期刊
BIOPHYSICAL JOURNAL
卷 107, 期 5, 页码 1082-1089出版社
CELL PRESS
DOI: 10.1016/j.bpj.2014.07.029
关键词
-
类别
资金
- Fundacao para a Ciencia e Tecnologia [PEst-OE/EQB/LA0004/2011, PTDC/BIA-MTC/099151/2008]
- European Research Council [ERC-2012-StG-310987]
- P.M.P. [SFRH/BD/41119/2007]
- Federal Ministry of Education and Research (Germany) [01K11301B]
- Deutsche Forschungsgemeinschaft [SFB 1027, GRK 1276, INST 256/305-1 FUGG]
- [EMBO ASTF 427-2011]
We have used atomic-force microscopy (AFM) to probe the effect of peptidoglycan crosslinking reduction on the elasticity of the Staphylococcus aureus cell wall, which is of particular interest as a target for antimicrobial chemotherapy. Penicillin-binding protein 4 (PBP4) is a nonessential transpeptidase, required for the high levels of peptidoglycan crosslinking characteristic of S. aureus. Importantly, this protein is essential for beta-lactam resistance in community-acquired, methicillin-resistant S. aureus (MRSA) strains but not in hospital-acquired MRSA strains. Using AFM in a new mode for recording force/distance curves, we observed that the absence of PBP4, and the concomitant reduction of the peptidoglycan crosslinking, resulted in a reduction in stiffness of the S. aureus cell wall. Importantly, the reduction in cell wall stiffness in the absence of PBP4 was observed both in community-acquired and hospital-acquired MRSA strains, indicating that high levels of peptidoglycan crosslinking modulate the overall structure and mechanical properties of the S. aureus cell envelope in both types of clinically relevant strains. Additionally, we were able to show that the applied method enables the separation of cell wall properties and turgor pressure.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据