Author
Listed:
- Qingshan Luo
(Chinese Academy of Sciences)
- Chengai Wang
(Chinese Academy of Sciences
University of Chinese Academy of Sciences)
- Shuai Qiao
(Chinese Academy of Sciences
University of Chinese Academy of Sciences
Zhejiang University)
- Shan Yu
(Chinese Academy of Sciences)
- Lianwan Chen
(Chinese Academy of Sciences)
- Seonghoon Kim
(Lehigh University)
- Kun Wang
(Nanjing University of Science and Technology
Wenzhou Medical University)
- Jiangge Zheng
(Chinese Academy of Sciences)
- Yong Zhang
(Chinese Academy of Sciences)
- Fan Wu
(Peking University)
- Xiaoguang Lei
(Peking University)
- Jizhong Lou
(University of Chinese Academy of Sciences
Chinese Academy of Sciences)
- Michael Hennig
(Park Innovaare)
- Wonpil Im
(Lehigh University)
- Long Miao
(University of Chinese Academy of Sciences
Chinese Academy of Sciences
Beijing Normal University
Fuyang Normal University)
- Min Zhou
(Nanjing University of Science and Technology)
- Weiwei Bei
(Chinese Academy of Sciences)
- Yihua Huang
(Chinese Academy of Sciences
University of Chinese Academy of Sciences)
Abstract
Lipopolysaccharide (LPS) and lipoprotein, two essential components of the outer membrane (OM) in Gram-negative bacteria, play critical roles in bacterial physiology and pathogenicity. LPS translocation to the OM is mediated by LptDE, yet how lipoproteins sort to the cell surface remains elusive. Here, we identify candidate lipoproteins that may be transported to the cell surface via LptDE. Notably, we determine the crystal structures of LptDE from Pseudomonas aeruginosa and its complex with an endogenous Escherichia coli lipoprotein LptM. The paLptDE-LptM structure demonstrates that LptM may translocate to the OM via LptDE, in a manner similar to LPS transport. The β-barrel domain serves as a passage for the proteinaceous moiety while its acyl chains are transported outside. Our finding has been corroborated by results from native mass spectrometry, immunofluorescence, and photocrosslinking assays, revealing a potential surface exposed lipoproteins (SLPs) transport mechanism through which lipoproteins are loaded into LptA by LolCDE prior to assembly of the LptB2FGCADE complex. These observations provide initial evidence of functional overlap between the Lpt and Lol pathways, potentially broadening current perspectives on lipoprotein sorting.
Suggested Citation
Qingshan Luo & Chengai Wang & Shuai Qiao & Shan Yu & Lianwan Chen & Seonghoon Kim & Kun Wang & Jiangge Zheng & Yong Zhang & Fan Wu & Xiaoguang Lei & Jizhong Lou & Michael Hennig & Wonpil Im & Long Mia, 2025.
"Surface lipoprotein sorting by crosstalk between Lpt and Lol pathways in gram-negative bacteria,"
Nature Communications, Nature, vol. 16(1), pages 1-14, December.
Handle:
RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-59660-y
DOI: 10.1038/s41467-025-59660-y
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