Characterization of the N-linked glycans of Giardia intestinalis

Morelle, Willy; Jimenez, Juan-Carlos; Cieniewski-Bernard, Caroline; Dei‐Cas, Eduardo

doi:10.1093/glycob/cwi035

Cited by 11 publications

(6 citation statements)

References 38 publications

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“…G. lamblia , similar to P. falciparum is proposed to produce hyper‐truncated chitobiose core N ‐glycoproteins due to the absence of key glycosylation enzymes, leaving it unable to produce full‐length LLO precursors (Samuelson et al ., ). Unsurprisingly, we did not identify any literature describing PMP expression nor the presence of any α‐mannosidases and Hex isoenzymes in G. lamblia or in the related G. intestinalis (Morelle et al ., ; Ratner 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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“…1). This robust and highly sensitive mass spectrometric approach for characterizing the glycosylation pattern of proteins, cells, tissues and physiological fluids allows a rapid characterization of the glycoforms as well as their relative quantitation [5][6][7][8][9][10] .…”

Section: Introductionmentioning

confidence: 99%

Analysis of protein glycosylation by mass spectrometry

2007

Self Cite

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We present a detailed protocol for the structural analysis of protein-linked glycans. In this approach, appropriate for glycomics studies, N-linked glycans are released using peptide N-glycosidase F and O-linked glycans are released by reductive alkaline b-elimination. Using strategies based on mass spectrometry (matrix-assisted laser desorption/ionization-time of flight mass spectrometry and nano-electrospray ionization mass spectrometry/mass spectrometry (nano-ESI-MS-MS)), chemical derivatization, sequential exoglycosidase digestions and linkage analysis, the structures of the N-and/or O-glycans are defined. This approach can be used to study the glycosylation of isolated complex glycoproteins or of numerous glycoproteins encountered in a complex biological medium (cells, tissues and physiological fluids).

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“…In addition, identification and characterization of glycan structures in E/S products of G. intestinalis have been reported by Morelle et al (2005). These findings may provide new insights for studies of carbohydrate molecules in the parasite related to the immune response.…”

Section: Introductionmentioning

confidence: 80%

“…In a recent study, Morelle et al (2005), using structural strategies based upon MALDI-TOF and electrospray mass spectrometry, identified major oligosaccharides in E/S products of G. intestinalis, which were constituted by complex structures composed mainly of Gal-β 1-4GlcNAc (LacNAc) and NeuAc alpha 2-6Galbeta 1-4GlcNAc (sialylated LacNAc). Analysis by Western blotting revealed the presence of glycan structures on several proteins that were affected seriously in the serum reactivity after chemical treatment and/or enzymatic deglycosylation of E/S products.…”

Section: Discussionmentioning

confidence: 99%

Excreted/secreted glycoproteins of G. intestinalis play an essential role in the antibody response

Morelle

et al. 2006

Parasitol Res

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In the present work, glycoproteins in the excretory/secretory products of G. intestinalis were identified and the reactivity in serum of immunized mice with these molecules was evaluated by western blotting before and after chemical treatment or enzymatic deglycosylation. Glycoproteins of 58 and 63 kDa were revealed in E/S products after periodic acid-Schiff (PAS) stain. Studies of carbohydrate specificity using digoxigenin-labeled lectins, revealed the presence of O-glycans and N-glycans. Chemical treatment of excretory/secretory products with sodium meta-periodate or enzymatic deglycosylation with N-glycosidase F reduced the reactivity in serum for proteins of 36, 58 and 63 kDa, respectively. These results show the presence of glycoproteins in E/S products of G. intestinalis and suggest that the antibody response is directed against glycoepitopes. The expression of carbohydrate moieties in the E/S-G. intestinalis may play an essential role in the antibody response and may be a target for serodiagnosis or immune intervention in human giardiasis.

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Characterization of the N-linked glycans of Giardia intestinalis

Cited by 11 publications

References 38 publications

Human protein paucimannosylation: cues from the eukaryotic kingdoms

Human protein paucimannosylation: cues from the eukaryotic kingdoms

Analysis of protein glycosylation by mass spectrometry

Excreted/secreted glycoproteins of G. intestinalis play an essential role in the antibody response

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