Gene Review:
pbpX - penicillin-binding protein 2X
Streptococcus pneumoniae R6
- Nucleotide sequences of the pbpX genes encoding the penicillin-binding proteins 2x from Streptococcus pneumoniae R6 and a cefotaxime-resistant mutant, C506. Laible, G., Hakenbeck, R., Sicard, M.A., Joris, B., Ghuysen, J.M. Mol. Microbiol. (1989)
- Mosaic pbpX genes of major clones of penicillin-resistant Streptococcus pneumoniae have evolved from pbpX genes of a penicillin-sensitive Streptococcus oralis. Sibold, C., Henrichsen, J., König, A., Martin, C., Chalkley, L., Hakenbeck, R. Mol. Microbiol. (1994)
- Penicillin-binding protein 2x of Streptococcus pneumoniae. Expression in Escherichia coli and purification of a soluble enzymatically active derivative. Laible, G., Keck, W., Lurz, R., Mottl, H., Frère, J.M., Jamin, M., Hakenbeck, R. Eur. J. Biochem. (1992)
- Pneumococcal beta-lactam resistance due to a conformational change in penicillin-binding protein 2x. Carapito, R., Chesnel, L., Vernet, T., Zapun, A. J. Biol. Chem. (2006)
- Kinetics of beta-lactam interactions with penicillin-susceptible and -resistant penicillin-binding protein 2x proteins from Streptococcus pneumoniae. Involvement of acylation and deacylation in beta-lactam resistance. Lu, W.P., Kincaid, E., Sun, Y., Bauer, M.D. J. Biol. Chem. (2001)
- Mutations in the active site of penicillin-binding protein PBP2x from Streptococcus pneumoniae. Role in the specificity for beta-lactam antibiotics. Mouz, N., Di Guilmi, A.M., Gordon, E., Hakenbeck, R., Dideberg, O., Vernet, T. J. Biol. Chem. (1999)
- Diversity of substitutions within or adjacent to conserved amino acid motifs of penicillin-binding protein 2X in cephalosporin-resistant Streptococcus pneumoniae isolates. Asahi, Y., Takeuchi, Y., Ubukata, K. Antimicrob. Agents Chemother. (1999)
- Complex relationship between acquisition of beta-lactam resistance and loss of virulence in Streptococcus pneumoniae. Rieux, V., Carbon, C., Azoulay-Dupuis, E. J. Infect. Dis. (2001)
- The crystal structure of the penicillin-binding protein 2x from Streptococcus pneumoniae and its acyl-enzyme form: implication in drug resistance. Gordon, E., Mouz, N., Duée, E., Dideberg, O. J. Mol. Biol. (2000)
- Activities of ceftobiprole and other beta-lactams against Streptococcus pneumoniae clinical isolates from the United States with defined substitutions in penicillin-binding proteins PBP 1a, PBP 2b, and PBP 2x. Davies, T.A., Shang, W., Bush, K. Antimicrob. Agents Chemother. (2006)
- Amino acid mutations essential to production of an altered PBP 2X conferring high-level beta-lactam resistance in a clinical isolate of Streptococcus pneumoniae. Smith, A.M., Klugman, K.P. Antimicrob. Agents Chemother. (2005)
- Deacylation kinetics analysis of Streptococcus pneumoniae penicillin-binding protein 2x mutants resistant to beta-lactam antibiotics using electrospray ionization- mass spectrometry. Di Guilmi, A.M., Mouz, N., Pétillot, Y., Forest, E., Dideberg, O., Vernet, T. Anal. Biochem. (2000)