Structural characterization and biological implications of sulfated<i>N</i>-glycans in a serine protease from the neotropical moth<i>Hylesia metabus</i>(Cramer [1775]) (Lepidoptera: Saturniidae)

Cabrera, Gleysin; Salazar, Víctor; Montesino, Raquel; Támbara, Yanet; Struwe, Weston B.; Leon, Evelyn; Harvey, David J.; Lesur, Antoine; Rincón, Mónica; Domon, Bruno; Méndez, Milagros; Portela, Madelón; González-Hernández, Annia; Triguero, Ada; Durán, Rosario; Lundberg, Ulf; Vonasek, Eva; González, Luís Javier Durán

doi:10.1093/glycob/cwv096

Cited by 19 publications

(26 citation statements)

References 60 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…A. mellifera , however, also secretes royal jelly comprising proteins carrying common PMGs (Glycans #2a/b, #4, #10a/b, and #12), a unique core β1,6‐mannosylated PMG (Glycan #vii) and a sulfated PMG (Glycan #xi) (Hykollari et al ., ). This unusual sulfo‐PMG (Glycan #xi) was amongst other PMGs (Glycans #4 and #12) also identified in the hair‐like ‘setae’ of the moth Hylesia metabus , which were found to mediate pro‐inflammatory immune reactions in humans (Cabrera et al ., ).…”

Section: Surveying Pmps Across the Eukaryotic Kingdoms And Phylamentioning

confidence: 97%

Human protein paucimannosylation: cues from the eukaryotic kingdoms

et al. 2019

View full text Add to dashboard Cite

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...

show abstract

Section: Surveying Pmps Across the Eukaryotic Kingdoms And Phylamentioning

confidence: 97%

Human protein paucimannosylation: cues from the eukaryotic kingdoms

et al. 2019

View full text Add to dashboard Cite

show abstract

“…In terms of N-glycans, sulphation of α-linked mannose and/or core α1,6-fucose is known from arthropods (specifically a lobster as well as insects; see examples in Fig. 1) and from Dictyostelium [21,[85][86][87][88], while sulphation of galactose is a feature of the Eastern oyster [89]. Based on studies with radioactive SO 4 labelling and PNGase F treatment, the occurrence of sulphated N-linked oligosaccharide chains on glycoproteins involved in sea urchin embryonic skeleton formation was postulated [90]; these glycan chains, recognised by the 1223 antibody, apparently bind calcium [91], but their exact structures were not defined.…”

Section: Sulphatementioning

confidence: 99%

Anionic and zwitterionic moieties as widespread glycan modifications in non-vertebrates

Paschinger

Wilson

2019

Glycoconj J

View full text Add to dashboard Cite

Glycan structures in non-vertebrates are highly variable; it can be assumed that this is a product of evolution and speciation, not that it is just a random event. However, in animals and protists, there is a relatively limited repertoire of around ten monosaccharide building blocks, most of which are neutral in terms of charge. While two monosaccharide types in eukaryotes (hexuronic and sialic acids) are anionic, there are a number of organic or inorganic modifications of glycans such as sulphate, pyruvate, phosphate, phosphorylcholine, phosphoethanolamine and aminoethylphosphonate that also confer a 'charged' nature (either anionic or zwitterionic) to glycoconjugate structures. These alter the physicochemical properties of the glycans to which they are attached, change their ionisation when analysing them by mass spectrometry and result in different interactions with protein receptors. Here, we focus on N-glycans carrying anionic and zwitterionic modifications in protists and invertebrates, but make some reference to O-glycans, glycolipids and glycosaminoglycans which also contain such moieties. The conclusion is that 'charged' glycoconjugates are a widespread, but easily overlooked, feature of 'lower' organisms.

show abstract

“…One of the first indications of the capacity of insects to produce complex type N-glycans came from bee venom phospholipase A2, which contains the core α1,3-fucose (an IgE epitope allergenic to humans). Anionic and zwitterionic N-glycans with up to three antennae have more recently been found in a range of insects [29][30][31][32] . Furthermore, Vandenborre et al 33 explored glycosylation differences comparing www.nature.com/scientificreports/ several economically important insects, and found glycoproteins to be involved in a broad range of biological processes such as cellular adhesion, homeostasis, communication and stress response.…”

Section: Discussionmentioning

confidence: 99%

Insights into the salivary N-glycome of Lutzomyia longipalpis, vector of visceral leishmaniasis

Mondragón-Shem

Wongtrakul-Kish

Kozak

et al. 2020

Sci Rep

View full text Add to dashboard Cite

During Leishmania transmission sand flies inoculate parasites and saliva into the skin of vertebrates. Saliva has anti-haemostatic and anti-inflammatory activities that evolved to facilitate bloodfeeding, but also modulate the host's immune responses. Sand fly salivary proteins have been extensively studied, but the nature and biological roles of protein-linked glycans remain overlooked. Here, we characterised the profile of N-glycans from the salivary glycoproteins of Lutzomyia longipalpis, vector of visceral leishmaniasis in the Americas. in silico predictions suggest half of Lu. longipalpis salivary proteins may be N-glycosylated. SDS-PAGE coupled to LC-MS analysis of sand fly saliva, before and after enzymatic deglycosylation, revealed several candidate glycoproteins. to determine the diversity of N-glycan structures in sand fly saliva, enzymatically released sugars were fluorescently tagged and analysed by HPLC, combined with highly sensitive LC-MS/MS, MALDI-TOF-MS, and exoglycosidase treatments. We found that the N-glycan composition of Lu. longipalpis saliva mostly consists of oligomannose sugars, with Man 5 GlcnAc 2 being the most abundant, and a few hybrid-type species. Interestingly, some glycans appear modified with a group of 144 Da, whose identity has yet to be confirmed. Our work presents the first detailed structural analysis of sand fly salivary glycans. Sand flies are small insects that can transmit bacteria and viruses 1,2 , but are known mainly as vectors of leishmaniasis, a disease that threatens 350 million people worldwide 3. When female sand flies feed, they inject a saliva comprised of molecules that facilitate the ingestion of blood, and modulate the host immune system and pathogen transmission 4-6. These effects have led researchers to explore the potential of insect salivary molecules as markers of biting exposure 5,7 (to determine risk of disease), or even as components of vaccines against leishmaniasis 8. Of the many types of molecules that make up saliva, most research has focused on the proteins; here, we have investigated the glycans that modify these proteins. In most eukaryotic cells, the addition of glycans to proteins is a highly conserved and diverse post-translational modification. The most common types of protein-linked glycans are N-linked (attached to asparagine residues in the sequon Asn-X-Thr/Ser), and O-linked (attached to serine or threonine residues). Glycoconjugates display a wide range of biological roles, from organism development to immune system functions against pathogens 9. One study has addressed the types and roles of glycans in insects using the model fruit fly, Drosophila melanogaster. In this species, biological functions have been attributed to different glycan classes, such as morphology and locomotion (N-linked glycans), or cell interaction and signalling (O-linked glycans) 10 .

show abstract

Structural characterization and biological implications of sulfatedN-glycans in a serine protease from the neotropical mothHylesia metabus(Cramer [1775]) (Lepidoptera: Saturniidae)

Cited by 19 publications

References 60 publications

Human protein paucimannosylation: cues from the eukaryotic kingdoms

Human protein paucimannosylation: cues from the eukaryotic kingdoms

Anionic and zwitterionic moieties as widespread glycan modifications in non-vertebrates

Insights into the salivary N-glycome of Lutzomyia longipalpis, vector of visceral leishmaniasis

Contact Info

Product

Resources

About