Dataset Information

Proteomic analysis of the fish pathogen Vibrio ordalii strain Vo-LM-18 and its outer membrane vesicles

ABSTRACT: Vibrio ordalii is the causative agent of atypical vibriosis in salmonids cultured in Chile. While extensive research has provided valuable insights into V. ordalii through phenotypic, antigenic, and genetic typing, as well as various virulence mechanisms (e.g., capsular material, iron-uptake systems, and outer membrane vesicles [OMVs]), proteomic characterization remains largely unexplored. This study aimed to advance the proteomic knowledge of Chilean V. ordalii Vo-LM-18 and its OMVs, which have been extensively characterized in several studies and have demonstrated their virulence. Using Nano-UHPLC-LC-MS/MS, we identified 2,242 proteins in the bacterium and 1,755 proteins in its OMVs. Among these, 644 unique proteins were detected in V. ordalii Vo-LM-18, 156 unique proteins were found in its OMVs, and 1,596 proteins were shared between both components. bioinformatics compartment prediction (PSORT algorithm) revealed that the major categories in the OMVs were similar to those in the bacteria (i.e., cytoplasmic and cytoplasmic membrane proteins), though with different proportions. Functional annotation with Gene Ontology identified 37 biological pathways in V. ordalii Vo-LM-18 and 28 in its OMVs. Proteins associated with transport, transcription, and virulence were predominant in both the bacteria and the vesicles. Comparison between the strain Vo-LM-18 and its OMVs showed evident differences in protein expression, with OMVs expressing a higher number of virulence-associated proteins, including those related to iron- and heme-uptake mechanisms. Notable pathways in the bacteria included flagellum assembly, heme group-associated proteins, and protein biosynthesis. This proteomic analysis also represents the first detection of RTX toxin in a V. ordalii strain (Vo-LM-18) and its vesicles. Our results highlight the crucial role of OMVs in the pathogenesis and adaptation of V. ordalii, suggesting their potential as diagnostic biomarkers and therapeutic targets for bacterial infections.

INSTRUMENT(S):

ORGANISM(S): Vibrio Ordalii

SUBMITTER: Guillermo Nourdin

LAB HEAD: Ruben Avendaño-Herrera

PROVIDER: PXD055136 | Pride | 2026-05-14

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	Protein_Vordalii_final.tsv	Tabular
	V1_OMV1_Slot1-28_1_317.d.zip	Other
	V2_OMV2_Slot1-29_1_318.d.zip	Other
	V3_OMV3_Slot1-30_1_319.d.zip	Other
	V4_Bacteria1_Slot1-31_1_320.d.zip	Other

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Project description:Membrane Vesicles (MVs) are envelope derived extracellular sacs that perform a broad diversity of physiological functions in bacteria. While considerably studied in pathogenic microorganisms, the roles, relevance and biotechnological potential of MVs from environmental bacteria are less well established. Acidithiobacillaceae family bacteria are active players in the sulfur and iron biogeochemical cycles in extreme acidic environments and drivers of the leaching of mineral ores contributing to acid rock/mine drainage (ARD/AMD) and industrial bioleaching. One key aspect to such rol is the ability of these bacteria to tightly interact with the mineral surfaces and extract electrons and nutrients to support their chemolithotrophic metabolism. Despite recent advances in the characterization of acidithiobacilli biofilms and extracellular matrix (ECM) components, our understanding of its architectural and mechanistic aspects remains scant. In this work, we show that vesiculation is a common phenomenon in distant members of the Acidithiobacillaceae family, and further explore the role of MVs in multicellular colonization behaviours using `Fervidacidithiobacillus caldus´ as bacterial model. Production of MVs in `F. caldus´ occurred in both planktonic cultures and biofilms formed on sulfur surfaces, where MVs appeared individually or in chains resembling Tube-Shaped Membranous Structures (TSMSs) important for microbial communication. Liquid chromatography-mass spectrometry data and bioinformatic analysis of the MVs-associated proteome revealed that F. caldus MVs were enriched in proteins involved in cell-cell and cell-surface processes, and largely typified the MVs as outer MVs (OMVs). Finally, microbiological assays showed that amendment of `F. caldus´ MVs to cells and/or biofilms affects collective colonizing behaviours relevant to the ecophysiology and applications of these acidophiles providing grounds for their exploitation in mining biotechnologies.

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Proteomic analysis of the fish pathogen Vibrio ordalii strain Vo-LM-18 and its outer membrane vesicles

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