Proteomic identification of galectin-11 and -14 ligands from Fasciola hepatica

Jaclyn Swan; Dhanasekaran Sakthivel; Timothy C Cameron; Pierre Faou; Rachael Downs; Harinda Rajapaksha; David Piedrafita; Travis Beddoe

doi:10.1016/j.ijpara.2019.06.007

Proteomic identification of galectin-11 and -14 ligands from Fasciola hepatica

Int J Parasitol. 2019 Nov;49(12):921-932. doi: 10.1016/j.ijpara.2019.06.007. Epub 2019 Sep 24.

Authors

Jaclyn Swan¹, Dhanasekaran Sakthivel², Timothy C Cameron¹, Pierre Faou³, Rachael Downs³, Harinda Rajapaksha³, David Piedrafita⁴, Travis Beddoe⁵

Affiliations

¹ Department of Animal, Plant and Soil Science and Centre for AgriBioscience (AgriBio), La Trobe University, Victoria 3086, Australia; Centre for Livestock Interactions with Pathogens (CLiP), La Trobe University, Victoria 3086, Australia.
² Department of Animal, Plant and Soil Science and Centre for AgriBioscience (AgriBio), La Trobe University, Victoria 3086, Australia.
³ Department of Biochemistry & Genetics, La Trobe Institute for Molecular Science, La Trobe University, Victoria 3086, Australia.
⁴ School of Applied and Biomedical Sciences, Federation University, Churchill, Victoria 3842, Australia.
⁵ Department of Animal, Plant and Soil Science and Centre for AgriBioscience (AgriBio), La Trobe University, Victoria 3086, Australia; Centre for Livestock Interactions with Pathogens (CLiP), La Trobe University, Victoria 3086, Australia. Electronic address: t.beddoe@latrobe.edu.au.

PMID: 31560927
DOI: 10.1016/j.ijpara.2019.06.007

Abstract

Fasciola hepatica is a globally distributed zoonotic trematode that causes fasciolosis in livestock, wildlife, ruminants and humans. Fasciolosis causes a significant economic impact on the agricultural sector and affects human health. Due to the increasing prevalence of triclabendazole resistance in F. hepatica, alternative treatment methods are required. Many protein antigens have been trialled as vaccine candidates with low success, however, the tegument of F. hepatica is highly glycosylated and the parasite-derived glycoconjugate molecules have been identified as an important mediator in host-parasite interactions and as prime targets for the host immune system. Galectin-11 (LGALS-11) and galectin-14 (LGALS-14) are two ruminant-specific glycan-binding proteins, showing upregulation in the bile duct of sheep infected with F. hepatica, which are believed to mediate host-parasite interaction and innate immunity against internal parasites. For the first known time, this study presents the ligand profile of whole worm and tegument extracts of F. hepatica that interacted with immobilised LGALS-11 and LGALS-14. LGALS-14 interacted with a total of 255 F. hepatica proteins. The protein which had the greatest interaction was identified as an uncharacterised protein which contained a C-type lectin domain. Many of the other proteins identified were previously trialled vaccine candidates including glutathione S-transferase, paramyosin, cathepsin L, cathepsin B, fatty acid binding protein and leucine aminopeptidase. In comparison to LGALS-14, LGALS-11 interacted with only 49 F. hepatica proteins and it appears to have a much smaller number of binding partners in F. hepatica. This is, to our knowledge, the first time host-specific lectins have been used for the enrichment of F. hepatica glycoproteins and this study has identified a number of glycoproteins that play critical roles in host-parasite interactions which have the potential to be novel vaccine candidates.

Keywords: Fasciola hepatica; Galectin; Glycoprotein; Host-parasite interactions; Mass spectrometry.

MeSH terms

Animals
Antigens, Helminth / analysis*
Antigens, Helminth / isolation & purification
Fasciola hepatica / growth & development*
Galectins / metabolism*
Helminth Proteins / analysis*
Helminth Proteins / isolation & purification
Host-Parasite Interactions*
Ligands
Mass Spectrometry
Protein Binding
Protein Interaction Mapping*
Proteomics
Sheep*

Substances

Antigens, Helminth
Galectins
Helminth Proteins
Ligands