Structural studies of the acidic oligosaccharide units from bovine glycophorin

Fukuda, Kayoko; Kawashima, Ikuo; Tomita, Motowo; Hamada, Akira

doi:10.1016/0304-4165(82)90180-5

Cited by 22 publications

(4 citation statements)

References 26 publications

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“…We have now also shown that less than 2% of a 3H-Iabeled EMC virus preparation became bound to bovine erythrocytes, whereas close to 80% attached to human cells (Table V). jV-Acetylneuraminic acid is apparently the only sialic acid species present in human erythrocytes (Klenk et al, 1955), while the predominant sialic acid in bovine erythrocytes is jV-glycolylneuraminic acid (Fukuda et al, 1982). To examine the possibility that EMC virus does not interact with bovine erythrocytes because it cannot recognize receptors containing TV-glycolylneuraminic acid, we measured attachment to equine erythrocytes, the sialic acid of which is 99% A-glycolyl derivative (Reuter et al, 1988).…”

Section: Resultsmentioning

confidence: 99%

Evidence for a direct role for sialic acid in the attachment of encephalomyocarditis virus to human erythrocytes

Tavakkol¹,

Burness²

1990

Biochemistry

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Sialic acid residues are required in cellular receptors for many different mammalian viruses. Sialic acid could have a direct role, being an integral part of the virus binding site on the receptor. Alternatively, negatively charged sialic acid could have an indirect role, being responsible for holding the receptor in the required configuration for virus recognition, for instance, by interacting with positively charged amino acid residues found in the polypeptide chain of receptors. We have investigated the role of sialic acid in virus attachment by studying the interaction of the small RNA virus encephalomyocarditis (EMC) with glycophorin A, its receptor on human erythrocytes. In several experiments, influenza virus A was used for control purposes. Blocking positive charges on glycophorin either in lysine residues by acetylation or in arginine residues with butanedione did not affect its interaction with EMC virus. In contrast, blocking negatively charged carboxyl groups in sialic acid residues by amidation destroyed the ability of glycophorin to inhibit EMC virus attachment suggesting an important role for this part of sialic acid in EMC virus attachment. Removal of the polyhydroxy side chain in sialic acid residues of glycophorin by mild oxidation with periodate followed by reduction with borohydride had little effect on its interaction with EMC virus. Further, sialic acid species with either an acetyl or glycolyl group attached to the amino group on position 5 interacted equally well with EMC virus.(ABSTRACT TRUNCATED AT 250 WORDS)

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Section: Resultsmentioning

confidence: 99%

Evidence for a direct role for sialic acid in the attachment of encephalomyocarditis virus to human erythrocytes

Tavakkol¹,

Burness²

1990

Biochemistry

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“…There are several reports on the sialic acid component of both human and non-human sources of glycophorin. In human, glycophorin contains NeuAc, whereas the presence of NeuGc has been reported in horse [ 34 ], bovine [ 35 ], porcine [ 36 ] and monkey [ 37 ] glycophorin. However, to date, little is known about sialic acid in teleost glycophorins.…”

Section: Discussionmentioning

confidence: 99%

Isolation and Characterization of Glycophorin from Carp Red Blood Cell Membranes

et al. 2014

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We isolated a high-purity carp glycophorin from carp erythrocyte membranes following extraction using the lithium diiodosalicylate (LIS)-phenol method and streptomycin treatment. The main carp glycophorin was observed to locate at the position of the carp and human band-3 proteins on an SDS-polyacrylamide gel. Only the N-glycolylneuraminic acid (NeuGc) form of sialic acid was detected in the carp glycophorin. The oligosaccharide fraction was separated into two components (P-1 and P-2) using a Glyco-Pak DEAE column. We observed bacteriostatic activity against five strains of bacteria, including two known fish pathogens. Fractions from the carp erythrocyte membrane, the glycophorin oligosaccharide and the P-1 also exhibited bacteriostatic activity; whereas the glycolipid fraction and the glycophorin fraction without sialic acid did not show the activity. The carp glycophorin molecules attach to the flagellum of V. anguillarum or the cell surface of M. luteus and inhibited bacterial growth.

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“…On the other hand, glycophorin patterns (PAS-stained band patterns) are different in humans [ 136 ], and these differences are caused by the component containing oligosaccharides. The glycophorins from horse [ 139 ], bovine [ 140 ], pig [ 141 ], and goat contain sialic acid as NeuGc ( N -glycolylneuraminic acid), not as NeuAc [ 142 ]. While the sialic acid of dog [ 143 ] and mouse [ 144 ] is NeuAc, canine individuals containing only NeuGc have been reported.…”

Section: Glycoproteins In Red Cell Membranes Of Non-human Originmentioning

confidence: 99%

A Comprehensive Review of Our Current Understanding of Red Blood Cell (RBC) Glycoproteins

Aoki

2017

Membranes

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Human red blood cells (RBC), which are the cells most commonly used in the study of biological membranes, have some glycoproteins in their cell membrane. These membrane proteins are band 3 and glycophorins A–D, and some substoichiometric glycoproteins (e.g., CD44, CD47, Lu, Kell, Duffy). The oligosaccharide that band 3 contains has one N-linked oligosaccharide, and glycophorins possess mostly O-linked oligosaccharides. The end of the O-linked oligosaccharide is linked to sialic acid. In humans, this sialic acid is N-acetylneuraminic acid (NeuAc). Another sialic acid, N-glycolylneuraminic acid (NeuGc) is present in red blood cells of non-human origin. While the biological function of band 3 is well known as an anion exchanger, it has been suggested that the oligosaccharide of band 3 does not affect the anion transport function. Although band 3 has been studied in detail, the physiological functions of glycophorins remain unclear. This review mainly describes the sialo-oligosaccharide structures of band 3 and glycophorins, followed by a discussion of the physiological functions that have been reported in the literature to date. Moreover, other glycoproteins in red blood cell membranes of non-human origin are described, and the physiological function of glycophorin in carp red blood cell membranes is discussed with respect to its bacteriostatic activity.

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Structural studies of the acidic oligosaccharide units from bovine glycophorin

Cited by 22 publications

References 26 publications

Evidence for a direct role for sialic acid in the attachment of encephalomyocarditis virus to human erythrocytes

Evidence for a direct role for sialic acid in the attachment of encephalomyocarditis virus to human erythrocytes

Isolation and Characterization of Glycophorin from Carp Red Blood Cell Membranes

A Comprehensive Review of Our Current Understanding of Red Blood Cell (RBC) Glycoproteins

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