PXD059642

PXD059642 is an original dataset announced via ProteomeXchange.

Title	LolB is conserved in Bacteroidetes and is crucial for gliding motility and Type IX secretion.Part2
Description	In Gram-negative bacteria, lipoproteins are major components of the outer membrane (OM) where they play a variety of roles, from the involvement in β-barrel assembly to virulence. Bacteroidetes, a widespread phylum of Gram-negative bacteria, including free-living organisms, commensals and pathogens, encode an exceptionally high number of outer membrane lipoproteins. These proteins are crucial in this phylum mainly because they are key components of SUS-like nutrient acquisition systems as well as of the Type IX secretion and gliding motility machineries. The transport of lipoproteins to the OM has mainly been studied in E. coli and relies on the Lol system, composed of the inner membrane extraction machinery LolCDE, the periplasmic carrier LolA and the OM lipoprotein LolB. While most Lol proteins are essential and conserved across Gram-negative bacteria, to date, no LolB homologs have been identified outside of γ- and β-proteobacteria. How lipoproteins reach and are inserted in the OM of Bacteroidetes is not known. Here we identified LolB homologs in Bacteroidetes and disclosed the co-existence of several LolA and LolB homologs in several species. We provide evidence that LolA1 and LolB1 of F. johnsoniae are devoted to targeting gliding and T9SS lipoproteins to the OM. A proteomic analysis of the OM composition of the lolA1 and lolB1 deletion strain supports this evidence. Furthermore, we show that, while LolB1 and LolA1 have conserved functions in Bacteroidetes, they are partially functionally different from their E. coli counterparts. We also show that surface lipoprotein transport is LolA and LolB independent. Finally, the finding that, in the absence of LolA and LolB homologs, lipoproteins still localize to the OM, strongly suggests the presence in Bacteroidetes of a yet unidentified Lol-alternative transport pathway. In conclusion, Bacteroidetes seem to have evolved different and probably more complex lipoprotein transport pathways than other Gram-negative bacteria and further research is required to uncover their complexity.
HostingRepository	PRIDE
AnnounceDate	2025-02-22
AnnouncementXML	Submission_2025-02-22_02:39:51.547.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD059642
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Marc Dieu
SpeciesList	scientific name: Flavobacterium johnsoniae; NCBI TaxID: 986;
ModificationList	acetylated residue; monohydroxylated residue; iodoacetamide derivatized residue
Instrument	timsTOF Pro

Revision	Datetime	Status	ChangeLog Entry
0	2025-01-10 08:26:41	ID requested
⏵ 1	2025-02-22 02:39:51	announced

10.6019/PXD059642;

submitter keyword: lipoprotein, transport, protein, Bacteroidetes, membrane

Dr Francesco RENZI
contact affiliation	University of Namur Research Unit in Biology of Microorganisms (URBM) Namur Research Institute for Life Sciences (NARILIS) Belgium.
contact email	francesco.renzi@unamur.be
lab head
Marc Dieu
contact affiliation	University of Namur - MaSUN
contact email	marc.dieu@unamur.be
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD059642
     1. Label: PRIDE project
     2. Name: LolB is conserved in Bacteroidetes and is crucial for gliding motility and Type IX secretion.Part2