Alterations of penicillin-binding proteins 1A, 2X, and 2B in Streptococcus pneumoniae isolates for which amoxicillin MICs are higher than penicillin MICs.
Penicillin-binding proteins (PBPs) of 15 selected penicillin- and amoxicillin-resistant Streptococcus pneumoniae isolates (MICs of 2 to 8 and 8 to 16 microg/ml, respectively) were studied. In addition to typical changes in PBPs 1A and 2X, these strains had 10 unique changes in PBP 2B, including a (618)A-G substitution, which may be the key alteration associated with amoxicillin resistance.
Kosowska
K
K
Laboratory Specialists, Inc., 1651 A Crossings Parkway, Westlake, OH 44145, USA.
Jacobs
M R
MR
Bajaksouzian
S
S
Koeth
L
L
Appelbaum
P C
PC
D000658:Amoxicillin / Q000494:pharmacology*; D017931:DNA Primers; D008826:Microbial Sensitivity Tests; D046915:Penicillin-Binding Proteins / Q000737:chemistry / Q000378:metabolism*; D010406:Penicillins / Q000494:pharmacology*; D011008:Pneumococcal Infections / Q000382:microbiology; D011159:Population Surveillance; D020133:Reverse Transcriptase Polymerase Chain Reaction; D013296:Streptococcus pneumoniae / Q000187:drug effects* / Q000378:metabolism
D017931:DNA Primers; D046915:Penicillin-Binding Proteins; D010406:Penicillins; D000658:Amoxicillin