The carbohydrate moiety of serum IgM from Atlantic cod (Gadus morhua L.)

Magnadóttir, Bergljót; Crispin, Max; Royle, Louise; Colominas, Cristina; Harvey, David J.; Dwek, Raymond A.; Rudd, Pauline M.

doi:10.1006/fsim.2001.0364

Cited by 21 publications

(12 citation statements)

References 47 publications

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“…This clearly indicates that sea bass Ig is glycoprotein in nature and the carbohydrates are linked to both H and L chains as had been reported from several teleostean species [2, 22,23].…”

Section: Discussionsupporting

confidence: 77%

“…The presence of carbohydrates in the heavy chain of mammalian IgM is important for C1q binding and complement activation through the Cµ3 domain [21]. The carbohydrate moiety of Salmo salar and Gadus morhua IgM was estimated to be approximately 12.5% and 10% of the whole molecule, respectively [22,23]. Recently, monoclonal antibodies were developed to Indian major carp, rohu (Labeo rohita) immunoglobulins as a diagnostic reagent in ELISA and immunocytochemical assays [24].…”

Section: Introductionmentioning

confidence: 99%

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Isolation and characterization of immunoglobulin M of Asian sea bass, Lates calcarifer and its level in serum

Choudhury

Prasad

2011

Open Life Sciences

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Asian sea bass immunoglobulin M (IgM) was purified from the sera of Lates calcarifer by affinity chromatography. Analysis of the purified IgM on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) under reducing and non-reducing conditions revealed that the sea bass IgM was a tetrameric protein with a molecular weight of 896 kDa; it contained an equimolar heavy chain and light chain with molecular weight of 83 kDa and 27 kDa respectively. However, besides the covalently linked tetrameric IgM, noncovalently linked tetramer dissociated into dimeric and monomeric forms also demonstrated by non-reducing SDS-PAGE. Carbohydrate moieties were found to be linked with both heavy and light chains. A polyclonal rabbit anti-Asian sea bass IgM was prepared which showed a specific reaction of anti-fish IgM antibody with IgM of sea bass. Sea bass IgM concentration was determined in the serum by indirect ELISA. The average IgM concentration in the sera of the healthy sea bass was 5.4±1.8 mg ml−1; it amounted to 16.7% of the total serum protein.

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“…This clearly indicates that sea bass Ig is glycoprotein in nature and the carbohydrates are linked to both H and L chains as had been reported from several teleostean species [2, 22,23].…”

Section: Discussionsupporting

confidence: 77%

Section: Introductionmentioning

confidence: 99%

Isolation and characterization of immunoglobulin M of Asian sea bass, Lates calcarifer and its level in serum

Choudhury

Prasad

2011

Open Life Sciences

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“…Another trait of the 3 cod species mentioned is that they express relatively high natural immunoglobulin levels in the blood (Israelson et al 1991, Magnadóttir et al 2002a, Dacanay et al 2004. Although individual variation exists, serum concentrations in cod are about 10 times as high as in salmon.…”

Section: Antibody Responses and Genesmentioning

confidence: 99%

Viral and bacterial diseases of Atlantic cod Gadus morhua, their prophylaxis and treatment: a review

Samuelsen¹,

Nerland²,

Jørgensen³

et al. 2006

Dis. Aquat. Org.

112

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This review summarises the state of knowledge of both viral and bacterial diseases of Atlantic cod Gadus morhua, and their diagnosis, prophylaxis and treatment. The most important losses have been at the larval and juvenile stages, and vibriosis has long been the most important bacterial disease in cod, with Listonella (Vibrio) anguillarum dominant among pathogenic isolates. Vaccination of cod against pathogens such as L. anguillarum and Aeromonas salmonicida clearly demonstrates that the cod immune system possesses an effective memory and appropriate mechanisms sufficient for protection, at least against some diseases. Well-known viruses such as the nodavirus that causes viral encephalopathy and retinopathy (VER), infectious pancreatic necrosis virus (IPNV) and viral haemorrhagic septicaemia virus (VHSV) have been isolated from Atlantic cod and can be a potential problem under intensive rearing conditions. No commercial vaccines against nodavirus are currently available, whereas vaccines against IPNV infections based upon inactivated virus as well as IPNV recombinant antigens are available. A number of investigations of the pharmacokinetic properties of antibacterial agents in cod and their efficacy in treating bacterial infections have been reviewed.

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“…Very little is known about the glycosylation of fish IgM; some early work reported compositions of the glycans from bony fish, namely pike IgM [3] and Atlantic salmon [4] but no structural details were elucidated. A later study on IgM from Atlantic cod [5] revealed a series of bi-and triantennary N-linked glycans of the type normally found in mammals. This paper reports the structures of N-linked glycans released from 19S IgM heavy chain from the cartilaginous fish, nurse shark (Ginglymostoma cirratum), a species whose IgM has seven consensus sequences for N-linked glycosylation [6], but for which there appear to be no details of the attached glycans.…”

Section: Introductionmentioning

confidence: 97%

Identification of high-mannose and multiantennary complex-type N-linked glycans containing α-galactose epitopes from Nurse shark IgM heavy chain

et al. 2009

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MALDI-TOF mass spectrometry, negative ion nano-electrospray MS/MS and exoglycosidase digestion were used to identify 36 N-linked glycans from 19S IgM heavy chain derived from the nurse shark (Ginglymostoma cirratum). The major glycan was the high-mannose compound, Man(6)GlcNAc(2) accompanied by small amounts of Man(5)GlcNAc(2), Man(7)GlcNAc(2) and Man(8)GlcNAc(2). Bi- and tri-antennary (isomer with a branched 3-antenna) complex-type glycans were also abundant, most contained a bisecting GlcNAc residue (beta1-->4-linked to the central mannose) and with varying numbers of alpha-galactose residues capping the antennae. Small amounts of monosialylated glycans were also found. This appears to be the first comprehensive study of glycosylation in this species of animal. The glycosylation pattern has implications for the mechanism of activation of the complement system by nurse shark IgM.

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The carbohydrate moiety of serum IgM from Atlantic cod (Gadus morhua L.)

Cited by 21 publications

References 47 publications

Isolation and characterization of immunoglobulin M of Asian sea bass, Lates calcarifer and its level in serum

Isolation and characterization of immunoglobulin M of Asian sea bass, Lates calcarifer and its level in serum

Viral and bacterial diseases of Atlantic cod Gadus morhua, their prophylaxis and treatment: a review

Identification of high-mannose and multiantennary complex-type N-linked glycans containing α-galactose epitopes from Nurse shark IgM heavy chain

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