Galactosylated Fucose Epitopes in Nematodes

Yan, Shi; Bleuler-Martinez, Silvia; Plaza, David Fernando; Künzler, Markus; Aebi, Markus; Joachim, Anja; Razzazi-Fazeli, Ebrahim; Jantsch, Verena; Geyer, Rudolf; Wilson, Iain B. H.; Paschinger, Katharina

doi:10.1074/jbc.m112.353128

Cited by 44 publications

(58 citation statements)

References 45 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The penultimate GlcNAc residue of D1, D3, and D4 are modified with a Hex-Fuc disaccharide, which is presumed to be Gala1-2Fuc. 8 This disaccharide moiety, however, does not affect the interaction, because D4egalactose, which contains this disaccharide unit, was not bound by the antibody. This disaccharide unit was also shown to have no effect on the interaction with the antibody, because no difference was observed between the elution profiles of D4 and E4, though D4 contains this disaccharide unit.…”

Section: Resultsmentioning

confidence: 99%

“…Galb1-4Fuc is a unique disaccharide unit found only in N-glycans of protostomia, 2,8 and some of its roles have been demonstrated in the free-living nematode Caenorhabditis elegans, which is widely used as a multicellular model organism and also as a model of parasitic nematodes. 9 We and others previously demonstrated that Galb1-4Fuc is an endogenous recognition unit of the C. elegans galectin LEC-6.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Preparation of a polyclonal antibody that recognizes a unique galactoseβ1-4fucose disaccharide epitope

Takeuchi

Nishiyama

Saito

et al. 2015

Carbohydrate Research

View full text Add to dashboard Cite

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Preparation of a polyclonal antibody that recognizes a unique galactoseβ1-4fucose disaccharide epitope

Takeuchi

Nishiyama

Saito

et al. 2015

Carbohydrate Research

View full text Add to dashboard Cite

“…Besides these proteins from C. cinerea, galectins from two different Agrocybe species: ACG from Agrocybe cylindracea and AAG from Agrocybe aegerita, have been characterized (Yagi et al 2001;Yang et al 2009) (Table 1). The latter two share 88 % sequence identity Butschi et al 2010;Cooper et al 1997;Titz et al 2009;Walser et al 2004;Yan et al 2012) Gal-β1,4-GlcNAc Gal-β1,4-Glc na nd (Luan et al 2010;Yang et al 2009;Yang et al 2005a;Yang et al 2005b;Yang et al 2005c) ACG Agrocybe cylindracea 160 aa…”

Section: Galectinsmentioning

confidence: 99%

“…XCL is toxic toward the hemipterans A. pisum and Myzus persicae, the dipterans Drosophila melanogaster and A. aegypti, as well as the nematode C. elegans (BleulerMartinez et al 2011;Jaber et al 2008;Trigueros et al 2003). Both the entomotoxic and nematotoxic activity of XCL are dependent on carbohydrate binding, and genetic data suggested that XCL binds to terminal GlcNAc residues in nematode N-glycans (Jaber et al 2008;Yan et al 2012). TAP1 is toxic to C. elegans, A. aegypti, and the amoebozoon A. castellanii .…”

Section: Actinoporin-type Lectinsmentioning

confidence: 99%

“…Thus, in vitro and in vivo experiments suggest that these proteins mediate their toxicity by binding, at the same time, to the Gal-β1,3-GalNAc epitope on mucin-type O-glycans and terminal GlcNAc on N-glycans. This binding mode would lead to clustering of glycoproteins on the intestinal epithelia of insects or nematodes via two types of protein-bound glycans (Chachadi et al 2011;Yan et al 2012). Interestingly, actinoporin-type lectins are also found in primitive plants, where they may also have a role in defense ).…”

Section: Actinoporin-type Lectinsmentioning

confidence: 99%

See 1 more Smart Citation

Entomotoxic and nematotoxic lectins and protease inhibitors from fungal fruiting bodies

Sabotič

Ohm

Künzler

2015

Appl Microbiol Biotechnol

Self Cite

View full text Add to dashboard Cite

Fruiting bodies or sporocarps of dikaryotic (ascomycetous and basidiomycetous) fungi, commonly referred to as mushrooms, are often rich in entomotoxic and nematotoxic proteins that include lectins and protease inhibitors. These protein toxins are thought to act as effectors of an innate defense system of mushrooms against animal predators including fungivorous insects and nematodes. In this review, we summarize current knowledge about the structures, target molecules, and regulation of the biosynthesis of the best characterized representatives of these fungal defense proteins, including galectins, beta-trefoil-type lectins, actinoporin-type lectins, beta-propeller-type lectins and beta-trefoil-type chimerolectins, as well as mycospin and mycocypin families of protease inhibitors. We also present an overview of the phylogenetic distribution of these proteins among a selection of fungal genomes and draw some conclusions about their evolution and physiological function. Finally, we present an outlook for future research directions in this field and their potential applications in medicine and crop protection.

show abstract

N‐glycomic profiling of a glucosidase II mutant of Dictyostelium discoideum by ‘‘off‐line’’ liquid chromatography and mass spectrometry

et al. 2014

Self Cite

View full text Add to dashboard Cite

In this study, we have performed the first mass spectrometric analysis of N-glycans of the M31 mutant strain of the cellular slime mould Dictyostelium discoideum, previously shown to have a defect in glucosidase II. Together with glucosidase I, this enzyme mediates part of the initial processing of N-glycans; defects in either glucosidase are associated with human diseases and result in an accumulation of incorrectly-processed oligosaccharides which are not, or only poor, substrates for a range of downstream enzymes. To examine the effect of the glucosidase II mutation in Dictyostelium, we employed off-line LC-MALDI-TOF-MS in combination with chemical and enzymatic treatments and MS/MS to analyse the neutral and anionic N-glycans of the mutant as compared to the wild-type. The major neutral species were, as expected, of the composition Hex 10-11 HexNAc 2-3 with one or two terminal glucose residues. Consistent with the block in processing of neutral N-glycans caused by the absence of glucosidase II, fucose was apparently absent from the N-glycans and bisecting N-acetylglucosamine was rare. The major anionic oligosaccharides were sulphated and/or methylphosphorylated forms of Hex 8-11 HexNAc 2-3 , many of which surprisingly lacked glucose residues entirely. As anionic Nglycans are considered to be mostly associated with lysosomal enzymes in Dictyostelium, we hypothesise that glycosidases present in the acidic compartments may act on the oligosaccharides attached to such slime mould proteins. Furthermore, our chosen analytical approach enabled us, via observation of diagnostic negative-mode MS/MS fragments, to determine the fine structure of the methylphosphorylated and sulphated N-glycans of the M31 glucosidase mutant in their native state.

show abstract

Galactosylated Fucose Epitopes in Nematodes

Cited by 44 publications

References 45 publications

Preparation of a polyclonal antibody that recognizes a unique galactoseβ1-4fucose disaccharide epitope

Preparation of a polyclonal antibody that recognizes a unique galactoseβ1-4fucose disaccharide epitope

Entomotoxic and nematotoxic lectins and protease inhibitors from fungal fruiting bodies

N‐glycomic profiling of a glucosidase II mutant of Dictyostelium discoideum by ‘‘off‐line’’ liquid chromatography and mass spectrometry

Contact Info

Product

Resources

About