Affinity of Ceftobiprole for Penicillin-Binding Protein 2b in Streptococcus pneumoniae Strains with Various Susceptibilities to Penicillin
2010 ◽
Vol 54
(10)
◽
pp. 4510-4512
◽
Keyword(s):
ABSTRACT Wild-type penicillin-binding protein (PBP) 2b from penicillin-susceptible Streptococcus pneumoniae had high affinity for ceftobiprole and penicillin (50% inhibitory concentrations [IC50s] of ≤0.15 μg/ml) but not ceftriaxone (IC50 of >8 μg/ml). In clinical isolates, ceftobiprole and PBP 2b affinities were reduced 15- to 30-fold with a Thr-446-Ala substitution and further still with an additional Ala-619-Gly PBP 2b substitution. Ceftobiprole remained active (MICs of ≤1 μg/ml) against all strains tested and behaved more like penicillin than ceftriaxone with respect to PBP 2b binding.
2002 ◽
Vol 46
(12)
◽
pp. 3744-3749
◽
1989 ◽
Vol 86
(22)
◽
pp. 8842-8846
◽
2006 ◽
Vol 50
(7)
◽
pp. 2530-2532
◽
2004 ◽
Vol 48
(6)
◽
pp. 2244-2250
◽
2007 ◽
Vol 51
(9)
◽
pp. 3404-3406
◽
2006 ◽
Vol 50
(11)
◽
pp. 3638-3645
◽
1992 ◽
Vol 11
(11)
◽
pp. 3831-3836
◽
2014 ◽
Vol 58
(7)
◽
pp. 3934-3941
◽
2003 ◽
pp. 245-264
◽