Proteomic identification of Galectin-11 and 14 ligands from Haemonchus contortus
A peer-reviewed article of this Preprint also exists.
Haemonchus contortus is the most pathogenic nematode of small ruminants. Infection in sheep and goats results in anaemia that decreases animal productivity and can ultimately cause death. The involvement of ruminant-specific galectin-11 (LGALS-11) and galectin-14 (LGALS-14) has been postulated to play important roles in protective immune responses against parasitic infection; however, their ligands are unknown. In the current study, LGALS-11 and LGALS-14 ligands in H. contortus were identified from larval (L4) and adult parasitic stages extracts using immobilised LGALS-11 and LGALS-14 affinity column chromatography and mass spectrometry. Both LGALS-11 and LGALS-14 bound more putative protein targets in the adult stage of H. contortus (43 proteins) when compared to the larval stage (2 proteins). Of the 43 proteins identified in the adult stage, 34 and 35 proteins were bound by LGALS-11 and LGALS-14, respectively, with 26 proteins binding to both galectins. Interestingly, hematophagous stage-specific sperm-coating protein and zinc metalloprotease (M13), which are known vaccine candidates, were identified as putative ligands of both LGALS-11 and LGALS-14. The identification of glycoproteins of H. contortus by LGALS-11 and LGALS-14 provide new insights into host-parasite interactions and the potential for developing new interventions.
Cite this as
2017. Proteomic identification of Galectin-11 and 14 ligands from Haemonchus contortus. PeerJ Preprints 5:e3473v1 https://doi.org/10.7287/peerj.preprints.3473v1note This preprint is not peer-reviewed. You may wish to reference the subsequent peer-reviewed version of this article.
This is a submission to PeerJ for review.
Additional Information
Competing Interests
The authors declare that they have no competing interests.
Author Contributions
Dhanasekaran Sakthivel conceived and designed the experiments, performed the experiments, analyzed the data, contributed reagents/materials/analysis tools, wrote the paper, prepared figures and/or tables, reviewed drafts of the paper.
Jaclyn Swan analyzed the data, contributed reagents/materials/analysis tools, wrote the paper, prepared figures and/or tables, reviewed drafts of the paper.
Sarah Preston conceived and designed the experiments, performed the experiments, contributed reagents/materials/analysis tools.
MD Shakif-Azam contributed reagents/materials/analysis tools.
Pierre Faou performed the experiments, analyzed the data, contributed reagents/materials/analysis tools, wrote the paper, reviewed drafts of the paper.
Yaqing Jiao contributed reagents/materials/analysis tools.
Rachel Downs performed the experiments, contributed reagents/materials/analysis tools, prepared figures and/or tables.
Harinda Rajapaksha performed the experiments, analyzed the data, contributed reagents/materials/analysis tools, prepared figures and/or tables, reviewed drafts of the paper.
Robin Gasser analyzed the data, contributed reagents/materials/analysis tools, wrote the paper, reviewed drafts of the paper.
David Piedrafita conceived and designed the experiments, analyzed the data, contributed reagents/materials/analysis tools, wrote the paper, reviewed drafts of the paper.
Travis Beddoe conceived and designed the experiments, analyzed the data, contributed reagents/materials/analysis tools, wrote the paper, prepared figures and/or tables, reviewed drafts of the paper.
Animal Ethics
The following information was supplied relating to ethical approvals (i.e., approving body and any reference numbers):
Animal experimental procedures were fully approved by the Monash University Animal Ethics Committee (Ethics # SOBSA/P/2009/44).
Data Deposition
The following information was supplied regarding data availability:
The mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium via the PRIDE partner repository with the data set identifier PXD008435 and 10.6019/PXD008435.
Funding
DS was supported by Victoria India Doctoral Fellowship from the Department of State Development, Business and Innovation (DSDBI), Victoria, Australia and Australia India Institute (AII). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.
