Coxsackieviruses B1, B3, and B5 use decay accelerating factor as a receptor for cell attachment

Shafren, Darren R.; Bates, Richard C.; Agrez, Michael; Herd, R; Burns, Gordon F.; Barry, Richard D.

doi:10.1128/jvi.69.6.3873-3877.1995

Cited by 261 publications

(127 citation statements)

References 32 publications

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“…Adherent cells were detached by incubation in 15 mM EDTA in Tris-buffered saline (TBS). For each replicate, 5 ϫ 10 5 cells were washed once in TBS and a nonsaturating amount (1,000 to 10,000 cpm) of 35 S-radiolabeled EV70 or 35 S-E11 in serum-free medium (prepared as in reference 18) was added to the cells. After incubation at 33 (EV70) or 37°C (E11) for 1 h, the cells were pelleted and the supernatant was removed.…”

Section: Methodsmentioning

confidence: 99%

“…After an additional 24 h, cells were detached from the culture dishes. A fraction of the cells was processed for 35 S-labeled virus binding, as described above, while the remaining fraction was used to measure transgene expression by flow cytometry, as described previously (17). Briefly, separate analyses were performed using monoclonal antibodies EVR1 (complement control protein domain 1 [CCP1] specific) (18), 11D7 (CCP1 specific) (9), IF7 (CCP2 specific) (5), and 8D11 (CCP4 specific) (9) as primary antibodies, each at a final concentration of 0.2 g/ml.…”

Section: Methodsmentioning

confidence: 99%

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Sialic Acid Functions in Enterovirus 70 Binding and Infection

Alexander

Dimock

2002

J Virol

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The interaction of viruses with host cell receptors is the initial step in viral infection and is an important determinant of virus host range, tissue tropism, and pathogenesis. The complement regulatory protein decayaccelerating factor (DAF/CD55) is an attachment receptor for enterovirus 70 (EV70), a member of the Picornaviridae, commonly associated with an eye infection in humans known as acute hemorrhagic conjunctivitis. In early work, the EV70 receptor on erythrocytes, responsible for its hemagglutinating activity, was shown to be sensitive to neuraminidase, implying an essential role for sialic acid in virus attachment. Here, we extend these results to show that cell surface sialic acid is required for EV70 binding to nucleated cells susceptible to virus infection and that sialic acid binding is important in productive infection. Through the use of site-directed mutagenesis to eliminate the single N-linked glycosylation site of DAF and of a chimeric receptor protein in which the O-glycosylated domain of DAF was replaced by a region of the HLA-B44 molecule, a role in EV70 binding for the sialic acid residues of DAF was excluded, suggesting the existence of at least one additional, sialylated EV70-binding factor at the cell surface. Treatment of cells with metabolic inhibitors of glycosylation excluded a role for the N-linked oligosaccharides of glycoproteins but suggested that O-linked glycosylation is important for EV70 binding.Enterovirus 70 (EV70) is an unusual human pathogen of the Enterovirus genus of the family Picornaviridae. Unlike the majority of human enteroviruses, EV70 apparently does not replicate in the enteric tract but rather is primarily associated with an infection of the eye commonly referred to as acute hemorrhagic conjunctivitis (AHC) (for a review, see reference 49). Since the emergence of the virus in western Africa in 1969, it has been responsible for two pandemics and numerous smaller outbreaks and has been implicated in roughly 100 million cases of AHC; most recently, occurrences have been reported in India (24, 47), Japan (44), and Israel (38). In rare instances, a neurological illness that resembles acute poliomyelitis follows, usually within several weeks of the onset of the conjunctivitis (13), suggesting that the tissue tropism of EV70 also includes the central nervous system (CNS). It has also been observed that, whereas the majority of human enteroviruses are restricted in vitro to replication in cells of human or primate origin, EV70 replicates with various efficiencies in cells derived from a wide variety of mammalian species (50).The first step in a viral infection is the binding of the virus to a specific cell surface receptor. This step is often an important determinant of virus host range, tissue tropism, and pathogenesis (for a review see reference 34) and may contribute to the molecular basis for the unusual tissue tropism and host range of EV70. Previous work in our laboratory demonstrated that EV70 binds to the complement control protein decay-accelerating factor (D...

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Sialic Acid Functions in Enterovirus 70 Binding and Infection

Alexander

Dimock

2002

J Virol

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“…As described above for Afa/Dr DAEC, DAF is hijacked by coxsackieviruses and enteroviruses as part of their pathogenicity mechanisms. DAF is a major cell attachment receptor for coxsackieviruses B-1, -3, and -5 (3,30,32,277,380,383), but cell infection requires an association with the coxsackievirus and adenovirus receptor (CAR) (31, 75,76,332,381,382,384). Enterovirus 70 utilizes DAF as an attachment protein (221), recognizing CCP-1 as a binding site (184,220), but some enteroviruses that bind to DAF also bind to cells of human and murine origins in a DAF-independent manner, suggesting that they use a multiplicity of receptors to achieve infection of the host (153,154).…”

Section: Daf (Cd55)mentioning

confidence: 99%

Pathogenesis of Afa/Dr Diffusely AdheringEscherichia coli

2005

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Over the last few years, dramatic increases in our knowledge about diffusely adhering Escherichia coli (DAEC) pathogenesis have taken place. The typical class of DAEC includes E. coli strains harboring AfaE-I, AfaE-II, AfaE-III, AfaE-V, Dr, Dr-II, F1845, and NFA-I adhesins (Afa/Dr DAEC); these strains (i) have an identical genetic organization and (ii) allow binding to human decay-accelerating factor (DAF) (Afa/DrDAF subclass) or carcinoembryonic antigen (CEA) (Afa/DrCEA subclass). The atypical class of DAEC includes two subclasses of strains; the atypical subclass 1 includes E. coli strains that express AfaE-VII, AfaE-VIII, AAF-I, AAF-II, and AAF-III adhesins, which (i) have an identical genetic organization and (ii) do not bind to human DAF, and the atypical subclass 2 includes E. coli strains that harbor Afa/Dr adhesins or others adhesins promoting diffuse adhesion, together with pathogenicity islands such as the LEE pathogenicity island (DA-EPEC). In this review, the focus is on Afa/Dr DAEC strains that have been found to be associated with urinary tract infections and with enteric infection. The review aims to provide a broad overview and update of the virulence aspects of these intriguing pathogens. Epidemiological studies, diagnostic techniques, characteristic molecular features of Afa/Dr operons, and the respective role of Afa/Dr adhesins and invasins in pathogenesis are described. Following the recognition of membrane-bound receptors, including type IV collagen, DAF, CEACAM1, CEA, and CEACAM6, by Afa/Dr adhesins, activation of signal transduction pathways leads to structural and functional injuries at brush border and junctional domains and to proinflammatory responses in polarized intestinal cells. In addition, uropathogenic Afa/Dr DAEC strains, following recognition of β1 integrin as a receptor, enter epithelial cells by a zipper-like, raft- and microtubule-dependent mechanism. Finally, the presence of other, unknown virulence factors and the way that an Afa/Dr DAEC strain emerges from the human intestinal microbiota as a “silent pathogen” are discussed

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“…Integrin v 3 (Roivainen et al, 1991;Roivainen et al, 1994;Berinstein et al, 1995;Triantafilou et al, 1999); GRP78 (Triantafilou et al, 2002); MHC class I via 2 -microglobulin (Triantafilou et al, 1999) Coxsackievirus B1-6 CAR (Bergelson et al, 1997;Shafren et al, 1997c;Tomko et al, 1997;Martino et al, 2000;He et al, 2001); murine CAR (Tomko et al, 1997;Bergelson et al, 1998) Coxsackievirus B1, B3, B5 DAF Shafren et al, 1995;Martino et al, 1998); integrin v 6 (Agrez et al,…”

Section: Coxsackievirus A9mentioning

confidence: 99%

Evolution of Cell Recognition by Viruses: A Source of Biological Novelty with Medical Implications

Baranowski

Ruiz-Jarabo

Pariente

et al. 2003

Advances in Virus Research

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Receptor classCellular structure a Extracellular matrix components, sugar derivatives and lipids GalactosylceramideGangliosides Glycosaminoglycans (heparan and chondroitin sulfates) Phospholipids Sialic acid (N-acetylneuraminic acid, N-acetyl-9-O-acetylneuraminic acid and N-glycolylneuraminic acid 3-O-sulfated heparan sulfate Cell adhesion and cell-cell contact proteins -Dystroglycan Coxsackievirus-adenovirus receptor (CAR; Ig superfamily) CD4 (Ig superfamily) CEACAMs (including Bgp1a, Bgp2, and pregnancy-specific glycoprotein) Intercellular adhesion molecule type 1 (ICAM-1; Ig superfamily) Integrins Junction adhesion molecule (JAM) Laminin receptor (high affinity) MHC class I and 2 -microglobulin Neural cell adhesion molecule (NCAM) Signaling lymphocyte activation molecule

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Coxsackieviruses B1, B3, and B5 use decay accelerating factor as a receptor for cell attachment

Cited by 261 publications

References 32 publications

Sialic Acid Functions in Enterovirus 70 Binding and Infection

Sialic Acid Functions in Enterovirus 70 Binding and Infection

Pathogenesis of Afa/Dr Diffusely AdheringEscherichia coli

Evolution of Cell Recognition by Viruses: A Source of Biological Novelty with Medical Implications

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