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Chapter 3 : Early Events in Infection: Receptor Binding and Cell Entry

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Early Events in Infection: Receptor Binding and Cell Entry, Page 1 of 2

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Abstract:

As knowledge of the early events in infection with enteroviruses is limited, this chapter focuses on studies with poliovirus but examines the emerging data on several other enteroviruses. The early events in virus infection, from virus binding to uncoating of the viral genome, are well characterized for a number of enveloped viruses. The poliovirus-receptor interaction is a particularly good model for studying virus entry because of the experimental manipulations that are possible given the known structure of the virus and our ability to mutagenize both the virus and its cellular receptor. Despite our increasing genetic and structural understanding of early events in poliovirus infection, many problems, such as the location of the uncoating event, remain unsolved. Perhaps imminent studies on the entry of echoviruses (ECVs) and coxsackieviruses, stimulated by the identification of their receptors, will provide clues. The roles of receptors in host range and pathogenesis have been extensively studied for poliovirus, but many questions, such as the basis of tissue tropism, remain. A study of the cell functions of virus receptors may provide information on their role in virus replication. It has been suggested that virus binding to cell receptors may lead to activation of cell events that lead to disease, and there is evidence that receptors may regulate virus-induced cytopathic effects. Studies of the interactions of cell receptors with their natural cell ligands may therefore provide clues about cell processes that are activated upon virus binding and govern the outcome of virus infections.

Citation: Racaniello V. 1995. Early Events in Infection: Receptor Binding and Cell Entry, p 73-93. In Rotbart H (ed), Human Enterovirus Infections. ASM Press, Washington, DC. doi: 10.1128/9781555818326.ch3

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Figures

Image of FIGURE 1
FIGURE 1

Locations of the VP 1 BC loop and mutations in the poliovirus capsid. The virion is shown schematically at left, with one protomer shaded gray. At right is an α-carbon tracing of VP1 and VP2 only. The BC loop is highlighted at the fivefold axis of symmetry. Sites of amino acid changes that confer the phenotype are shown as dots, and the amino acid residues are indicated. Sphingosine in the hydrocarbon-binding pocket is shown in dark gray.

Citation: Racaniello V. 1995. Early Events in Infection: Receptor Binding and Cell Entry, p 73-93. In Rotbart H (ed), Human Enterovirus Infections. ASM Press, Washington, DC. doi: 10.1128/9781555818326.ch3
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Image of FIGURE 2
FIGURE 2

Structural model of the first Ig-like domain of PVR. The structure was predicted as described in reference . The β strands are lettered, and locations of mutations that affect virus binding are given as amino acid numbers, which begin with the first methionine of PVR ( ). This predicted structure differs slightly from two other published versions ( ).

Citation: Racaniello V. 1995. Early Events in Infection: Receptor Binding and Cell Entry, p 73-93. In Rotbart H (ed), Human Enterovirus Infections. ASM Press, Washington, DC. doi: 10.1128/9781555818326.ch3
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Image of FIGURE 3
FIGURE 3

Model for poliovirus entry into cells. Binding of virus to cells is reversible when carried out at temperatures below 33°C; at higher temperatures, bound viruses are converted to A particles. These particles are found both outside and inside the cell and may be intermediates in the uncoating process. Uncoating may occur at the cell surface or from within endosomes.

Citation: Racaniello V. 1995. Early Events in Infection: Receptor Binding and Cell Entry, p 73-93. In Rotbart H (ed), Human Enterovirus Infections. ASM Press, Washington, DC. doi: 10.1128/9781555818326.ch3
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