Alterations of penicillin-binding proteins 1A, 2X, and 2B in Streptococcus pneumoniae isolates for which amoxicillin MICs are higher than penicillin MICs

被引：39

作者：

Kosowska, K

Jacobs, MR

Bajaksouzian, S

Koeth, L

Appelbaum, PC

机构：

[1] Lab Specialists Inc, Westlake, OH 44145 USA

[2] Milton S Hershey Med Ctr, Hershey, PA USA

[3] Case Western Reserve Univ, Cleveland, OH 44106 USA

来源：

ANTIMICROBIAL AGENTS AND CHEMOTHERAPY | 2004年 / 48卷 / 10期

关键词：

D O I：

10.1128/AAC.48.10.4020-4022.2004

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Penicillin-binding proteins (PBPs) of 15 selected penicillin- and amoxicillin-resistant Streptococcus pneumoniae isolates (MICs of 2 to 8 and 8 to 16 mug/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.

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页码：4020 / 4022

页数：3

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