Surface lipoprotein sorting by crosstalk between Lpt and Lol pathways in gram-negative bacteria

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 Miao, Min Zhou (), Weiwei Bei () and Yihua Huang ()
Additional contact information
Qingshan Luo: Chinese Academy of Sciences
Chengai Wang: Chinese Academy of Sciences
Shuai Qiao: Chinese Academy of Sciences
Shan Yu: Chinese Academy of Sciences
Lianwan Chen: Chinese Academy of Sciences
Seonghoon Kim: Lehigh University
Kun Wang: Nanjing University of Science and Technology
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
Michael Hennig: Park Innovaare
Wonpil Im: Lehigh University
Long Miao: University of Chinese Academy of Sciences
Min Zhou: Nanjing University of Science and Technology
Weiwei Bei: Chinese Academy of Sciences
Yihua Huang: Chinese Academy of Sciences

Nature Communications, 2025, vol. 16, issue 1, 1-14

Abstract: 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.

Date: 2025
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DOI: 10.1038/s41467-025-59660-y

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