Cellular Receptors of Picornaviruses: an Overview

Elizabeth Rieder; Eckard Wimmer

doi:10.1128/9781555817916.ch6

Chapter 6 : Cellular Receptors of Picornaviruses: an Overview

Authors: Elizabeth Rieder¹, Eckard Wimmer¹

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Affiliations: 1: Department of Molecular Genetics and Microbiology, School of Medicine, State University of New York at Stony Brook, Stony Brook, NY 11794

Content Type: Monograph

Publication Year: 2002

Category: Viruses and Viral Pathogenesis

Book DOI: 10.1128/9781555817916

Chapter DOI: 10.1128/9781555817916.ch6

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Abstract:

The most surprising result of studies focused on early events in animal virus infection is the diversity of cell surface proteins serving as receptors. Two viruses belonging to two entirely different families, say, the small RNA coxsackievirus B and the large DNA adenovirus 2, have chosen the same small cell surface protein as receptor (CAR). Perhaps Retroviridae assembled the most diverse menu of cellular receptors. Most receptors belong to the immunoglobulin (Ig) superfamily or the integrin receptor family. Considering the many unresolved puzzles concerning enterovirus entry, and the steady expansion of picornavirus genera, the number of picornavirus receptors can increase significantly in the future. The cellular function of integrins includes binding extracellular matrix proteins, cell-cell interactions, and signal transduction. Decay accelerating factor (DAF) (CD55) is a member of the regulator of the complement activity protein family and protects the cell from autologous lysis. Heparan sulfate has been implicated in receptor function for certain strains of foot-and-mouth disease virus (FMDV) and clinical isolates of echovirus 6. The difference in receptor utilization not only yields host range phenotypes in vitro, but it has also a profound effect on pathogenesis in animals. The polypeptide chain of decay-accelerating factor (DAF) consists of four short consensus sequences (SCRs), some of which are involved in virus binding. Pathogenesis is determined by tissue tropism, spread of the virus to target tissues, and virulence.

Citation: Rieder E, Wimmer E. 2002. Cellular Receptors of Picornaviruses: an Overview, p 61-70. In Semler B, Wimmer E (ed), Molecular Biology of Picornavirus. ASM Press, Washington, DC. doi: 10.1128/9781555817916.ch6

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Foot-and-mouth disease virus: 0.4879586
Major Histocompatibility Complex: 0.46235743
Sodium Dodecyl Sulfate: 0.4515208
MHC Class I: 0.44067052

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Cellular Receptors of Picornaviruses: an Overview

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FIGURE 1

Classes of molecules chat serve as cell receptor for picornaviruses. The structure shown for the integrins family is a generic representation. Abbreviations: PVR, poliovirus receptor; CAR, coxsackievirus-adenovirus receptor; DAF, decay-accelerating factor; GPI, glycosylphosphatidylinositol; HAVCR-1, hepatitis A virus cellular receptor type 1; ICAM-1, intercellular adhesion molecule type 1; VCAM-1, vascular cell adhesion molecule type 1; VLDL-R, very-low-density lipoprotein receptor. Other molecules of the LDL receptor gene superfamily also serve as receptor for minor group human rhinoviruses (see chapter 9). Adapted from Wimmer ( 78 ). Numbers indicate domains implicated in virus binding.

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FIGURE 1

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Tables

Cellular Receptors of Picornaviruses: an Overview

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TABLE 1

Overview of disease syndromes and receptors a of six genera of Picornaviridae

a Receptors: the molecules listed are sufficient to dock a virion to the cell surface, but they are not necessarily competent to initiate an infectious cycle. Receptors in bold letters are likely to be essential and sufficient for infectivity. Abbreviations: α v β 3, α v β 6, α 2 β 1, integrins (α v β 3, α v β 6, vitronectin receptors; α 2 β 1 = VLA-2, a collagen and laminin receptor); DAF, decay-accelerating factor (CD55); CD155, poliovirus receptor (Pvr); ICAM-1, intercellular adhesion molecule 1; HCAR, human coxsackievirus B and adenovirus 2 receptor; VCAM, vascular cell adhesion molecule; HAVcr-1, receptor for hepatitis A virus; β 2-m, β 2-microglobulin, a component of MHC class I; MAP-70, a protein of the MHC class I; CD59, complement control protein. Italics denote a nonhuman pathogen; ND, not determined.

b Clusters of enteroviruses refer to groups of enteroviruses arranged predominantly according to genotypic kinship ( 33a ; chapter 2). Poliovirus was added to the C-cluster because of its close relationship to the Ocluster coxsackieviruses A. More clusters including mainly animal enteroviruses have been proposed.

c Receptors may be specific for specific serotypes. For details, see text.

d Accessory factors are defined here as proteins that enhance infectivity. In some cases, blocking an accessory factor by monoclonal antibodies may block infection. This, however, may be restricted to specific virus-cell pairing (e.g., infectivity of some echoviruses on RD cells, but not on HeLa cells, can be blocked with monoclonal antibodies to β 2:-m).

e Numbers in this column refer to references describing the identification of receptors.

f List of human syndromes adapted from reference 22a . Common syndromes in humans caused predominantly by one and/or other member(s) of the cluster, but member viruses of other clusters or even genera may cause the same syndrome.

g Rieder and Wimmer, unpublished data.

h Coxsackievirus A24v is a genetic variant of coxsackievirus A24.

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TABLE 1

Overview of disease syndromes and receptors a of six genera of Picornaviridae

c Receptors may be specific for specific serotypes. For details, see text.

e Numbers in this column refer to references describing the identification of receptors.

g Rieder and Wimmer, unpublished data.

h Coxsackievirus A24v is a genetic variant of coxsackievirus A24.

/content/10.1128/9781555817916.chap6.tab6-2

TABLE 2

Sites of attachment on virions and receptors

a V, V domain; C, C domain; * indicates N-terminal binding domain.

10.1128/9781555817916/tab6-2_thmb.gif

10.1128/9781555817916/tab6-2.gif

TABLE 2

Sites of attachment on virions and receptors

a V, V domain; C, C domain; * indicates N-terminal binding domain.