Chapter 7 : Poliovirus Receptors and Cell Entry

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Poliovirus is an ideal model for understanding how non-enveloped viruses enter cells and initiate infection. The study of entry of a wide variety of viruses reveals common themes that are the consequence of a central problem faced by all viruses in the passage from cell to cell or from host to host. The final stage of assembly for many viruses involves proteolytic processing of a virion protein. The replication cycle is initiated when poliovirus encounters the poliovirus receptor (Pvr), a transmembrane glycoprotein with three extracellular immunoglobulin (Ig)- like domains. Although there is still considerable controversy concerning the role of the two particles, the A particle may be an intermediate in the cell entry pathway, and the 80S empty particle may be the final protein product that accumulates after the RNA is released into the cytoplasm to initiate translation and replication. An attempt has been made to obtain structural “snapshots” of stable intermediates in the poliovirus cell entry pathway and to couple the structural information with the results of genetic, biophysical, and biochemical observations to fill in the gaps in the pathway. On the basis of structural, genetic, and biochemical evidence available to date, a working model for the cell entry of poliovirus, related enteroviruses, and major group rhinoviruses is proposed. An alternative model is proposed in which the transition from the initial binding complex to the tight-binding complex is characterized by movements of VP1, VP2, and VP3 that mimic the umbrella-like movements of the virion to A particle transition.

Citation: Hogle J, Racaniello V. 2002. Poliovirus Receptors and Cell Entry, p 71-83. In Semler B, Wimmer E (ed), Molecular Biology of Picornavirus. ASM Press, Washington, DC. doi: 10.1128/9781555817916.ch7

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Tomato bushy stunt virus
Cowpea chlorotic mottle virus
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Image of FIGURE 1

Structural features of poliovirus. (A) Electron micrograph of negatively stained poliovirus, magnification ×270.000. Courtesy of N. Cheng and D. M. Belnap, NIH. (B) Schematic of the poliovirus capsid, showing the arrangement of VP1, VP2, and VP3; VP4 is on the interior. The biological protomer (gray) is not the same as the icosahedral asymmetric subunit (triangle at right). (C) Diagram of the wedge-like structure formed by eight -strands of each capsid protein. Also shown are ribbon diagrams of poliovirus VP1, VP2, and VP3. Adapted from J. M. Hogle et al., 229:1358-1365, 1985, with permission. (D) Model of poliovirus type 1, based on X-ray crystallographic structure determined at 2.9 Å ( ). The model is highlighted by radial depth cuing so that portions of the model farthest from the center are bright. The fivefold axis of symmetry (5×) is characterized by a star-shaped mesa. Surrounding the fivefold axis is the canyon, which is the receptor-binding site. At the threefold axis is a propeller-shaped feature. (E) Model of poliovirus type 1 (20 Å), made by image reconstruction from cryo-electron microscopy data. The star-shaped mesa, canyon, and propeller are visible.

Citation: Hogle J, Racaniello V. 2002. Poliovirus Receptors and Cell Entry, p 71-83. In Semler B, Wimmer E (ed), Molecular Biology of Picornavirus. ASM Press, Washington, DC. doi: 10.1128/9781555817916.ch7
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Image of FIGURE 2

Interaction of poliovirus with its cellular receptor, Pvr. (A) Image reconstruction of poliovirus type 1 and a soluble form of Pvr ( ). Only domain 1 of Pvr binds in the canyon of the virus; there are 60 receptor-binding sites on the viral capsid. (B) Model of Pvr produced from homology modeling and the density map from cryo-electron microscopy data of the virus-receptor complex ( ). Ig-like domains are labeled. Carbohydrate side chains have been modeled on domains 1 and 2. (C) “Roadmap” view of poliovirus 1 (left) and rhinovirus 14 (right). The corresponding triangular area of the capsid surface, bounded by a fivefold and two threefold icosahedral symmetry axes, is shown. The radial distances of surface residues from the virion center are coded by different shades of gray. Receptor footprints (Pvr on poliovirus, ICAM-1 on rhinovirus 14) are white.

Citation: Hogle J, Racaniello V. 2002. Poliovirus Receptors and Cell Entry, p 71-83. In Semler B, Wimmer E (ed), Molecular Biology of Picornavirus. ASM Press, Washington, DC. doi: 10.1128/9781555817916.ch7
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Image of FIGURE 3

Models for poliovims entry into cells. (Top) Overview. The 160S native virion binds to the cell receptor, Pvr, and at temperatures greater than 33°C is converted to the A particle. The viral RNA (curved line) might exit the particle from the plasma membrane or from within vesicles, although clathrin-mediated endocytosis is not required for poliovirus entry. (Bottom) Hypothetical mechanism for translocation of poliovirus RNA across the cell membrane, (a) Cross section of the initial virus-receptor complex. The viral RNA is in the capsid, and lipid occupies the hydrophobic pocket, (b) Docking of the receptor in the canyon leads to loss of the lipid in the hydrophobic pocket, allowing the capsid to undergo conformational changes including the externalization of VP4 and the N terminus of VP1. (c) Five copies of the N terminus of VP1 insert into the membrane and form a channel by a mechanism that may be facilitated by myristoyl-VP4. (d) Later in the entry process VP1 moves away from the fivefold axis, the five amphipathic helices rotate, and the internal plug formed by the N termini of VP3 moves, resulting in the formation of a channel through which the viral RNA may pass.

Citation: Hogle J, Racaniello V. 2002. Poliovirus Receptors and Cell Entry, p 71-83. In Semler B, Wimmer E (ed), Molecular Biology of Picornavirus. ASM Press, Washington, DC. doi: 10.1128/9781555817916.ch7
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Image of FIGURE 4

Structures of poliovirus A (135S) and 80S particles. Stereo views of reconstructions of the 160S, 135S, and 80S particles ( ) are shown in the left panel. Pseudo-atomic models for each of the forms of the virus were derived by fitting the atomic model of the capsid proteins derived from X-ray crystallographic studies of the 160S particle ( ) to the low-resolution reconstruction density, treating each of the capsid proteins, VP1, VP2, and VP3, as rigid bodies. The models for the capsid proteins of one protomer for (A) the 160S particle, (B) the 135S particle, and (C) the 80S particles and their fit to the reconstruction densities are shown in the panel on the right. The fivefold axis (pentagons) and threefold axis (triangles) are indicated. In (D) the individual capsid proteins for the 160S particle (dark gray), 135S particle (light gray), and 80S particle (intermediate gray) are represented as simple stick models. Note that there is significant density in all three reconstructions that corresponds to the VP3 -tube plug at the fivefold axes (gray arrows).

Citation: Hogle J, Racaniello V. 2002. Poliovirus Receptors and Cell Entry, p 71-83. In Semler B, Wimmer E (ed), Molecular Biology of Picornavirus. ASM Press, Washington, DC. doi: 10.1128/9781555817916.ch7
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