMC2709197 DOI: 10.1074/mcp.M800486-MCP200
Source DB: PubMed Journal: Mol Cell Proteomics ISSN: 1535-9476 Impact factor: 5.911