Foot-and-Mouth Disease Virus-Receptor Interactions: Role in Pathogenesis and Tissue Culture Adaptation

Barry Baxt; Sherry Neff; Peter W. Mason; Elizabeth Rieder

doi:10.1128/9781555817916.ch11

Chapter 11 : Foot-and-Mouth Disease Virus-Receptor Interactions: Role in Pathogenesis and Tissue Culture Adaptation

Authors: Barry Baxt¹, Sherry Neff¹, Peter W. Mason¹, Elizabeth Rieder²

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Affiliations: 1: United States Department of Agriculture, Agricultural Research Service, Plum Island Animal Disease Center, Greenport, NY 11944-0848; 2: Department of Molecular Genetics and Microbiology, State University of New York at Stony Brook, Stony Brook, NY 11794-5222

Content Type: Monograph

Publication Year: 2002

Category: Viruses and Viral Pathogenesis

Book DOI: 10.1128/9781555817916

Chapter DOI: 10.1128/9781555817916.ch11

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Abstract:

This chapter examines the early events that occur upon infection of cultured cells with foot-and-mouth disease virus (FMDV) and defines the known virus-receptor interactions. In addition, the authors try to relate what is known about these early interactions to disease pathogenesis. The first identification of the integrin receptor for FMDV was made by comparing its receptor specificity with that of the human enterovirus, coxsackievirus A9 (CAV9), which contains a 17-amino-acid C-terminal insertion in VPl containing an arginineglycine- aspartic acid (RGD) sequence. Other important functional domains of integrins include the cytoplasmic domains of the α and β subunits. The authors examined the role of the cytoplasmic domains of the bovine integrin αv β3 in FMDV infection of cultured cells. While they have learned much about the early interactions of FMDV with its receptors in vitro, the role these receptors play in the pathogenesis of the disease is still unclear. Studies on the pathogenesis of FMD have shown that initial sites of viral replication are the lung and pharyngeal areas followed by rapid dissemination of the virus to the oral and pedal epithelia. Application of knowledge of the detailed mechanisms of FMDV-receptor interactions in vitro to the disease in the whole animal should provide insights into viral pathogenesis and may provide new information on how to control this important disease. Thus, future research should concentrate on determining which of the RGD-binding integrins found in susceptible hosts are capable of serving as receptors for FMDV.

Citation: Baxt B, Neff S, Mason P, Rieder E. 2002. Foot-and-Mouth Disease Virus-Receptor Interactions: Role in Pathogenesis and Tissue Culture Adaptation, p 115-123. In Semler B, Wimmer E (ed), Molecular Biology of Picornavirus. ASM Press, Washington, DC. doi: 10.1128/9781555817916.ch11

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Foot-and-Mouth Disease Virus-Receptor Interactions: Role in Pathogenesis and Tissue Culture Adaptation

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/content/10.1128/9781555817916.chap11.fig11-1

FIGURE 1

Competition binding of FMDV types A12 and O1BFS. Purified 3H-uridine-labeled FMDV types A12 (○) or O1BFS (■), at a concentration of 1 × 103 particles/cell, were mixed with increasing concentrations of either purified unlabeled (a) type A12 or (b) O1BFS and allowed to bind to BHK-21 cells for 90 min at room temperature. The level of binding was determined for labeled virus in the absence of unlabeled competitor, and the inhibition of binding of the labeled viruses by the unlabeled viruses is shown.

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FIGURE 1

References

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Tables

Foot-and-Mouth Disease Virus-Receptor Interactions: Role in Pathogenesis and Tissue Culture Adaptation

/content/10.1128/9781555817916.chap11.tab11-1

TABLE 1

Replication of FMDV in CHO cells with defined receptor specificity a

a Adapted from data in reference 74 .

b See text for descriptions of the viruses.

c Viral proteins detected in infected cells by radioimmunoprecipitation.

d No viral proteins detected in infected cells.

e Not determined.

10.1128/9781555817916/tab11-1_thmb.gif

10.1128/9781555817916/tab11-1.gif

TABLE 1

Replication of FMDV in CHO cells with defined receptor specificity a

a Adapted from data in reference 74 .

b See text for descriptions of the viruses.

c Viral proteins detected in infected cells by radioimmunoprecipitation.

d No viral proteins detected in infected cells.

e Not determined.