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Chapter 7 : Enterovirus Structure and Assembly

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Abstract:

This chapter describes the structures of enterovirus capsid proteins and virions and the process by which virions are assembled and the genome is encapsidated. Enterovirus capsid proteins are translated in the order VP4-VP2-VP3-VP1 as part of a large polyprotein and are separated by proteolytic cleavage. The four poliovirus capsid proteins and their precursors have been mapped onto the genome by alignment of its nucleotide sequence with partial amino acid sequences derived from the amino and carboxy termini of these polypeptides. The RNA genomes of poliovirus and other enteroviruses are translated into single large polyproteins that are subsequently proteolytically processed to yield diverse structural and nonstructural proteins. Proteolytic cleavage of enterovirus capsid proteins from the P1 precursor, assembly, and eventual maturation of the virion are regulated, sequential processes that appear to be intimately connected. Two models have been proposed for virion formation. The first involves encapsidation into procapsids and is supported by the reported association of procapsids with the viral replication complex and the conversion of procapsids into virions in pulse-chase experiments. The second model involves the association of pentamers or pentamer assemblies around virion RNA.

Citation: Hellen C, Wimmer E. 1995. Enterovirus Structure and Assembly, p 155-174. In Rotbart H (ed), Human Enterovirus Infections. ASM Press, Washington, DC. doi: 10.1128/9781555818326.ch7

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Figures

Image of FIGURE 1
FIGURE 1

Quaternary organization of poliovirus capsid proteins VP2, VP3, and VP1 within the protomer. The ribbon drawing represents the arrangement of the three β barrels within the virus quaternary structure. The heavy outline in the capsid model represents the biological protomer, which is not identical to the triangular asymmetric unit. The shading matches the β barrel units found in each trapezoid. Quasi-twofold, fivefold, and quasi-sixfold axes of symmetry are indicated by solid diamonds, pentagons, and triangles, respectively.

Citation: Hellen C, Wimmer E. 1995. Enterovirus Structure and Assembly, p 155-174. In Rotbart H (ed), Human Enterovirus Infections. ASM Press, Washington, DC. doi: 10.1128/9781555818326.ch7
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Image of FIGURE 2
FIGURE 2

Gene organization, processing scheme, and cleavage sites of the P1 poliovirus capsid protein precursor. Proteolytic cleavages occur between amino acid pairs, indicated by standard single-letter code. Arrows above and below the P1 partial polyprotein indicate sites that are cleaved in inter- and intramolecular reactions, respectively, by proteinases as indicated. The question mark indicates that the mechanism of cleavage at this site is not known.

Citation: Hellen C, Wimmer E. 1995. Enterovirus Structure and Assembly, p 155-174. In Rotbart H (ed), Human Enterovirus Infections. ASM Press, Washington, DC. doi: 10.1128/9781555818326.ch7
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Image of FIGURE 3
FIGURE 3

Enterovirus morphogenesis. (A) The P1 capsid protein precursor is released from the nascent polyprotein following autocatalytic cleavage by 2A at its own amino terminus and is then cleaved twice by 3CD. The cleaved termini of all three capsid proteins undergo considerable rearrangement after P1 cleavage, and cleavage is a prerequisite for assembly (B) of five 5S monomers into 14S pentamers. Twelve 14S pentamers either may associate directly with genomic RNA to form provirions, possibly by way of 55S half-shell intermediates (C and D), or may assemble to form empty capsids (E) into which genomic RNA is subsequently inserted (F). Maturation cleavage (G) of VPO to yield VP4 and VP2 results in conversion of 150S provirions into 160S virions.

Citation: Hellen C, Wimmer E. 1995. Enterovirus Structure and Assembly, p 155-174. In Rotbart H (ed), Human Enterovirus Infections. ASM Press, Washington, DC. doi: 10.1128/9781555818326.ch7
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Image of FIGURE 4
FIGURE 4

Structures of the three major capsid proteins of poliovirus. (a) Schematic representation of the wedgelike eight-stranded antiparallel β barrel protein fold shared by VP1, VP2, and VP3. Individual β strands are shown as arrows and labeled with letters. Flanking helices are shown as cylinders, (b to d) Ribbon diagrams of VP1 (b),VP2 (c), and VP3 (d). The numbers indicate amino acid residues; extensions at the amino and carboxy termini of VPl andVP3 have been truncated for clarity.

Citation: Hellen C, Wimmer E. 1995. Enterovirus Structure and Assembly, p 155-174. In Rotbart H (ed), Human Enterovirus Infections. ASM Press, Washington, DC. doi: 10.1128/9781555818326.ch7
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Tables

Generic image for table
TABLE 1

Physical properties of enterovirus virions

Citation: Hellen C, Wimmer E. 1995. Enterovirus Structure and Assembly, p 155-174. In Rotbart H (ed), Human Enterovirus Infections. ASM Press, Washington, DC. doi: 10.1128/9781555818326.ch7
Generic image for table
TABLE 2

Proteolytic cleavage sites within P1 structural protein precursor of enteroviruses

Citation: Hellen C, Wimmer E. 1995. Enterovirus Structure and Assembly, p 155-174. In Rotbart H (ed), Human Enterovirus Infections. ASM Press, Washington, DC. doi: 10.1128/9781555818326.ch7
Generic image for table
Table 3

Amino acid sequence similarity between capsid proteins of poliovirus type 1 (Mahoney) and other enteroviruses and rhinoviruses

Citation: Hellen C, Wimmer E. 1995. Enterovirus Structure and Assembly, p 155-174. In Rotbart H (ed), Human Enterovirus Infections. ASM Press, Washington, DC. doi: 10.1128/9781555818326.ch7

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