Evidence map›Paper›PMID 40348743›Full record

ArticleNature communications2025

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 and 8 more

Abstract read
In one paragraph

Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

11 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Identification and characterization of the functional LolB ortholog inbioRxiv : the preprint server for biology · 2026
    Article
  6. Article
  7. Small siphophage binding to an open state of the LptDE outer membrane lipopolysaccharide translocon.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Article
  9. Review
  10. Review
  11. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

18 authors.

Qingshan Luo *National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China.ORCID http://orcid.org/0000-0002-2849-0123
Chengai Wang *National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China.
Shuai Qiao *National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China.
Shan Yu *National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China.
Lianwan ChenNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China.
Seonghoon KimDepartments of Biological Sciences and Bioengineering, Lehigh University, Bethlehem, PA, USA.ORCID http://orcid.org/0000-0002-0050-1054
Kun WangInstitute of Bio-analytical Chemistry, School of Chemical Engineering, Nanjing University of Science and Technology, No.200 Xiao Ling Wei Street, Nanjing, 210094, China.ORCID http://orcid.org/0000-0001-9636-9264
Jiangge ZhengNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China.
Yong ZhangKey Laboratory of RNA Biology, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China.
Fan WuSynthetic and Functional Biomolecules Center, Beijing National Laboratory for Molecular Sciences, Key Laboratory of Bioorganic Chemistry and Molecular Engineering of Ministry of Education, Peking University, Beijing, 100871, China.
Xiaoguang LeiSynthetic and Functional Biomolecules Center, Beijing National Laboratory for Molecular Sciences, Key Laboratory of Bioorganic Chemistry and Molecular Engineering of Ministry of Education, Peking University, Beijing, 100871, China.ORCID http://orcid.org/0000-0002-0380-8035
Jizhong LouUniversity of Chinese Academy of Sciences, Beijing, 100101, China.ORCID http://orcid.org/0000-0003-4031-6125
Michael HennigleadXpro AG, Park Innovaare, Villigen, Switzerland.ORCID http://orcid.org/0000-0002-1839-2351
Wonpil ImDepartments of Biological Sciences and Bioengineering, Lehigh University, Bethlehem, PA, USA.ORCID http://orcid.org/0000-0001-5642-6041
Long MiaoUniversity of Chinese Academy of Sciences, Beijing, 100101, China.
Min ZhouInstitute of Bio-analytical Chemistry, School of Chemical Engineering, Nanjing University of Science and Technology, No.200 Xiao Ling Wei Street, Nanjing, 210094, China. minzhou@njust.edu.cn.
Weiwei BeiNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China. wwbei1990@ibp.ac.cn.ORCID http://orcid.org/0009-0005-6744-5340
Yihua HuangNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China. yihuahuang@sun5.ibp.ac.cn.ORCID http://orcid.org/0000-0001-5910-5972

Funding

Ministry of Science and Technology of the People's Republic of China (Chinese Ministry of Science and Technology) 2021YFF0700201National Science Foundation (NSF) MCB-1727508 and MCB-1810695
6 · The paper itself

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 LptB

Indexed as

Bacterial Outer Membrane ProteinsEscherichia coliEscherichia coli ProteinsGram-Negative BacteriaLipoproteinsPseudomonas aeruginosaATP-Binding Cassette TransportersCrystallography, X-RayLipopolysaccharidesModels, MolecularProtein TransportATP-Binding Cassette TransportersBacterial Outer Membrane ProteinsEscherichia coli ProteinsLipopolysaccharidesLipoproteinsLolC protein, E coli

Identifiers

PMID40348743
PMCPMC12065857

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.