Structural Features of<i>N</i>-Glycans Linked to Glycoproteins from Oil Palm Pollen, an Allergenic Pollen*

Kimura, Yoshinobu; Yoshiie, Takeo; Kit, Woo Kwan; Maeda, Megumi; Kimura, M.; Tan, Siang Hee

doi:10.1271/bbb.67.2232

Cited by 9 publications

(9 citation statements)

References 19 publications

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“…Concerning plant allergens, the abundant natural allergens from peanuts ( Arachis hypogaea ), olives ( Olea europaea ) and rubber plants ( Hevea brasiliensis ) including Ara h1, Ole e1 and Hev b4 were found to be decorated with the plant‐typic M3, M3X and M3FX (Glycans #4, #8, and #24) (Kolarich & Altmann, ; Kolarich, Altmann, & Sunderasan, ). In addition, common wild‐type mung beans ( Phaseolus aureus ) (Hori & Elbein, ; Pabst et al ., ), soya beans ( Glycine max ) (Kimura, Ohno, & Takagi, ), kidney beans ( Phaseolus vulgaris ) (Sturm et al ., ), jack beans ( Canavalia ensiformis ) (Kimura, Hess, & Sturm, ), pea seeds ( Pisum sativum ) (Kimura, Ohno, & Takagi, ), ginkgo ( Ginkgo biloba ) seeds and pollen (Kimura, Suzuki, & Kimura, ), ginger ( Zingiber officinale ) (Wang et al ., ), papaya ( Carica papaya ) (Makino et al ., ), castor beads ( Ricinus communis ) (Kimura et al ., ), oil palm ( Elaeis guineensis ) (Kimura et al ., ), miracle fruit ( Richardella dulcifica ) (Takahashi et al ., ) and zucchini ( Cucurbita pepo ) (Altmann, ) were reported naturally to express soluble PMPs. Furthermore, the legume‐derived Lotus japonicus convicilin storage protein 2, a homologue of the Ara h 1 allergen (Kolarich & Altmann, ), was shown to carry PMGs (Glycans #8, #22a/b, and #24) (Dam et al ., ).…”

Section: Surveying Pmps Across the Eukaryotic Kingdoms And Phylamentioning

confidence: 99%

Human protein paucimannosylation: cues from the eukaryotic kingdoms

et al. 2019

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Paucimannosidic proteins (PMPs) are bioactive glycoproteins carrying truncated α-or β-mannosyl-terminating asparagine (N )-linked glycans widely reported across the eukaryotic domain. Our understanding of human PMPs remains limited, despite findings documenting their existence and association with human disease glycobiology. This review comprehensively surveys the structures, biosynthetic routes and functions of PMPs across the eukaryotic kingdoms with the aim of synthesising an improved understanding on the role of protein paucimannosylation in human health and diseases. Convincing biochemical, glycoanalytical and biological data detail a vast structural heterogeneity and fascinating tissue-and subcellular-specific expression of PMPs within invertebrates and plants, often comprising multi-α1,3/6-fucosylation and β1,2-xylosylation amongst other glycan modifications and non-glycan substitutions e.g. O-methylation. Vertebrates and protists express less-heterogeneous PMPs typically only comprising variable core fucosylation of bi-and trimannosylchitobiose core glycans. In particular, the Manα1,6Manβ1,4GlcNAc(α1,6Fuc)β1,4GlcNAcβAsn glycan (M2F) decorates various human neutrophil proteins reportedly displaying bioactivity and structural integrity demonstrating that they are not degradation products. Less-truncated paucimannosidic glycans (e.g. M3F) are characteristic glycosylation features of proteins expressed by human cancer and stem cells. Concertedly, these observations suggest the involvement of human PMPs in processes related to innate immunity, tumorigenesis and cellular differentiation. The absence of human PMPs in diverse bodily fluids studied under many (patho)physiological conditions suggests extravascular residence and points to localised functions of PMPs in peripheral tissues. Absence of PMPs in Fungi indicates that paucimannosylation is common, but not universally conserved, in eukaryotes. Relative to human PMPs, the expression of PMPs in plants, invertebrates and protists is more tissue-wide and constitutive yet, similar to their human counterparts, PMP expression remains regulated by the physiology of the producing organism and PMPs evidently serve essential functions in development, cell-cell communication and host-pathogen/symbiont interactions. In most PMP-producing organisms, including humans, the N -acetyl-β-hexosaminidase isoenzymes and linkage-specific α-mannosidases are glycoside hydrolases critical for generating PMPs via N -acetylglucosaminyltransferase I (GnT-I)-dependent and GnT-I-independent truncation pathways. However, the identity and structure of many species-specific PMPs in eukaryotes, their biosynthetic routes, strong tissue-and development-specific expression, and diverse functions are still elusive. Deep exploration of these PMP features involving, for example, the characterisation of endogenous PMP-recognising lectins across a variety of healthy and N -acetyl-β-hexosaminidase-deficient human tissue types and identification of microbial adhesins reactive to human PMPs, are amongs...

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Section: Surveying Pmps Across the Eukaryotic Kingdoms And Phylamentioning

confidence: 99%

Human protein paucimannosylation: cues from the eukaryotic kingdoms

et al. 2019

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“…Fax: +81-86-251-8388; E-mail: yosh8mar@cc.okayama-u.ac.jp Abbreviations: PA-, pyridylamino; RP-HPLC, reverse-phase HPLC; SF-HPLC, size-fractionation HPLC; ESI-MS, electrospray ionization mass spectrometry; Hex, hexose; HexNAc, N-acetylhexosamine; Deoxhex, deoxyhexose; Pen, pentose; MFX, Xyl1-2Man1-4GlcNAc1-4(Fuc1-3)GlcNAc-PA; M3FX, Man1-6(Man1-3)(Xyl1-2)Man1-4GlcNAc1-4(Fuc1-3)GlcNAc-PA; GN1M3FX, GlcNAc1-2Man1-6(Man1-3)(Xyl1-2)Man1-4GlcNAc1-4(Fuc1-3)GlcNAc-PA; GN2M3FX, GlcNAc1-2Man1-6(GlcNAc1-2Man1-3)(Xyl1-2)Man1-4GlcNAc1-4(Fuc1-3)GlcNAc-PA; GFGN2M3FX, Gal 1 Fuc 1 GlcNAc 2 Man 3 Xyl 1 Fuc 1 GlcNAc 2 -PA; G2F2GN2M3FX, Gal 2 Fuc 2 GlcNAc 2 Man 3 Xyl 1 Fuc 1 GlcNAc 2 -PA column (0:6 Â 25 cm) from Nacalai Tesque (Kyoto). GN2M3FX and M3FX were prepared from the glycoproteins of oil palm pollens and ricin D. 10,11) GN1M3FX was prepared from glycoproteins of oil palm pollens 10) and Ginkgo biloba pollens. 12) -Mannosidase (jack bean) and 1-3/6 specific -galactosidase (recombinant expressed in E. coli) were purchased from Sigma (St. Louis, MO).…”

Section: Methodsmentioning

confidence: 99%

Glycoform Analysis of Japanese Cedar Pollen Allergen, Cry j 1

Maeda

Kamamoto

Hino

et al. 2005

Bioscience, Biotechnology, and Biochemistry

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In our previous study (Y. Kimura et al., Biosci. Biotechnol. Biochem., 69, 137-144 (2005)), we found that plant complex type N-glycans harboring Lewis a epitope are linked to the mountain cedar pollen allergen Jun a 1. Jun a 1 is a glycoprotein highly homologous with Japanese cedar pollen glycoallergen, Cry j 1. Although it has been found that some plant complex type N-glycans are linked to Cry j 1, the occurrence of Lewis a epitope in the N-glycan moiety has not been proved yet. Hence, we reinvestigated the glycoform of the pollen allergen to find whether the Lewis a epitope(s) occur in the N-glycan moiety of Cry j 1. From the cedar pollen glycoallergen, the N-glycans were liberated by hydrazinolysis and the resulting sugar chains were N-acetylated and then coupled with 2-aminopyridine. Three pyridylaminated sugar chains were purified by reversed-phase HPLC and size-fractionation HPLC. The structures were analyzed by a combination of exo- and endo-glycosidase digestions, sugar chain mapping, and electrospray ionization mass spectrometry (ESI-MS). Structural analysis clearly indicated that Lewis a epitope (Galbeta1-3(Fucalpha1-4)GlcNAcbeta1-), instead of the Galbeta1-4(Fucalpha1-6)GlcNAc, occurs in the N-glycans of Cry j 1.

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“…An Asahipak NH2P-50 column (0:46 Â 25 cm) was purchased from Showa Denko (Tokyo, Japan), and a Cosmosil 5C18-AR column (0:6 Â 25 cm) from Nacalai Tesque (Kyoto, Japan). GN2M3FX and M3FX were prepared from the glycoproteins of oil palm pollens and ricin D. 8,9) GN M3FX was prepared from glycoproteins of oil palm pollens 9) and Ginkgo biloba pollens.…”

Section: Methodsmentioning

confidence: 99%

“…Digestions with jack bean -mannosidase, diplococcal -Nacetylglucosaminidase, and Lacto-N-biosidase were done using about 200 pmol of the PA-sugar chains under the conditions described in our previous reports. [8][9][10] Digestion with the -fucosidase was done using 200 pmol in 25 mM Na-citrate buffer, pH 5.0 for 16 h. The resulting glycosidase-digests were analyzed by SF-HPLC using the Asahipak NH2P-50 column (0:46 Â 25 cm).…”

Section: Electrospray Ionization (Esi) Mass Spectrometrymentioning

confidence: 99%

Occurrence of Lewis a Epitope inN-Glycans of a Glycoallergen, Jun a 1, from Mountain Cedar (Juniperus ashei) Pollen

Kimura

Kamamoto

Maeda

et al. 2005

Bioscience, Biotechnology, and Biochemistry

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We have determined the structures of N-glycans linked to major allergens in the mountain cedar (Juniperus ashei) pollen, Jun a 1. First, two kinds of the pollen glycoallergen (Jun a 1-A and Jun a 1-B) were purified from partially purified Jun a 1 by cation exchange chromatography. The N-glycans were liberated by hydrazinolysis from the two glycoallergens and the resulting sugar chains were N-acetylated and then coupled with 2-aminopyridine. Three pyridylaminated sugar chains were purified by reversed-phase HPLC and size-fractionation HPLC from Jun a 1-A and Jun a 1-B respectively. The structures were determined by a combination of exo-and endo-glycosidase digestions, two dimensional sugar chain mapping, and electrospray ionization mass spectrometry (ESI-MS) analysis. Structural analysis indicated that Lewis a epitope (Gal1-3(Fuc1-4)GlcNAc1-) occurs in the N-glycans of the pollen allergens.

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Structural Features ofN-Glycans Linked to Glycoproteins from Oil Palm Pollen, an Allergenic Pollen*

Cited by 9 publications

References 19 publications

Human protein paucimannosylation: cues from the eukaryotic kingdoms

Human protein paucimannosylation: cues from the eukaryotic kingdoms

Glycoform Analysis of Japanese Cedar Pollen Allergen, Cry j 1

Occurrence of Lewis a Epitope inN-Glycans of a Glycoallergen, Jun a 1, from Mountain Cedar (Juniperus ashei) Pollen

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