Evidence map›Paper›PMID 32826940›Full record

ArticleCommunications biology2020

The oligomeric assembly of galectin-11 is critical for anti-parasitic activity in sheep (Ovis aries).

Dhanasekaran Sakthivel, Sarah Preston, Robin B Gasser, Tatiana P Soares da Costa, Julia N Hernandez, Adam Shahine, M D Shakif-Azam, Peter Lock, Jamie Rossjohn, Matthew A Perugini and 4 more

Abstract read
In one paragraph

Article in Communications biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

6 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. What is the Sugar Code?Chembiochem : a European journal of chemical biology · 2022
    Review
  5. Evaluation of the Role of Galectins in Parasite Immunity.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  6. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

14 authors.

Dhanasekaran SakthivelDepartment of Biochemistry and Molecular Biology, Monash University, Clayton, VIC, 3800, Australia.ORCID http://orcid.org/0000-0003-2894-2545
Sarah PrestonSchool of Science, Psychology and, Sport, Federation University, Churchill, VIC, 3842, Australia.
Robin B GasserFaculty of Veterinary and Agricultural Sciences, The University of Melbourne, Bundoora, VIC, 3010, Australia.
Tatiana P Soares da CostaDepartment of Biochemistry and Genetics, La Trobe Institute for Molecular Science, La Trobe University, Bundoora, VIC, 3086, Australia.
Julia N HernandezInstituto Universitario de Sanidad Animal, Faculty of Veterinary Medicine, Universidad de Las Palmas de Gran Canaria, Arucas, Spain.
Adam ShahineDepartment of Biochemistry and Molecular Biology, Monash University, Clayton, VIC, 3800, Australia.
M D Shakif-AzamSchool of Science, Psychology and, Sport, Federation University, Churchill, VIC, 3842, Australia.
Peter LockBioimaging Platform, La Trobe Institute for Molecular Science, La Trobe University, Bundoora, VIC, 3086, Australia.ORCID http://orcid.org/0000-0003-4421-3609
Jamie RossjohnDepartment of Biochemistry and Molecular Biology, Monash University, Clayton, VIC, 3800, Australia.
Matthew A PeruginiDepartment of Biochemistry and Genetics, La Trobe Institute for Molecular Science, La Trobe University, Bundoora, VIC, 3086, Australia.
Jorge Francisco GonzálezInstituto Universitario de Sanidad Animal, Faculty of Veterinary Medicine, Universidad de Las Palmas de Gran Canaria, Arucas, Spain.
Els MeeusenSchool of Science, Psychology and, Sport, Federation University, Churchill, VIC, 3842, Australia.ORCID http://orcid.org/0000-0003-1239-6287
David PiedrafitaDepartment of Biochemistry and Molecular Biology, Monash University, Clayton, VIC, 3800, Australia. david.piedrafita@federation.edu.au.
Travis BeddoeDepartment of Biochemistry and Molecular Biology, Monash University, Clayton, VIC, 3800, Australia. t.beddoe@latrobe.edu.au.ORCID http://orcid.org/0000-0003-4550-2277

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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.

Indexed as

Protein MultimerizationAmino Acid SequenceAnimalsAntiparasitic AgentsGalectinsModels, MolecularParasitic Diseases, AnimalParasitic Sensitivity TestsProtein ConformationSheepSheep, DomesticStructure-Activity RelationshipAntiparasitic AgentsGalectins

Identifiers

PMID32826940
PMCPMC7442640

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.