Plant-TypeN-Glycans Containing Fucose and Xylose in Bryophyta (Mosses) and Tracheophyta (Ferns)

Abstract

The presence of typical plant-type N-glycans (eg, M3FX, Gn2M3FX, and Le a 2M3FX) in mosses, ferns, and other organisms was examined to determine which plant initially acquired glycosyltransferases to produce plant-type N-glycans during organic evolution. No M3FX-type N-glycan was detected in lichens (Cladonia humilis) or in any one of the three preland plants Enteromorpha prolifera, Ulva pertusa Kjellman, and Chara braunii Gmelin. In Bryophyta, M3FX-type Nglycan was detected at trace amounts in Anthocerotopsida (hornworts) and at certain amounts in Bryopsida (mosses), but not in Hepaticopsida (liverworts). Le a 2M3FX was detected in some Bryopsida of relatively high M3FX content. Most Tracheophyta (ferns and higher plants) contained the three typical M3FX-type glycans as the main N-glycans in different ratios. These results suggest that organisms acquired xylosyltransferase and fucosyltransferase during the development of mosses from liverworts, and that later all plants retained both enzymes. Bryopsida have also obtained galactosyltransferase and fucosyltransferase to synthesize the Le a antigen.Key words: N-glycan; fern; moss; M3FX Gn2M3FX and Le a M3FX; Le a antigenSince the structure of the oligosaccharide of pineapple stem bromelain was elucidated, 1) the determined fucoseand xylose-containing core structure has been found universally in plant glycoproteins. M3FX, consisting of three Man (M), two GlcNAc (Gn), and one each of Fuc (F) and Xyl (X) residues is the most common structure in plants. The oligosaccharides GnM3FX and Gn2M3FX, composed of one and two GlcNAc residues respectively attached to M3FX, are also found universally in plants. The oligosaccharide with the Lewis a antigen, Le a 2M3FX, in which galactose and fucose residues are attached to both GlcNAc residues of Gn2M3FX, is also a main N-glycan universally found in plants, [2][3][4][5] except for Brassicaceae plants such as Arabidopsis thaliana and Raphanus sativus (kaiware raddish). Accordingly, the processing of plant N-glycans in the Golgi apparatus as shown in Fig. 1 is assumed to be almost universal. 5,6) N-Glycan processing byglucosidases I and II in ER is important in plants, [7][8][9][10] whereas N-glycan processing in the Golgi apparatus has little effect on plant growth, as determined in the varous studies: Arabidopsis mutants that lack N-acetylglucosaminyltransferase I 11) or both fucosyltrasferase and xylosyltransferase activities 12) grow normally and produce normal seeds. Fucosyltransferase and xylosyltransferase knockout plants of Bryopsida (Physcomitrella patens) grow normally.13) In my study using glycosidase inhibitors on germination, the seedling and leaf growth of R. sativus showed that ER-glucosidase inhibition inhibited the growth of the plant, although the inhibition of N-glycan processing in Golgi by deoxymannojirimycin, swainsonine, and 1,2-dideoxy-2-acetamido-nojirimysin had no eminent effect except for a change in the N-glycan structure. 10,14) These results indicate that the final N-glycan structure is not directly as...

Human protein paucimannosylation: cues from the eukaryotic kingdoms

“…However, building blocks specific to or preferred by some kingdoms, phyla or classes for N ‐glycoprotein production are known, e.g. the frequent usage of β‐D‐xylose (Xyl) in plants (Mega, ), gastropods (Gutternigg et al ., ; Velkova et al ., ) and trematodes (Khoo et al ., ; Hokke et al ., ) and N ‐glycolyl‐α‐D‐neuraminic acid (NeuGc) in non‐human mammals as well as specific glycosidic linkages e.g. α1,3‐linked ‘core’ fucosylation preferred by plants and invertebrates (Rini & Esko, ).…”

Characterization of Three β-Galactoside Phosphorylases from Clostridium phytofermentans

“…GNBs from plant polysaccharides are little known, and LNB is known to exist in biosynthetic intermediates of N-linked glycoproteins during the processing of plant N-glycans in the Golgi apparatus, which is quite a minor component in plants (39). Moreover, there are no endo-␣-N-acetylgalactosaminidase (7,40,41) and lacto-N-biosidase (5) (GNB-and LNB-releasing enzyme, respectively) homologs in the genome of C. phytofermentans.…”

N-glycan transition of the early developmental stage in Oryza sativa

“…MathieuRivet et al (2013) showed that the N-glycan structures in Chlamydomonas reinhardtii, a green unicellular alga, are almost all highmannose type and its xylosylated forms [13], and Mega (2007) has proposed that the appearance of paucimannose type N-glycans was one of the major events in plant evolution [14]. In addition, Ulvskov et al (2013) have proposed that the numbers of glycosyltransferases reflect the process of adaptation in plant evolution [15].…”

“…On the basis of our own work and a series of recent studies, we propose the hypothesis that N-glycan evolution proceeded simultaneously with plant evolution. Thus, the first evolutionarily significant event was the appearance of paucimannose type N-glycans in Bryophyta [14]. These plants developed glycosyltransferases and glycosylhydrolases to convert high-mannose type N-glycan into paucimannose type N-glycan.…”