N-glycan structures of β-HlH subunit of Helix lucorum hemocyanin

Velkova, Lyudmila; Dolashka, Pavlina; Beeumen, Jozef Van; Devreese, Bart

doi:10.1016/j.carres.2017.06.012

Cited by 17 publications

(17 citation statements)

References 51 publications

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“…Furthermore, β1,2‐Xyl‐modified (Glycans #8 and #16) and O ‐methylated (Glycan #vi) PMGs were recently identified from the land snail Helix lucorum (Velkova et al ., ), glyco‐features similarly observed in plants and nematodes. Other gastropods including the land slug Arion lusitanicus , reportedly produce β1,2‐xylosylated and α1,6‐fucosylated PMGs (Glycans #2b, #4, #6b, #8, #10b, #12, and #16), some of which were partially O ‐methylated.…”

Section: Surveying Pmps Across the Eukaryotic Kingdoms And Phylamentioning

confidence: 74%

“…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, ).…”

Section: Introductionmentioning

confidence: 99%

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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: 74%

Section: Introductionmentioning

confidence: 99%

Human protein paucimannosylation: cues from the eukaryotic kingdoms

et al. 2019

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“…New methods and approaches for analyzing the carbohydrate structure of hemocyanin from the snail Helix lucorum (HlH) show а complex carbohydrate structure ( Figure 10 ). The glycans obtained after treatment of βc-HlH with PNGase F are determined by MALDI-MS analyses, mainly as triple charged [M-3H] 3+ ions [ 36 , 37 , 38 ]. The determined methylated monosaccharides in glycan structures may be MeMan or MeGal found in βc-HlH.…”

Section: Carbohydrate Structure Of Hemocyanins From Helimentioning

confidence: 99%

“…The determined methylated monosaccharides in glycan structures may be MeMan or MeGal found in βc-HlH. It is important to note the absence of acid glycans with HexA at βc-HlH ( Figure 11 ) [ 38 ].…”

Section: Carbohydrate Structure Of Hemocyanins From Helimentioning

confidence: 99%

De Novo Structural Determination of the Oligosaccharide Structure of Hemocyanins from Molluscs

et al. 2020

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A number of studies have shown that glycosylation of proteins plays diverse functions in the lives of organisms, has crucial biological and physiological roles in pathogen–host interactions, and is involved in a large number of biological events in the immune system, and in virus and bacteria recognition. The large amount of scientific interest in glycoproteins of molluscan hemocyanins is due not only to their complex quaternary structures, but also to the great diversity of their oligosaccharide structures with a high carbohydrate content (2–9%). This great variety is due to their specific monosaccharide composition and different side chain composition. The determination of glycans and glycopeptides was performed with the most commonly used methods for the analysis of biomolecules, including peptides and proteins, including Matrix Assisted Laser Desorption/Ionisation–Time of Flight (MALDI-TOF-TOF), Liquid Chromatography - Electrospray Ionization-Mass Spectrometry (LC/ESI-MS), Liquid Chromatography (LC-Q-trap-MS/MS) or Nano- Electrospray Ionization-Mass Spectrometry (nano-ESI-MS) and others. The molluscan hemocyanins have complex carbohydrate structures with predominant N-linked glycans. Of interest are identified structures with methylated hexoses and xyloses arranged at different positions in the carbohydrate moieties of molluscan hemocyanins. Novel acidic glycan structures with specific glycosylation positions, e.g., hemocyanins that enable a deeper insight into the glycosylation process, were observed in Rapana venosa, Helix lucorum, and Haliotis tuberculata. Recent studies demonstrate that glycosylation plays a crucial physiological role in the immunostimulatory and therapeutic effect of glycoproteins. The remarkable diversity of hemocyanin glycan content is an important feature of their immune function and provides a new concept in the antibody–antigen interaction through clustered carbohydrate epitopes.

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“…Glycoproteins are polysaccharide-peptide or polysaccharide-protein complexes of varying structures and bioactivities when compared to those of polysaccharides [6][7][8][9]. The analysis of glycopeptide structure involves polysaccharide chain elucidation prior to that of the peptide chain [10] as well as monosaccharide composition, glycosidic linkage configuration, monosaccharide sequence [11] and secondary and 3D structure determination [12]. Sialic acid, a nine-carbon monosaccharide derivative, is often located at the terminal monosaccharide of glycoproteins existing in various biological tissues [13,14] and forms an important basis of the glycoprotein/glycopeptide functional diversity [15,16].…”

Section: Introductionmentioning

confidence: 99%

Isolation and Characterization of a Novel Sialoglycopeptide Promoting Osteogenesis from Gadus morhua Eggs

et al. 2019

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Gadus morhua eggs contain several nutrients, including polyunsaturated fatty acids, lecithin and glycoproteins. A novel sialoglycopeptide from the eggs of G. morhua (Gm-SGPP) was extracted with 90% phenol and purified by Q Sepharose Fast Flow (QFF) ion exchange chromatography, followed by S-300 gel filtration chromatography. Gm-SGPP contained 63.7% carbohydrate, 16.2% protein and 18.6% N-acetylneuraminic acid. High-performance size exclusion chromatography and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) demonstrated that Gm-SGPP is a 7000-Da pure sialoglycopeptide. β-elimination reaction suggested that Gm-SGPP contained N-glycan units. Amino acid N-terminal sequence analysis indicated the presence of Ala-Ser-Asn-Gly-Thr-Gln-Ala-Pro amino acid sequence. Moreover, N-glycan was connected at the third Asn location of the peptide chain through GlcNAc. Gm-SGPP was composed of D-mannose, D-glucuronic acid and D-galactose. Fourier transform-infrared spectroscopy (FT-IR), 1H-nuclear magnetic resonance spectroscopy (1H-NMR) and methylation analysis were performed to reveal the structure profile of Gm-SGPP. In vitro results showed that the proliferation activity of MC3T3-E1 cells was significantly promoted by Gm-SGPP. In vivo data revealed that Gm-SGPP increased the calcium and phosphorus content of tibias and promoted longitudinal bone growth in adolescent rats.

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N-glycan structures of β-HlH subunit of Helix lucorum hemocyanin

Cited by 17 publications

References 51 publications

Human protein paucimannosylation: cues from the eukaryotic kingdoms

Human protein paucimannosylation: cues from the eukaryotic kingdoms

De Novo Structural Determination of the Oligosaccharide Structure of Hemocyanins from Molluscs

Isolation and Characterization of a Novel Sialoglycopeptide Promoting Osteogenesis from Gadus morhua Eggs

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