Analysis of the Bond between Encephalomyocarditis Virus and Its Human Erythrocyte Receptor by Affinity Chromatography on Virus-sepharose Columns

Allaway, Graham P.; Burness, A. T. H.

doi:10.1099/0022-1317-68-7-1849

Cited by 9 publications

(4 citation statements)

References 21 publications

(18 reference statements)

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“…We have shown previously that attachment of EMC virus to receptors on red cells or the binding of glycophorin to EMC virus-Sepharose is inhibited by NaCl, suggesting that the attachment involves weak ionic bonds (Pardoe & Burness, 1981;Allaway & Burness, 1987). The results presented here are consistent with an important role for the carboxyl group in sialic acid, this negatively charged group possibly interacting with positive charges in the receptor binding site on the virus.…”

Section: Discussionsupporting

confidence: 88%

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: Discussionsupporting

confidence: 88%

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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“…The prototype cardioviruses mengovirus and EMCV, agglutinate human erythrocytes (10), and their attachment to erythrocyte membranes has provided a useful tool for studying virus-receptor interactions. Both mengovirus and EMCV use glycophorin A, a major sialoglycoprotein on the surface of mammalian erythrocytes, for hemagglutination (2,3). In the present study, pretreatment of erythrocytes with neuraminidase demonstrated that sialic acid is required for BeAn virus hemagglutination.…”

Section: Substitutions At Bean Residues Q2161 and G2174 Indicate Contsupporting

confidence: 48%

Amino Acid Substitutions in VP2 Residues Contacting Sialic Acid in Low-Neurovirulence BeAn Virus Dramatically Reduce Viral Binding and Spread of Infection

Kumar

Kallio²,

Luo

et al. 2003

J Virol

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Theiler's murine encephalomyelitis viruses (TMEV) consist of two groups, the high-and low-neurovirulence groups, based on lethality in intracerebrally inoculated mice. Low-neurovirulence TMEV result in a persistent central nervous system infection in mice, leading to an inflammatory demyelinating pathology and disease. Low-but not high-neurovirulence strains use sialic acid as an attachment factor. The recent resolution of the crystal structure of the low-neurovirulence DA virus in complex with the sialic acid mimic sialyllactose demonstrated that four capsid residues make contact with sialic acid through noncovalent hydrogen bonds. To systematically test the importance of these sialic acid-binding residues in viral entry and infection, we mutated three VP2 puff B amino acids proposed to make contact with sialic acid and analyzed the consequences of each amino acid substitution on viral entry and spread. The fourth residue is in the VP3-VP1 cleavage dipeptide and could not be mutated. Our data suggest that residues Q2161 and G2174 are directly involved in BeAn virus attachment to sialic acid and that substitutions of these two residues result in the loss of or reduced viral binding and hemagglutination and in the inability to spread among BHK-21 cells. In addition, a gain of function-revertant virus was recovered with the Q2161A mutation after prolonged passage in cells.The cardiovirus Theiler's murine encephalomyelitis virus (TMEV) consists of two groups based on neurovirulence in intracerebrally (i.c.) inoculated mice: high-neurovirulence strains, such as GDVII, produce acute encephalitis, whereas low-neurovirulence TMEV, such as BeAn and DA, produce persistent central nervous system (CNS) infection, leading to an inflammatory demyelinating process (21,22). Persistent TMEV infection in mice provides a highly relevant experimental animal model for the human demyelinating disease multiple sclerosis, in which a viral infection is believed to play a central pathogenetic role.Attenuating mutations in the high-neurovirulence GDVII genome enable host survival but do not result in persistent CNS infection, suggesting that a genetic element(s) for TMEV persistence is present in only the low-neurovirulence genome (23, 31). Genetic analyses of recombinant TMEV have mapped a major element for persistence to the sequences encoding the capsid proteins (8,23,28). In addition, studies of recombinant viruses in which the capsid sequences of the lowneurovirulence BeAn strain progressively replaced those of the high-neurovirulence GDVII virus starting at the leader N terminus suggest that a conformational determinant involving homologous BeAn sequences in the VP2 puff and VP1 loops is required for persistence (1). The mapping of a genetic element for persistence to the capsid suggests that a virus-receptor interaction(s) underlies TMEV persistence.The low-but not high-neurovirulence TMEV use sialic acid as an attachment factor, and the sialic acid binding phenotype has been correlated with changes in virulence in several virusho...

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“…This might occur as a result of variation in the types of sialic acid presented on the different cells, where stronger binding of ERAV to a particular sialic acid may be more difficult to inhibit with these lectins. Allaway & Burness (1987) demonstrated that treatment of the sialylated glycoprotein glycophorin with neuraminidase prevented it binding to encephalomyocarditis virus-Sepharose columns, indicating a requirement for sialic acid for receptor activity. However, sialoglycoconjugates such as fetuin, which binds to specific sialic acids, were unable to bind the virus.…”

Section: Discussionmentioning

confidence: 99%

Sialic acid acts as a receptor for equine rhinitis A virus binding and infection

Stevenson

Huang

Studdert

et al. 2004

Journal of General Virology

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Equine rhinitis A virus (ERAV) is a member of the genus Aphthovirus, family Picornaviridae, and causes respiratory disease in horses worldwide. To characterize the putative receptor molecule(s) of the ERAV isolate 393/76 (ERAV.393/76) on the surface of Vero and other cells, an assay was developed to measure the binding of purified biotinylated ERAV.393/76 virions to cells by flow cytometry. Using this assay, the level of binding to different cell types correlated with the relative infectivity of ERAV in each cell type. In particular, equine fetal kidney cells, mouse fibroblast cells, rabbit kidney-13 and Crandell feline kidney cells bound virus at high levels and produced high virus yields (¢10 7 TCID 50 ml "1 ). Madin-Darby bovine kidney and baby hamster kidney cells showed little or no binding of virus, producing yields of ¡10 1?8 TCID 50 ml "1 . Treatment of Vero and other cells with sodium periodate and the metabolic inhibitors tunicamycin, benzyl N-acetyl-a-D-galactosamide, D,L-threo-1-phenyl-2-decanoylamino-3-morpholino-1-propanol and proteases indicated that part of the receptor-binding and entry complex for ERAV.393/76 is on N-linked carbohydrates and that the carbohydrate is likely to be present on a protein rather than a lipid backbone. The effect of carbohydrate-specific lectins and neuraminidases on ERAV.393/76 binding and infection of Vero and other cell types implicated a2,3-linked sialic acid residues on the carbohydrate complex in the binding and infection of ERAV.

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Analysis of the Bond between Encephalomyocarditis Virus and Its Human Erythrocyte Receptor by Affinity Chromatography on Virus-sepharose Columns

Cited by 9 publications

References 21 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

Amino Acid Substitutions in VP2 Residues Contacting Sialic Acid in Low-Neurovirulence BeAn Virus Dramatically Reduce Viral Binding and Spread of Infection

Sialic acid acts as a receptor for equine rhinitis A virus binding and infection

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