Extracellular Vesicle Subproteome Differences among Filifactor alocis Clinical Isolates

Filifactor alocis is a Gram-positive asaccharolytic, obligate anaerobic rod of the Firmicutes phylum, which has recently been implicated in oral infections. Extracellular vesicles (EVs) are crucial conveyors of microbial virulence in bacteria and archaea. Previously, in highly purified EVs from the...

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Bibliographic Details
Published in:Microorganisms (Basel) 2022, Vol.10 (9), p.1826
Main Authors: Bao, Kai, Claesson, Rolf, Belibasakis, Georgios N., Oscarsson, Jan
Format: Article
Language:English
Subjects:
Archaea
Arginine
Bacteria
Biosynthesis
Clinical isolates
extracellular vesicles (EVs)
Filifactor alocis
Gram-positive bacteria
Medicin och hälsovetenskap
Microorganisms
Neutrophils
oral infections
Peptides
Pilin
predicted EV subproteome
Proteins
Proteomics
Ribosomal proteins
Software
Strains (organisms)
Toxins
Virulence
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Summary:Filifactor alocis is a Gram-positive asaccharolytic, obligate anaerobic rod of the Firmicutes phylum, which has recently been implicated in oral infections. Extracellular vesicles (EVs) are crucial conveyors of microbial virulence in bacteria and archaea. Previously, in highly purified EVs from the F. alocis reference strain ATCC 35896 (CCUG 47790), 28 proteins were identified. The present study aimed to use label-free quantification proteomics in order to chart these EV proteins, in the reference strain, and in nine less-well-characterized clinical F. alocis isolates. In total, 25 of the EV proteins were identified and 24 were quantified. Sixteen of those were differentially expressed between the ten strains and the novel FtxA RTX toxin and one lipoprotein were among them. Consistent expression was observed among ribosomal proteins and proteins involved in L-arginine biosynthesis and type IV pilin, demonstrating a degree of EV protein expression preservation among strains. In terms of protein–protein interaction analysis, 21 functional associations were revealed between 19 EV proteins. Interestingly, FtxA did not display predicted interactions with any other EV protein. In conclusion, the present study charted 25 EV proteins in ten F. alocis strains. While most EV proteins were consistently identified among the strains, several of them were also differentially expressed, which justifies that there may be potential variations in the virulence potential among EVs of different F. alocis strains.
ISSN:2076-2607
2076-2607
DOI:10.3390/microorganisms10091826