Effects of Size and Geographical Origin on Atlantic salmon, Salmo salar, Mucin O-Glycan Repertoire

Benktander, John; Venkatakrishnan, Vignesh; Padra, János Tamás; Sundh, Henrik; Sundell, Kristina; Murugan, Abarna V. M.; Maynard, Ben T.; Lindén, Sara K.

doi:10.1074/mcp.ra119.001319

Cited by 21 publications

(35 citation statements)

References 33 publications

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“…The supernatants containing the mucins were kept at 4 °C. We have previously demonstrated that these two methods of mucin isolation yield similar O -glycan profiles using liquid-chromatography–mass spectrometry (LC-MS), with differences between O -glycan profiles being of a similar magnitude to those observed among technical replicates within each extraction method [ 3 ].…”

Section: Methodsmentioning

confidence: 99%

“…All mucosal epithelia are covered by a continuously secreted mucus layer and mucins are the main components of the mucus [ 1 , 2 ]. Mucins are comprised of 50–90% carbohydrate in the form of O -glycans, and substantial differences in glycosylation have been demonstrated in epithelia within and between species [ 3 , 4 ]. However, the inter-individual variation in glycosylation between Atlantic salmon (ATS, Salmo salar ) is very low compared to that of pigs and humans [ 3 , 4 , 5 , 6 , 7 ].…”

Section: Introductionmentioning

confidence: 99%

“…Mucins are comprised of 50–90% carbohydrate in the form of O -glycans, and substantial differences in glycosylation have been demonstrated in epithelia within and between species [ 3 , 4 ]. However, the inter-individual variation in glycosylation between Atlantic salmon (ATS, Salmo salar ) is very low compared to that of pigs and humans [ 3 , 4 , 5 , 6 , 7 ]. Since the large inter-individual variation in humans is considered a population-based defense against infection, the low variation in ATS glycosylation may indicate that they are vulnerable to infection at a population level [ 3 , 4 ].…”

Section: Introductionmentioning

confidence: 99%

“…However, the inter-individual variation in glycosylation between Atlantic salmon (ATS, Salmo salar ) is very low compared to that of pigs and humans [ 3 , 4 , 5 , 6 , 7 ]. Since the large inter-individual variation in humans is considered a population-based defense against infection, the low variation in ATS glycosylation may indicate that they are vulnerable to infection at a population level [ 3 , 4 ]. Furthermore, glycosylation can change with infection and inflammation [ 5 , 8 ].…”

Section: Introductionmentioning

confidence: 99%

“…Skin O -glycans from ATS have been identified as being of core type 1, 2, 3 and 5 and relatively short (2–6 monosaccharides) [ 4 ]. The ATS mucin O -glycans are highly sialylated (~90% sialylation), with N -acetylneuraminic acid (NeuAc) being the most abundant sialic acid found both in skin and intestine, while N -glycolylneuraminic acid (NeuGc)- and keto-deoxynononic acid (Kdn)-containing structures were only detected on skin mucins [ 3 , 4 ]. The gill mucin glycosylation has not been studied in detail previously.…”

Section: Introductionmentioning

confidence: 99%

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Gill Mucus and Gill Mucin O-glycosylation in Healthy and Amebic Gill Disease-Affected Atlantic Salmon

et al. 2020

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Amoebic gill disease (AGD) causes poor performance and death in salmonids. Mucins are mainly comprised by carbohydrates and are main components of the mucus covering the gill. Since glycans regulate pathogen binding and growth, glycosylation changes may affect susceptibility to primary and secondary infections. We investigated gill mucin O-glycosylation from Atlantic salmon with and without AGD using liquid chromatography–mass spectrometry. Gill mucin glycans were larger and more complex, diverse and fucosylated than skin mucins. Confocal microscopy revealed that fucosylated mucus coated sialylated mucus strands in ex vivo gill mucus. Terminal HexNAcs were more abundant among O-glycans from AGD-affected Atlantic salmon, whereas core 1 structures and structures with acidic moieties such as N-acetylneuraminic acid (NeuAc) and sulfate groups were less abundant compared to non-infected fish. The fucosylated and NeuAc-containing O-glycans were inversely proportional, with infected fish on the lower scale of NeuAc abundance and high on fucosylated structures. The fucosylated epitopes were of three types: Fuc-HexNAc-R, Gal-[Fuc-]HexNAc-R and HexNAc-[Fuc-]HexNAc-R. These blood group-like structures could be an avenue to diversify the glycan repertoire to limit infection in the exposed gills. Furthermore, care must be taken when using skin mucus as proxy for gill mucus, as gill mucins are distinctly different from skin mucins.

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Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Gill Mucus and Gill Mucin O-glycosylation in Healthy and Amebic Gill Disease-Affected Atlantic Salmon

et al. 2020

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Lectin binding to pectoral fin of neonate little skates reared under ambient and projected‐end‐of‐century temperature regimes

Thomas,

Peele,

Yopak

et al. 2024

Journal of Morphology

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The glycosylation of macromolecules can vary both among tissue structural components and by adverse conditions, potentially providing an alternative marker of stress in organisms. Lectins are proteins that bind carbohydrate moieties and lectin histochemistry is a common method to visualize microstructures in biological specimens and diagnose pathophysiological states in human tissues known to alter glycan profiles. However, this technique is not commonly used to assess broad‐spectrum changes in cellular glycosylation in response to environmental stressors. In addition, the binding of various lectins has not been studied in elasmobranchs (sharks, skates, and rays). We surveyed the binding tissue structure specificity of 14 plant‐derived lectins, using both immunoblotting and immunofluorescence, in the pectoral fins of neonate little skates (Leucoraja erinacea). Skates were reared under present‐day or elevated (+5°C above ambient) temperature regimes and evaluated for lectin binding as an indicator of changing cellular glycosylation and tissue structure. Lectin labeling was highly tissue and microstructure specific. Dot blots revealed no significant changes in lectin binding between temperature regimes. In addition, lectins only detected in the elevated temperature treatment were Canavalia ensiformis lectin (Concanavalin A) in spindle cells of muscle and Ricinus communis agglutinin in muscle capillaries. These results provide a reference for lectin labeling in elasmobranch tissue that may aid future investigations.

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Mucin modified SPR interfaces for studying the effect of flow on pathogen binding to Atlantic salmon mucins

Padra

Pagneux

Bouckaert

et al. 2019

Biosensors and Bioelectronics

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et al.. Mucin modified SPR interfaces for studying the effect of flow on pathogen binding to Atlantic salmon mucins. Biosensors and Bioelectronics, Elsevier, 2019, 146, pp. AbstractKnowledge on host-pathogen interactions contributes to the development of approaches to alleviate infectious disease. In this work, we developed a surface plasmon resonance (SPR) based method for investigating bacteria/mucins interactions. Furthermore, we investigated adhesion of three pathogens, Aeromonas salmonicida, Aeromonas hydrophila and Vibrio harveyi, to Atlantic salmon mucins isolated from different epithelial sites, using SPR and microtiter-based binding assays. We demonstrated that performing bacterial binding assays to mucins using SPR is feasible and has advantages over microtiter-based binding assays, especially under flow conditions. The fluid flow in the SPR is linear and continuous and SPR enables real-time reading of mucin-bacterial bonds, which provides an in vivo-like setup for analysis of bacterial binding to mucins. The variation between technical replicates was smaller using SPR detection compared to the adenosine 5'-triphosphate (ATP) bioluminescence assay in microtiter plates. Furthermore, we demonstrated that the effect of flow on pathogen-mucin interaction is significant and that bacterial adhesion differ non-linearly with flow rates and depend on the epithelial source of the mucin.

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Effects of Size and Geographical Origin on Atlantic salmon, Salmo salar, Mucin O-Glycan Repertoire

Cited by 21 publications

References 33 publications

Gill Mucus and Gill Mucin O-glycosylation in Healthy and Amebic Gill Disease-Affected Atlantic Salmon

Gill Mucus and Gill Mucin O-glycosylation in Healthy and Amebic Gill Disease-Affected Atlantic Salmon

Lectin binding to pectoral fin of neonate little skates reared under ambient and projected‐end‐of‐century temperature regimes

Mucin modified SPR interfaces for studying the effect of flow on pathogen binding to Atlantic salmon mucins

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