[en] Although the rate of acylation of a penicillin-resistant form of Streptococcus pneumoniae PBP2x by ceftaroline is 80-fold lower than that of its penicillin-sensitive counterpart, it remains sufficiently high (k(2)/K = 12600 M(-1)s(-1)) to explain the sensitivity of the penicillin-resistant strain to this new cephalosporin. Surprisingly, the Actinomadura R39 DD-peptidase is not very sensitive to ceftaroline.
Research center :
GIGA CRC (Cyclotron Research Center) In vivo Imaging-Aging & Memory - ULiège CIP - Centre d'Ingénierie des Protéines - ULiège
Sader HS, Fritsche TR, Kaniga K, Ge Y, Jones RN. 2005. Antimicrobial activity and spectrum of PPI-0903M (T-91825), a novel cephalosporin, tested against a worldwide collection of clinical strains. Antimicrob. Agents Chemother. 49:3501-3512.
Hakenbeck R, Balmelle N, Weber B, Gardes C, Keck W, de Saizieu A. 2001. Mosaic genes and mosaic chromosomes: intra- and interspecies genomic variation of Streptococcus pneumoniae. Infect. Immun. 69:2477-2486.
Laible G, Spratt BG, Hakenbeck R. 1991. Interspecies recombinational events during the evolution of altered PBP 2x genes in penicillin-resistant clinical isolates of Streptococcus pneumoniae. Mol. Microbiol. 5 :1993-2002.
Munoz R, Dowson CG, Daniels M, Coffey TJ, Martin C, Hakenbeck R, Spratt BG. 1992. Genetics of resistance to third-generation cephalosporins in clinical isolates of Streptococcus pneumoniae. Mol. Microbiol. 6:2461-2465.
Kosowska-Shick K, McGhee PL, Appelbaum PC. 2010. Affinity of ceftaroline and other β-lactams for penicillin-binding proteins from Staphylococcus aureus and Streptococcus pneumoniae. Antimicrob. Agents Chemother. 54:1670-1677.
Carapito R, Chesnel L, Vernet T, Zapun A. 2006. Pneumococcal β-lactam resistance due to a conformational change in penicillin-binding protein 2x. J. Biol. Chem. 281:1771-1777.
Granier B, Jamin M, Adam M, Galleni M, Lakaye I, Zorzi W, Grandchamps J, Wilkin J-M, Fraipont C, Joris B, Duez C, Nguyen-Disteche M, Coyetteme J, Leyh-Bouille L, Dusart J, Christiaens L, Frere J-M, Ghuysen J-M. 1994. Serine-type D-Ala-D-Ala peptidases and penicillin-binding proteins. Methods Enzymol. 244:249-266.
Mouz N, Gordon E, Di Guilmi AM, Petit I, Petillot Y, Dupont Y, Hakenbeck R, Vernet T, Dideberg O. 1998. Identification of a structural determinant for resistance to beta-lactam antibiotics in Gram-positive bacteria. Proc. Natl. Acad. Sci. U. S. A. 95:13403-13406.
De Meester F, Joris B, Reckinger G, Bellefroid-Bourguignon C, Frère J-M, Waley SG. 1987. Automated analysis of enzyme inactivation phenomena: application to β-lactamases and DD-peptidases. Biochem. Pharmacol. 36:2393-2403.
Frère J-M, Nguyen-Disteche M, Coyette J, Joris B. 1992. Mode of action: interaction with penicillin binding proteins, p 148-195. In Page M (ed), The chemistry of beta-lactams. Chapman and Hall, Glasgow, Scotland.
Macheboeuf P, Fischer DS, Brown T, Jr, Zervosen A, Luxen A, Joris B, Dessen A, Schofield CJ. 2007. Structural and mechanistic basis of penicillin-binding protein inhibition by lactivicins. Nat. Chem. Biol. 3:565-569.
Sauvage E, Zervosen A, Dive G, Herman R, Amoroso A, Joris B, Fonze E, Pratt RF, Luxen A, Charlier P, Kerff F. 2009. Structural basis of the inhibition of class A β-lactamases and penicillin-binding proteins by 6-β-iodopenicillanate. J. Am. Chem. Soc. 131:15262-15269.
Jamin M, Damblon C, Millier S, Hakenbeck R, Frere JM. 1993. Penicillin-binding protein 2x of Streptococcus pneumoniae: enzymic activities and interactions with beta-lactams. Biochem. J. 292(Part 3):735-741.
Jamin M, Hakenbeck R, Frere JM. 1993. Penicillin binding protein 2x as a major contributor to intrinsic beta-lactam resistance of Streptococcus pneumoniae. FEBS Lett. 331:101-104.
Lassaux P, Traore DA, Loisel E, Favier A, Docquier JD, Sohier JS, Laurent C, Bebrone C, Frere JM, Ferrer JL, Galleni M. 2011. Biochemical and structural characterization of the subclass B1 metallo-β-lactamase VIM-4. Antimicrob. Agents Chemother. 55:1248-1255.
Zervosen A, Bouillez A, Herman A, Amoroso A, Joris B, Sauvage E, Charlier P, Luxen A. 2012. Synthesis and evaluation of boronic acids as inhibitors of penicillin binding proteins of classes A, B and C. Bioorg. Med. Chem. 20:3915-3924.
Lu WP, Kincaid E, Sun Y, Bauer MD. 2001. 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. J. Biol. Chem. 276:31494-31501.
Chesnel L, Carapito R, Croize J, Dideberg O, Vernet T, Zapun A. 2005. Identical penicillin-binding domains in penicillin-binding proteins of Streptococcus pneumoniae clinical isolates with different levels of beta-lactam resistance. Antimicrob. Agents Chemother. 49:2895-2902.
