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Proteomic characterization of Opisthorchis felineus execretory/secretory and tegumental proteins

ABSTRACT: Opisthorchis felineus is one of the three most medically important species belonging to the family of fish-borne zoonotic trematodes known as Opisthorchiidae. O. felineus is endemic to the river plains of Western Siberia and Eastern Europe and it is estimated that more than 1.6 million people could be infected with this parasite. To aid in the development of better control and diagnosis strategies for opisthorchiasis, we set out to deduce the secreted proteome of O. felineus. Adult flukes were collected from experimentally infected hamsters and cultured in vitro in serum-free media. We extracted proteins from different compartments of the O. felineus secretome, including (i) soluble excretory/secretory (ES) products; (ii) secreted microvesicles (MVs); and (iii) tegument. The tegument was further separated into three fractions of varying solubility via sequential extraction.

INSTRUMENT(S): TripleTOF 5600

ORGANISM(S): Opisthorchis Felineus

SUBMITTER: Javier Sotillo

LAB HEAD: Javier Sotillo

PROVIDER: PXD040364 | Pride | 2023-02-24

REPOSITORIES: Pride

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Project description:Proteases constitute the largest enzyme gene family in vertebrates with intracellular and secreted proteases having critical roles in cellular and organ physiology. Intestinal tract contains diverse set of proteases mediating digestion, microbial responses, epithelial and immune signaling. Transit of chyme through the intestinal tract results in significant suppression of proteases. Although endogenous protease inhibitors have been identified, the broader mechanisms underlying protease regulation in the intestinal tract remains unclear. The objective of this study was to determine microbial regulation of proteolytic activity in intestinal tract using phenotype of post-infection irritable bowel syndrome, a condition characterized by high fecal proteolytic activity. Proteases of host pancreatic origin (chymotrypsin like pancreatic elastase 2A, 3B and trypsin 2) drove proteolytic activity. Of the 14 differentially abundant taxa, high proteolytic activity state was characterized by complete absence of the commensal Alistipes putredinis. Germ free mice had very high proteolytic activity (10-fold of specific-pathogen free mice) which dropped significantly upon humanization with microbiota from healthy volunteers. In contrast, high proteolytic activity microbiota failed to inhibit it, a defect that corrected with fecal microbiota transplant as well as addition of A. putredinis. These mice also had increased intestinal permeability similar to that seen in patients. Microbiota β-glucuronidases mediate bilirubin deconjugation and unconjugated bilirubin is an inhibitor of serine proteases. We found that high proteolytic activity patients had lower urobilinogen levels, a product of bilirubin deconjugation. Mice colonized with β-glucuronidase overexpressing E. coli demonstrated significant inhibition of proteolytic activity and treatment with β-glucuronidase inhibitors increased it. The findings establish that specific commensal microbiota mediates effective inhibition of host pancreatic proteases and maintains intestinal barrier function through the production of β-glucuronidases. This suggests an important homeostatic role for commensal intestinal microbiota.

			Action	DRS
	ES_HQisoforms.group	Other
	MV1_A.wiff	Wiff
	MV1_A.wiff.scan	Wiff
	MV1_B.wiff	Wiff
	MV1_B.wiff.scan	Wiff

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Proteomic characterization of Opisthorchis felineus execretory/secretory and tegumental proteins

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