ArticlemBio2016
Identification of a New Lipoprotein Export Signal in Gram-Negative Bacteria.
Article in mBio, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 35 papers.
What it found
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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.
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.
Who cites it
35 citing papers in PubMed, 47 citations in OpenAlex.
- A standardized toolkit for programmable protein secretion and surface display inbioRxiv : the preprint server for biology · 2026Article
- Structural basis of iron piracy by human gutProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Identification of a LolB-like protein in Porphyromonas gingivalis reveals selective LolA-LolB pairing.Scientific reports · 2026Article
- Co-opting the bacterial lipoprotein pathway for the biosynthesis of lipidated macrocyclic peptides.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Identification and characterization of the functional LolB ortholog inbioRxiv : the preprint server for biology · 2026Article
- Article
- Fructan utilization by members of marine Gammaproteobacteria involves SusC/D-like proteins.The ISME journal · 2026Article
- Glycoside hydrolase-mediated glucomannan catabolism inProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Lessons from the model gut BacteroidalesJournal of bacteriology · 2025Review
- Bam complex redefined in Bacteroidota.Nature microbiology · 2025Article
- Structure of a distinct β-barrel assembly machinery complex in the Bacteroidota.Nature microbiology · 2025Article
- DNA-utilization loci enable exogenous DNA metabolism in gut Bacteroidales.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Surface protein machineries in Gram-negative bacteria.Journal of cell science · 2025Review
- The Type II Secretion System Utilizes AsmA-like Protein GspN to Facilitate Transport of Lipoproteins to the Cell Surface inbioRxiv : the preprint server for biology · 2025Article
- TamL is a Key Player of the Outer Membrane Homeostasis in Bacteroidota.Journal of molecular biology · 2025Article
- LolA and LolB are conserved in Bacteroidota and are crucial for gliding motility and Type IX secretion.Communications biology · 2025Article
- Dual membrane-spanning anti-sigma factors regulate vesiculation inProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Differential temporal release and lipoprotein loading in B. thetaiotaomicron bacterial extracellular vesicles.Journal of extracellular vesicles · 2024Article
- A molecular toolkit for heterologous protein secretion acrossbioRxiv : the preprint server for biology · 2023Article
- Iron acquisition by a commensal bacterium modifies host nutritional immunity during Salmonella infection.Cell host & microbe · 2023Article
Corrections and comments
- Erratum issued
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacteria of the phylum Bacteroidetes, including commensal organisms and opportunistic pathogens, harbor abundant surface-exposed multiprotein membrane complexes (Sus-like systems) involved in carbohydrate acquisition. These complexes have been mostly linked to commensalism, and in some instances, they have also been shown to play a role in pathogenesis. Sus-like systems are mainly composed of lipoproteins anchored to the outer membrane and facing the external milieu. This lipoprotein localization is uncommon in most studied Gram-negative bacteria, while it is widespread in Bacteroidetes Little is known about how these complexes assemble and particularly about how lipoproteins reach the bacterial surface. Here, by bioinformatic analyses, we identify a lipoprotein export signal (LES) at the N termini of surface-exposed lipoproteins of the human pathogen Capnocytophaga canimorsus corresponding to K-(D/E) IMPORTANCE: Bacteria of the phylum Bacteroidetes are important human commensals and pathogens. Understanding their biology is therefore a key question for human health. A main feature of these bacteria is the presence of abundant lipoproteins at their surface that play a role in nutrient acquisition. To date, the underlying mechanism of lipoprotein transport is unknown. We show for the first time that Bacteroidetes surface lipoproteins share an N-terminal signal that drives surface localization. The localization and overall negative charge of the lipoprotein export signal (LES) are crucial for its role. Overall, our findings provide the first evidence that Bacteroidetes are endowed with a new bacterial lipoprotein export pathway that flips lipoproteins across the outer membrane.
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Registered trials
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.