In silico analyses of protein glycosylating genes in the helminth Fasciola hepatica (liver fluke) predict protein-linked glycan simplicity and reveal temporally-dynamic expression profiles.

McVeigh, Paul ORCID: 0000-0003-1850-9692, Cwiklinski, Krystyna ORCID: 0000-0001-5577-2735, Garcia-Campos, Andres, Mulcahy, Grace, O'Neill, Sandra M, Maule, Aaron G ORCID: 0000-0003-0862-2667 and Dalton, John P ORCID: 0000-0003-3829-9186 (2018) In silico analyses of protein glycosylating genes in the helminth Fasciola hepatica (liver fluke) predict protein-linked glycan simplicity and reveal temporally-dynamic expression profiles. Scientific reports, 8 (1). 11700-.

Access the full-text of this item by clicking on the Open Access link.

Official URL: http://dx.doi.org/10.1038/s41598-018-29673-3

Abstract

Glycoproteins secreted by helminth parasites are immunogenic and represent appealing components of vaccine preparations. Our poor knowledge of the pathways that mediate protein glycosylation in parasitic flatworms hinders our understanding of how proteins are synthesised and modified, and our ability to target these pathways for parasite control. Here we provide the first detailed description of genes associated with protein glycosylation in a parasitic flatworm, focusing on the genome of the liver fluke (Fasciola hepatica), which is a globally important trematode parasite of humans and their livestock. Using 190 human sequences as search queries against currently available F. hepatica genomes, we identified 149 orthologues with putative roles in sugar uptake or nucleotide sugar synthesis, and an array of glycosyltransferase and glycosidase activities required for protein N- and O-glycosylation. We found appreciable duplication within these orthologues, describing just 87 non-redundant genes when paralogues were excluded. F. hepatica lacks many of the enzymes required to produce complex N- and O-linked glycans, which explains the genomic basis for the structurally simple glycans described by F. hepatica glycomic datasets, and predicts pervasive structural simplicity in the wider glycome. These data provide a foundation for functional genomic interrogation of these pathways with the view towards novel parasite intervention strategies.

Item Type:	Article
Uncontrolled Keywords:	Endoplasmic Reticulum, Animals, Humans, Fasciola hepatica, Polysaccharides, Helminth Proteins, Gene Expression Profiling, Gene Duplication, Biological Transport, Glycosylation, Genes, Helminth, Time Factors, Computer Simulation, Sugars
Divisions:	Faculty of Health and Life Sciences Faculty of Health and Life Sciences > Institute of Infection, Veterinary and Ecological Sciences
Depositing User:	Symplectic Admin
Date Deposited:	24 Feb 2022 09:00
Last Modified:	18 Jan 2023 21:11
DOI:	10.1038/s41598-018-29673-3
Open Access URL:	https://www.nature.com/articles/s41598-018-29673-3
Related URLs:	Author Publisher
URI:	https://livrepository.liverpool.ac.uk/id/eprint/3149581