Deletion of PBP1a/LpoA complex compromises cell envelope integrity in Shewanella oneidensis

作者：Yin, Jianhua; Cai, Jingxiao; Yuan, Zhe; Wang, Zhewei; Gao, Haichun; Qiu, Juanping; Yu, Zhiliang^*

来源：FEMS Microbiology Letters, 2018, 365(12): fny128.

DOI：10.1093/femsle/fny128

• Shewanella oneidensis
• penicillin-binding protein
• outer membrane lipoprotein
• peptidoglycan
• envelope integrity
• outer membrane permeability

High molecular weight penicillin-binding proteins (PBPs) are responsible for the biosynthesis of peptidoglycan. In Escherichia coli, PBP1a and PBP1b form multienzyme peptidoglycan-synthesizing complexes with outer membrane lipoproteins LpoA and LpoB, respectively. The two complexes appear to be largely redundant, although their distinct physiological roles remain unclear. PBP1a/LpoA and PBP1b/LpoB also exist in Shewanella oneidensis strain MR-1, but effects of the two complexes on aerobic growth and beta-lactam resistance are quite different. In this study, the phenotypes of strains lacking a certain complex in S. oneidensis were compared. Deletion of PBP1a/LpoA caused aberrant cell morphology (including branches and bulges), enhanced sensitivity to various envelope stresses and outer membrane permeability. On the contrary, strains lacking PBP1b/LpoB displayed phenotypes similar to the wild type.

• 出版日期2018-6
• 单位浙江大学; 浙江工业大学