Penicillin-binding proteins regulate multiple steps in the polarized cell division process of Chlamydia

Penicillin-binding proteins regulate multiple steps in the polarized cell division process of Chlamydia
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DOI:
10.1038/s41598-020-69397-x
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发表时间:
2020-07-28
期刊:
影响因子:
4.6
通讯作者:
Ouellette, Scot P.
Ouellette, Scot P.
中科院分区:
综合性期刊3区
文献类型:
--
作者:
Cox, John, V;Abdelrahman, Yasser Mohamed;Ouellette, Scot P.

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不表达FtsZ的沙眼衣原体L2和小鼠衣原体经历了极化的细胞分裂。在分裂过程中,肽聚糖聚集在沙眼衣原体细胞分裂的极点,在那里发生子细胞形成,并且在沙眼衣原体和沙眼衣原体的极化分裂中,肽聚糖至少调节两个不同的步骤。用阻止青霉素结合蛋白2(PBP2)合成或交联肽多糖的抑制剂处理的细胞不能启动极化分裂,而用阻止青霉素结合蛋白3(PBP3/FTSI)交联肽聚糖的抑制剂处理的细胞启动极化分裂,但这一过程在子细胞生长的早期停止。与它们在极化分裂中的不同作用相一致,在PBP2和PBP3特异性抑制剂处理的细胞中,肽聚糖的组织是不同的。我们的分析表明,PBP2和PBP3的顺序作用驱动肽聚糖组织的变化,这对于这些专性细胞内细菌的极化分裂是必不可少的。此外,我们已经表征的PBP2和PBP3在调节衣原体细胞分裂的特定步骤中的作用还没有在其他细菌中描述。
Chlamydia trachomatis serovar L2 and Chlamydia muridarum, which do not express FtsZ, undergo polarized cell division. During division, peptidoglycan assembles at the pole of dividing Chlamydia trachomatis cells where daughter cell formation occurs, and peptidoglycan regulates at least two distinct steps in the polarized division of Chlamydia trachomatis and Chlamydia muridarum. Cells treated with inhibitors that prevent peptidoglycan synthesis or peptidoglycan crosslinking by penicillin-binding protein 2 (PBP2) are unable to initiate polarized division, while cells treated with inhibitors that prevent peptidoglycan crosslinking by penicillin-binding protein 3 (PBP3/FtsI) initiate polarized division, but the process arrests at an early stage of daughter cell growth. Consistent with their distinct roles in polarized division, peptidoglycan organization is different in cells treated with PBP2 and PBP3-specific inhibitors. Our analyses indicate that the sequential action of PBP2 and PBP3 drives changes in peptidoglycan organization that are essential for the polarized division of these obligate intracellular bacteria. Furthermore, the roles we have characterized for PBP2 and PBP3 in regulating specific steps in chlamydial cell division have not been described in other bacteria.