MassIVE MSV000092443

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Exposure to extracellular vesicles from Anisakis simplex induce changes in protein composition of human intestinal epithelial cell line (CACO-2) - parasite-host interaction overview

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Description

Anisakis simplex is one of the most prevalent parasitic nematodes (Nematoda) of marine organisms and is characterized by a complex life cycle. Humans can be accidental hosts for this parasitic species. Therefore, A. simplex was acknowledged as a biohazardous organism. The finding that nematodes can release extracellular vesicles (EVs), which are able to enter host cells, was the breakthrough discovery in parasite research. Although several approaches have been employed to study the biology of nematodes and their interactions with the host, the secretion of EVs by parasitic nematodes, as signal molecules, has been poorly studied. This led us to identify differentially regulated proteins (DRPs) between the proteome of a human intestinal epithelial cell line (CACO 2) exposed to EVs of A. simplex and the proteome of CACO 2 directly exposed to L3 larvae of A. simplex. In addition, we identified proteins present in EVs of A. simplex larvae and linked them to host proteins that they might regulate. To achieve this goal the shotgun proteomics method based on isobaric mass labeling (TMT) with a combination of nano high-performance liquid chromatography (nLC) coupled to an LTQ Orbitrap Elite mass spectrometer was used. [doi:10.25345/C5KW57V0R] [dataset license: CC0 1.0 Universal (CC0 1.0)]

Keywords: CACO 2, Anisakis simplex, extracellular vesicles, host parasite interactions

Contact

Principal Investigators:
(in alphabetical order) 		Robert Stryinski, University of Warmia and Mazury in Olsztyn, Poland
Submitting User: robertstr

Publications

Stryi?ski R, Fiedorowicz E, Mateos J, Andronowska A, ?opie?ska-Biernat E, Carrera M.
Exploring the exoproteome of the parasitic nematode Anisakis simplex (s. s.) and its impact on the human host - an in vitro cross-talk proteomic approach.
Front Immunol. Epub 2025 Feb 3. 10.3389/fimmu.2025.1509984.

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