Interestingly, the highly conserved serine threonine-kinase of S. pneumoniae is thus involved in the processes underlying three key features of bacterial physiology and IWR1 evolution: virulence in animals, www.selleckchem.com/screening-libraries.html development of competence for genetic transformation culminating in gene transfers , and susceptibility to penicillin (this work). This makes StkP a potentially promising target in S. pneumoniae for the development of new prophylactic measurements against pneumococcal
disease. Conclusion In summary, the results of the present study suggest that pneumococcal serine-theonine kinase (StkP) is related to penicillin susceptibility, as demonstrated in isogenic strains. However, is a highly conserved protein, not functionally related to the major genetic determinants for penicillin susceptibility in pneumococci, being a promising target for the development of new therapies. Acknowledgements R. Dias
was supported by grant BIC 03.2002 from NIH Dr. Ricardo Jorge and was BGB324 in vivo the recipient of a short-term research fellowship grant from the Fundação Calouste Gulbenkian. The authors thank Tania Arcondeguy for her critical reading of the manuscript and suggestions. Electronic supplementary material Additional file 1: Data Tables. Data tables. This file contains table ST1 for the deduced amino acid substitutions in StkP and related PBP profiles of 50 clinical strains and 6 reference as well as tables ST2, ST3 and ST4 for the deduced amino acid substitutions in PBP2B; PBP2X and PBP1A, respectively, of 25 representative pneumococcal strains. (PDF 358 KB) References 1. Filipe SR, Tomasz A: Inhibition of the expression of penicillin resistance in Streptococcus pneumoniae by inactivation of cell wall muropeptide branching genes. Proc Natl Acad Sci USA 2000, 97:4891–4896.CrossRefPubMed 2. Guenzi E, Gasc AM, Sicard MA, Hakenbeck R: A two-component signal-transducing
system is involved in competence and Rho penicillin susceptibility in laboratory mutants of Streptococcus pneumoniae. Mol Microbiol 1994, 12:505–515.CrossRefPubMed 3. Hakenbeck R, Grebe T, Zahner D, Stock JB: Beta-lactam resistance in Streptococcus pneumoniae : penicillin-binding proteins and non-penicillin-binding proteins. Mol Microbiol 1999, 33:673–678.CrossRefPubMed 4. Mengin-Lecreulx D, van Heijenoort J: Characterization of the essential gene glmM encoding phosphoglucosamine mutase in Escherichia coli. J Biol Chem 1996, 271:32–39.CrossRefPubMed 5. Jolly L, Ferrari P, Blanot D, Van Heijenoort J, Fassy F, Mengin-Lecreulx D: Reaction mechanism of phosphoglucosamine mutase from Escherichia coli. Eur J Biochem 1999, 262:202–210.CrossRefPubMed 6.