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Document proteins. It is typically a signal moiety that directs the protein to which it is attached towards cellular membranes [26]. Page 494 Above the β cylinder is an ion, thought to be Ca 2+, which lies right on the five-fold axis and coordinates to the five adjacent VP1 polypeptides [25,27]. The proximity of the β cylinder to structures shown later to become external during uncoating (portions of VP1, VP4) suggests that it may be important in uncoating. III. The Human Rhinovirus Life Cycle The HRVs must undergo a number of transitions to replicate (Figure 3). First, they must attach to the cell surface at a cellular receptor. They are then internalized into the cell via the endosomal compartment. Following internalization, they must eject their RNA out of the viral capsid, through a lipid bilayer, and into the cytosol in a manner that preserves the integrity of the RNA. Replication Figure 3 A schematic diagram depicting some of the required steps in viral replication. http://legacy.netlibrary.com/nlreader/nlReader.dll?bookid=12640&filename=Page_494.html (1 of 2) [4/9/2004 12:34:39 AM]
Document Page 495 of the RNA and production of a polyprotein ensues. The polyprotein is then processed by viral proteases to form the viral polypeptides. The coat must then assemble, package RNA, and leave the cell. The capsid-binding compounds' effect on propagation have been shown to occur at the attachment, uncoating, and assembly steps (25,27–30). The relative effect on each of these steps appears to be variable and has not yet been extensively characterized. The most universal effect appears to be on the uncoating step. During uncoating several different rhinovirus subparticles are observed. These are thought to be intermediates in the uncoating process [32–33]. The fully infectious 149S particle becomes an 125S Aparticle, which has lost VP4 but still maintains viral RNA. This A-particle is no longer infectious. The Aparticle then releases RNA to become an 80S empty shell. The formation of these types of particles can be induced by association of the virion with the cell receptor or acidification [32,34]. In poliovirus, attachment to cells has been shown to lead to a particle that has lost VP4 and has externalized the N-terminal region of VP1, which normally resides on the virion interior. There has been considerable debate about how the HRVs accomplish the transfer of RNA from inside the virion into the cell cytosol. This step is crucial for productive uncoating. An important question concerns the requirement for acidification of the endosome for HRVs to release their RNA. Evidence that appeared to conflict was found in a number of studies using either entero- or rhinoviruses (35–39). This question was later addressed by experiments that specifically separated entero- and rhinovirus behavior [40]. These experiments showed that HRVs, unlike poliovirus, require a pH-lowering step for productive infection. This pH lowering is likely to occur in the endosomal compartment. It should be noted that HRV and enteroviruses have been classified historically based on their resistance to acid: HRVs are acid-labile, while enteroviruses are stable in acid. Consequently, differences in behavior between the rhino- and enteroviruses in an acidic environment within the cell are not surprising. To replicate the changes in HRV that might be induced by acidification in the endosome, HRV14 was acidified in the crystalline state and examined via x-ray diffraction. When compared to the native HRV14, the acidified HRV14 capsid becomes disordered in three regions: the Ca 2+ ion on the five-fold axis; a region of the β cylinder and the adjacent portion of VP4; and the GH loop [41]. The GH loop is the region of structure that connects β-strands G and H and lies directly between the hydrophobic pocket and the receptor binding site (Figure 4). It forms the roof of the VP1 hydrophobic pocket and the floor of the canyon at the receptor binding site. Mutants that are resistant to acid in vitro were isolated [41,42]. These mutants cluster about the GH loop (Table 1, Figure 4), and typically would be thought of as mutants that stabilize protein structure (e.g., larger or more http://legacy.netlibrary.com/nlreader/nlReader.dll?bookid=12640&filename=Page_495.html [4/9/2004 12:34:53 AM]
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