Galectin-2 suppresses nematode development by binding to the invertebrate-specific galactoseβ1-4fucose glyco-epitope

Takeuchi, Tomoharu; Tamura, Masahito; Ishiwata, Kenji; Hamasaki, Megumi; Hamano, Shinjiro; Arata, Yoichiro; Hatanaka, Tomomi

doi:10.1093/glycob/cwz022

Cited by 7 publications

(9 citation statements)

References 58 publications

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“…elegans (Figure a); LEC-1, LEC-2, LEC-3, LEC-4, and LEC-5 are the tandem-repeat galectins in C. elegans (Figure b); and LEC-7, LEC-8, LEC-9, LEC-10, and LEC-11 are the chimera galectins in this species (Figure c) …”

Section: Introductionmentioning

confidence: 86%

Nanoparticles To Study Lectins in Caenorhabditis elegans: Multivalent Galactose β1-4 Fucose-Functionalized Dendrimers Provide Protection from Oxidative Stress

2021

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Galectins are galactoside-binding lectins that are functional dimers or higher-order oligomers. Multivalent binding has been shown to augment the relatively low affinity of the galectins for their galactoside-binding partners, enabling the galectins to play an important role in the global remodeling of cells that occurs during the stress conditions of disease states, including heart disease and cancer. The presence of galectins in the nematode Caenorhabditis elegans and their galactoside-binding properties have been demonstrated, but the role of multivalent interactions for C. elegans galectins is unknown. Here, we describe the synthesis of Galβ1-4Fuc-functionalized poly(amidoamine) dendrimers and their utility in studies using C. elegans during oxidative stress. C. elegans were fed Galβ1-4Fuc-functionalized dendrimers and RNA interference to knock down lectins lec-1 and lec-10 while undergoing oxidative stress. C. elegans that were pretreated with the glycodendrimers were less susceptible to oxidative stress than untreated controls. Worms that were fed fluorescently tagged glycodendrimers and imaged indicated that the dendrimers are primarily present in the digestive tract of the worms, and uptake into the vulva and proximal gonads could also be observed in some instances. This study suggests that multivalently presented Galβ1-4Fuc can protect C. elegans from oxidative stress.

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Section: Introductionmentioning

confidence: 86%

Nanoparticles To Study Lectins in Caenorhabditis elegans: Multivalent Galactose β1-4 Fucose-Functionalized Dendrimers Provide Protection from Oxidative Stress

2021

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“…Mouse galectin-1C2S, galectin-2, and galectin-3 recombinant proteins were expressed in Escherichia coli and affinity-purified with an asialofetuin- or Galβ1-4Fuc-immobilized sepharose column basically as described previously [ 13 ]. After sterilization by filtration, each recombinant protein (1 µg) was subjected to SDS-PAGE and stained with Bio-Safe™ Coomassie (Bio-Rad, Hercules, CA, USA).…”

Section: Methodsmentioning

confidence: 99%

“…Adult S. mansoni and mixed stage of C. elegans were prepared and lysed by sonication and boiling in SDS-PAGE sample buffer as described previously [ 13 ]. Worm extracts and BSA (50 ng) were separated by SDS-PAGE and then subjected to lectin blotting, as described previously [ 18 ].…”

Section: Methodsmentioning

confidence: 99%

“…Sheep galectin-11 directly binds to the parasitic nematode Haemonchus contortus and suppresses larval growth and development [ 12 ]. Mammalian galectin-2 directly binds to an invertebrate-specific Galactoseβ1-4Fucose disaccharide epitope and has demonstrated potential anti-parasitic activity in an experiment performed using Caenorhabditis elegans [ 13 ].…”

Section: Introductionmentioning

confidence: 99%

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In vitro evaluation of the effect of galectins on Schistosoma mansoni motility

Takeuchi,

Nakamura,

Hamasaki

et al. 2023

BMC Res Notes

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Objective Galectins are sugar-binding proteins that participate in many biological processes, such as immunity, by regulating host immune cells and their direct interaction with pathogens. They are involved in mediating infection by Schistosoma mansoni, a parasitic trematode that causes schistosomiasis. However, their direct effects on schistosomes have not been investigated. Results We found that galectin-2 recognizes S. mansoni glycoconjugates and investigated whether galectin-1, 2, and 3 can directly affect S. mansoni in vitro. Adult S. mansoni were treated with recombinant galectin-1, 2, and 3 proteins or praziquantel, a positive control. Treatment with galectin-1, 2, and 3 had no significant effect on S. mansoni motility, and no other differences were observed under a stereoscopic microscope. Hence, galectin-1, 2, and 3 may have a little direct effect on S. mansoni. However, they might play a role in the infection in vivo via the modulation of the host immune response or secretory molecules from S. mansoni. To the best of our knowledge, this is the first study to investigate the direct effect of galectins on S. mansoni and helps in understanding the roles of galectins in S. mansoni infection in vivo.

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“…Gal-1 mediates T lymphocyte apoptosis (Perillo et al ., 1995) as does gal-2 (Sturm et al ., 2004). Gal-2 has also been shown to inhibit the development of the parasitic nematode Ascaris suum as well as the free-living nematode Caenorhabditis elegans by binding to the galactose β 1-4fucose epitope (Takeuchi et al ., 2019).…”

Section: Function Of Host Galectinsmentioning

confidence: 99%

The interaction of host and nematode galectins influences the outcome of gastrointestinal nematode infections

Donskow‐Łysoniewska

Maruszewska-Cheruiyot

Stear

2021

Parasitology

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Galectin-2 suppresses nematode development by binding to the invertebrate-specific galactoseβ1-4fucose glyco-epitope

Abstract: Galectin-2 suppresses nematode development by binding to the invertebrate-specific galactoseβ1-4fucose glyco-epitope

Cited by 7 publications

References 58 publications

Nanoparticles To Study Lectins in Caenorhabditis elegans: Multivalent Galactose β1-4 Fucose-Functionalized Dendrimers Provide Protection from Oxidative Stress

Nanoparticles To Study Lectins in Caenorhabditis elegans: Multivalent Galactose β1-4 Fucose-Functionalized Dendrimers Provide Protection from Oxidative Stress

In vitro evaluation of the effect of galectins on Schistosoma mansoni motility

The interaction of host and nematode galectins influences the outcome of gastrointestinal nematode infections

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