Inhibition of Streptococcus pneumoniae penicillin-binding protein 2x and Actinomadura R39 DD-peptidase activities by ceftaroline.

Astrid Zervosen 1 André Zapun 2 Jean-Marie Frère
1 Centre de Recherches du Cyclotron
2 IBS - UMR 5075 - Institut de biologie structurale
Abstract : Although the rate of acylation of a penicillin-resistant form of Streptococcus pneumoniae penicillin-binding protein 2x (PBP2x) by ceftaroline is 80-fold lower than that of its penicillin-sensitive counterpart, it remains sufficiently high (k(2)/K = 12,600 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.
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Antimicrobial Agents and Chemotherapy, American Society for Microbiology, 2013, 57 (1), pp.661-3
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http://hal.univ-grenoble-alpes.fr/hal-01322362
Contributeur : Frank Thomas <>
Soumis le : vendredi 27 mai 2016 - 09:57:28
Dernière modification le : lundi 11 février 2019 - 16:51:29

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Astrid Zervosen, André Zapun, Jean-Marie Frère. Inhibition of Streptococcus pneumoniae penicillin-binding protein 2x and Actinomadura R39 DD-peptidase activities by ceftaroline.. Antimicrobial Agents and Chemotherapy, American Society for Microbiology, 2013, 57 (1), pp.661-3. 〈hal-01322362〉

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