A Caenorhabditis elegans Glycolipid-binding Galectin Functions in Host Defense against Bacterial Infection

Ideo, Hiroko; Fukushima, Keiko; Gengyo-Ando, Keiko; Mitani, Shohei; Dejima, Katsufumi; Nomura, Kazuya; Yamashita, Katsuko

doi:10.1074/jbc.m109.038257

Cited by 53 publications

(43 citation statements)

References 38 publications

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“…2C, lanes 2-4). The main glycolipid bands were observed in positions similar to those reported previously (12,16). TLC overlay staining of upper phase glycolipids with MOA revealed binding to N2 and bre-2(ye31) but not bre-4(ye27) glycolipids (Fig.…”

Section: Moa Inhibits C Elegans Development and Amoebal Growthsupporting

confidence: 82%

“…This is consistent with MOA susceptibility of N2 and bre-2(ye31) worms and resistance of bre-4(ye27) animals. To identify the glycolipid species that is recognized by MOA, comparative overlay staining with t-Cry5B as described by Ideo et al (12) was performed. The pattern of the orcinol staining and the t-Cry5B overlay of N2-derived glycolipids (Fig.…”

Section: Moa Inhibits C Elegans Development and Amoebal Growthmentioning

confidence: 99%

“…Detailed information can be found under supplemental "Materials and Methods." Truncated Cry5B (t-Cry5B) was prepared as described previously (12). For TLC overlay analysis, purified MOA and t-Cry5B were labeled with EZ-Link sulfo-NHS-biotin (Pierce) using a 20-fold molar excess of labeling reagent.…”

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confidence: 99%

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Nematotoxicity of Marasmius oreades Agglutinin (MOA) Depends on Glycolipid Binding and Cysteine Protease Activity

Wohlschlager¹,

Butschi

Zurfluh³

et al. 2011

Journal of Biological Chemistry

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Fruiting body lectins have been proposed to act as effector proteins in the defense of fungi against parasites and predators. The Marasmius oreades agglutinin (MOA) is a Gal␣1,3Gal/ GalNAc-specific lectin from the fairy ring mushroom that consists of an N-terminal ricin B-type lectin domain and a C-terminal dimerization domain. The latter domain shows structural similarity to catalytically active proteins, suggesting that, in addition to its carbohydrate-binding activity, MOA has an enzymatic function. Here, we demonstrate toxicity of MOA toward the model nematode Caenorhabditis elegans. This toxicity depends on binding of MOA to glycosphingolipids of the worm via its lectin domain. We show further that MOA has cysteine protease activity and demonstrate a critical role of this catalytic function in MOA-mediated nematotoxicity. The proteolytic activity of MOA was dependent on high Ca 2؉ concentrations and favored by slightly alkaline pH, suggesting that these conditions trigger activation of the toxin at the target location. Our results suggest that MOA is a fungal toxin with intriguing similarities to bacterial binary toxins and has a protective function against fungivorous soil nematodes.

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Section: Moa Inhibits C Elegans Development and Amoebal Growthsupporting

confidence: 82%

Section: Moa Inhibits C Elegans Development and Amoebal Growthmentioning

confidence: 99%

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Nematotoxicity of Marasmius oreades Agglutinin (MOA) Depends on Glycolipid Binding and Cysteine Protease Activity

Wohlschlager¹,

Butschi

Zurfluh³

et al. 2011

Journal of Biological Chemistry

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“…3B) that does not contain Galβ1-4Fuc epitope (27). In addition, although LEC-1 has affinity for the chemically Since LEC-1 could bind to glycans containing Galβ1-3GalNAc disaccharide such as Galβ1-3GalNAcβ1-4Galβ1-4Glc (note that this is asialo-GM1 structure found in glycolipid of vertebrate species, while it has not been found in C. elegans glycolipid) (17), a potential endogenous ligand of LEC-1 might be C. elegans Oglycans containing Galβ1-3GalNAc (31, 32) (Fig.…”

Section: Endogenous Ligand Glycans Of C Elegans Galectinsmentioning

confidence: 99%

Galectins in Invertebrates with a focus on <i>Caenorhabditis elegans</i>

Takeuchi

2018

TIGG

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Galectins are a family of β-galactoside-binding lectins widely distributed among animals and fungi, and Galβ1-4GlcNAc is considered the major recognition unit of vertebrate galectins. On the other hand, more than 10 galectins have been reported in Caenorhabditis elegans that belong to the invertebrate class and these C. elegans galectins have been confirmed to have affinity for Galβ1-4GlcNAc. However, the glycan structure differs among species and glycan containing Galβ1-4GlcNAc has not been reported in C. elegans so far. Therefore, the endogenous ligands of C. elegans galectins remained undetermined. Recent studies uncovered that the structures of endogenous ligand glycans of C. elegans galectins are different from those of vertebrate galectins, for e.g., Nglycan containing Galactoseβ1-4 fucose epitope which is not found in vertebrates. Further, C. elegans galectins play a role in host defense against infection and oxidative stress. The roles of mammalian galectins in host defense have been explored in recent years. Taken together, one of the fundamental functions of galectins is possibly host defense because both C. elegans and mammalian galectins function in host defense despite alterations of their ligand structure in the evolutionary process. A. IntroductionGalectins are a family of widely distributed animal lectins that specifically bind to β-galactoside sugars such as Galβ1-4Glc and shown to function in various biological phenomena such as development, cancer, and immunity, and Galβ1-4GlcNAc is thought to be the major endogenous recognition unit of vertebrate galectins (5-8). Meanwhile, in recent years, the recognition of exogenous glycans by galectin is also thought to be important for innate immunity (3, 6), and it has been shown that galectins have affinities for various disaccharide units that contain β-galactoside structure regardless of whether such disaccharides are found endogenously or exogenously (9). B. Galectin (-like) Proteins in InvertebratesNumerous galectin (-like) proteins have also been found in

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“…Other groups of researchers have suggested that lec-8 is involved in resistance to bacterial infection. 25,26) It will be necessary to combine the results of the 3 different approaches described above to understand the functions of galectins in C. elegans in vivo. The K a and K d values for the interaction between LEC-12 and the pyridylaminated oligosaccharides were calculated as described in Materials and Methods.…”

Section: )mentioning

confidence: 99%

The DC2.3 Gene in Caenorhabditis elegans Encodes a Galectin That Recognizes the Galactose.BETA.1.RAR.4Fucose Disaccharide Unit

Nemoto-Sasaki

Takaı̈

Takeuchi

et al. 2011

Biological & Pharmaceutical Bulletin

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Galectins comprise a large family of b b-galactoside-binding proteins in animals and fungi. We previously isolated cDNAs of 10 galectin and galectin-like genes (lec-1 to lec-6 and lec-8 to lec-11) from Caenorhabditis elegans and characterized the carbohydrate-binding properties of their recombinant proteins. In the present study, we isolated cDNA corresponding to an open reading frame of the DC2.3a gene from C. elegans total RNA; this cDNA encodes another potential galectin. A recombinant DC2.3a protein was expressed in Escherichia coli and used for analysis. The protein displayed hemagglutinating activity against rabbit erythrocytes, bound to an asialofetuin-Sepharose column, and was eluted with lactose. Furthermore, frontal affinity chromatography (FAC) analysis confirmed that DC2.3a recognized oligosaccharides with a non-reducing terminal galactose. According to these results, we designated DC2.3 as lec-12. The carbohydrate-binding property of the recombinant DC2.3a/LEC-12a was essentially similar to that of LEC-6. Additionally, DC2.3a/LEC-12a and LEC-6 showed higher affinities for the galactoseb b1→ →4fucose (Galb b1→ →4Fuc) disaccharide than for N-acetyllactosamine. This suggests that the principal recognition unit is the Galb b1→ →4Fuc disaccharide as in the case of the C. elegans galectins. However, the recombinant DC2.3a/LEC-12a showed weak affinity for N-glycan E3, which was previously shown to be a preferential endogenous ligand for LEC-6. The DC2.3a/LEC-12a endogenous ligand structures appear to be somewhat different but contain the same galactose-fucose recognition motif.

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A Caenorhabditis elegans Glycolipid-binding Galectin Functions in Host Defense against Bacterial Infection

Cited by 53 publications

References 38 publications

Nematotoxicity of Marasmius oreades Agglutinin (MOA) Depends on Glycolipid Binding and Cysteine Protease Activity

Nematotoxicity of Marasmius oreades Agglutinin (MOA) Depends on Glycolipid Binding and Cysteine Protease Activity

Galectins in Invertebrates with a focus on <i>Caenorhabditis elegans</i>

The DC2.3 Gene in Caenorhabditis elegans Encodes a Galectin That Recognizes the Galactose.BETA.1.RAR.4Fucose Disaccharide Unit

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