- Title
- The oligomeric assembly of galectin-11 is critical for anti-parasitic activity in sheep (Ovis aries)
- Creator
- Sakthivel, Dhanasekaran; Preston, Sarah; Gasser, Robin; Meeusen, Els; Piedrafita, David
- Date
- 2020
- Type
- Text; Journal article
- Identifier
- http://researchonline.federation.edu.au/vital/access/HandleResolver/1959.17/177146
- Identifier
- vital:15237
- Identifier
-
https://doi.org/10.1038/s42003-020-01179-7
- Identifier
- ISBN:2399-3642 (ISSN)
- Abstract
- Galectins are a family of glycan-binding molecules with a characteristic affinity for ß-D-glycosides that mediate a variety of important cellular functions, including immune and inflammatory responses. Galectin-11 (LGALS-11) has been recently identified as a mediator induced specifically in animals against gastrointestinal nematodes and can interfere with parasite growth and development. Here, we report that at least two natural genetic variants of LGALS-11 exist in sheep, and demonstrate fundamental differences in anti-parasitic activity, correlated with their ability to dimerise. This study improves our understanding of the role of galectins in the host immune and inflammatory responses against parasitic nematodes and provides a basis for genetic studies toward selective breeding of animals for resistance to parasites. © 2020, The Author(s). **Please note that there are multiple authors for this article therefore only the name of the first 5 including Federation University Australia affiliate “Dhanasekaran Sakthivel, Sarah Preston, Robin Gasser, Els Meeusen, David Piedrafita” is provided in this record**
- Publisher
- Nature Research
- Relation
- Communications Biology Vol. 3, no. 1 (2020), p.
- Rights
- All metadata describing materials held in, or linked to, the repository is freely available under a CC0 licence
- Rights
- http://creativecommons.org/licenses/by/4.0/
- Rights
- Copyright © The Author(s) 2020. This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
- Rights
- Open Access
- Subject
- 06 Biological Sciences
- Full Text
- Reviewed
- Funder
- We thank staff at the Monash Macromolecular Crystallisation Facility (MMCF) for assistance with crystallisation, and at the Australian Synchrotron for support with X-ray data collection. We are grateful to Dr. Dene Littler for initial support with crystal structure analysis. DS acknowledges support from the Department of State Development, Business and Innovation (DSDBI), Victoria, Australia and Australia-India Institute (AII). DS acknowledges the financial support from the Australian Society for Parasitology to attend CCP4 crystallography workshop. R.B.G.’s research was funded through grants from the Australian Research Council (ARC), the National Health and Medical Research Council (NHMRC) of Australia, Yourgene Bioscience Taiwan, and Melbourne Water Corporation.
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