Purification and chemical analysis of the erythrocyte receptor for hemagglutinating enteroviruses

Philipson, Lennart; Bengtsson, Stellan; Brishammar, Sture; Svennerholm, Lars; Zetterqvist, Örjan

doi:10.1016/0042-6822(64)90080-7

Cited by 52 publications

(21 citation statements)

References 22 publications

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“…It is conceivable that the residual nucleic acid in the purified microvillus membrane is not a contaminant but actually a structural component of the plasma membrane. A DNA-containing receptor for haemagglutinating enteroviruses has been isolated from human erythrocyte plasma membranes Philipson, Bengtsson, Brishammar, Svennerholm & Zetterqvist, 1964). Further, density-gradient centrifugation of the purified membrane preparation has shown that the nucleic acid component is evenly distributed with the membrane particles (G. G. Forstner & K. J. Isselbacher, unpublished work).…”

Section: Methodsmentioning

confidence: 99%

Rat intestinal microvillus membranes. Purification and biochemical characterization

Forstner

Sabesin

Isselbacher

1968

Biochemical Journal

436

141

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1. A technique is described for the removal of subcellular contaminants from intact rat intestinal brush borders, and for the subsequent separation of a microvillus membrane fraction from a fibrillar residue. 2. Increments in invertase activity, microscopic homogeneity and low nucleic acid content indicate that the microvillus plasma membrane has been extensively purified. Multiple membrane preparations have been shown to be highly reproducible with respect to their invertase specific activity, cholesterol content and phospholipid content. Alkaline phosphatase, leucine aminopeptidase, Mg(2+)- and Ca(2+)-dependent adenosine triphosphatase and seven separate disaccharidases were shown to be predominantly confined to the membrane fraction. 3. The fibrillar fraction has been shown to contain approximately 30% of the total protein of purified brush borders, plus most of the residual nucleic acid contaminant. No evidence was found for the localization of any specific enzyme in this fraction.

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Section: Methodsmentioning

confidence: 99%

Rat intestinal microvillus membranes. Purification and biochemical characterization

Forstner

Sabesin

Isselbacher

1968

Biochemical Journal

436

141

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“…DAF was originally isolated from erythrocytes (14). The relation between the putative erythrocyte virus receptor (15) and the receptor present on nucleated cells is uncertain, and it will be interesting to learn whether anti-DAF antibodies prevent virus-induced hemagglutination.…”

Section: Discussionmentioning

confidence: 99%

Decay-accelerating factor (CD55), a glycosylphosphatidylinositol-anchored complement regulatory protein, is a receptor for several echoviruses.

Bergelson

Chan

Solomon

et al. 1994

Proc. Natl. Acad. Sci. U.S.A.

296

199

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Echoviruses are human pathogens belonging to the picornavirus family. Decay-accelerating factor (DAF) is a glycosylphosphatidylhinostol (GPI)-anchored surface protein that protects cells from lysis by autologous complement. Anti-DAF monoclonal antibodies prevented echovirus 7 attachment to susceptible cells and protected cells from infection. HeLa cells specifically lost the capacity to bind echovirus 7 when treated with phosphatidylinositol-specific phospholipase C, an enzyme that releases GPI-anchored proteins from the cell surface, indicating that the virus receptor, like DAF, is a GPI-anchored protein. Although Chinese hamster ovary cells do not bind echovirus 7, transfectants expressing human DAF bound virus efficiently, and binding was prevented by pretreatment with an anti-DAF monoclonal antibody. Anti-DAF antibodies prevented infection by at least six echovirus seroypes. These results indicate that DAF is the receptor mediating attachment and infection by several echoviruses.

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“…The gel was stained with Coomassie blue. Molecular weight (moI wt) standards (C): a-lactalbumin (mol wt 14 000), soybean trypsin inhibitor (moI wt )20 100), carbonic anhydrase (tool wt 30 000), ovalbumin (mol wt 43 000), bovine serum albumin (mol wt 67 000), phosphorylase B (mol wt 94 000) Protein fraction (about 11 per cent of total) was prepared by extraction of RBSMliposomes with n-butanol in two different ionic environments according to Philipson et al [15]: (i) RBSM-liposomes in PBS or (ii) RBSM-liposomes in 2.5 M CaC12 adjusted to pH 6.7 with NaOH, were mixed with an equal volume of n-butanol. The tubes were shaken briefly and centrifuged at 2 000 x g for 10 minutes.…”

Section: Fig 1 Sds Gel Electrophoresis Of Rbm (A) and Rbsm-liposomementioning

confidence: 99%

Inhibition of rabies virus infection by a soluble membrane fraction from the rat central nervous system

Conti

Hauttecoeur

Morelec

et al. 1988

Archives of Virology

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This paper describes the inhibitory effect of a normal rat brain solubilized membrane preparation (RBSM-liposomes) on rabies virus infection. Rabies virus was incubated with RBSM-liposomes or their separated components (proteins, phospholipids, gangliosides) before infection of CER or neuroblastoma cells. In addition, both RBSM-liposomes and target cells were treated with enzymes prior to the infection step. All these experimental procedures showed that the active components were mainly lipids.

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Purification and chemical analysis of the erythrocyte receptor for hemagglutinating enteroviruses

Cited by 52 publications

References 22 publications

Rat intestinal microvillus membranes. Purification and biochemical characterization

Rat intestinal microvillus membranes. Purification and biochemical characterization

Decay-accelerating factor (CD55), a glycosylphosphatidylinositol-anchored complement regulatory protein, is a receptor for several echoviruses.

Inhibition of rabies virus infection by a soluble membrane fraction from the rat central nervous system

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