Chapter 46 : Rhinovirus

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Human rhinoviruses (HRVs) constitute the largest genus in the family. In addition, rapid progress has been made in understanding the clinical characteristics and epidemiology of the rhinoviruses. Phylogenetic analysis of these sequences showed that 100 rhinovirus serotypes are divided into two genetic groups or species and that HRV87 is an enterovirus (enterovirus 68). The rhinovirus genome, like that of polio virus, is organized into three major regions based on proteolytic processing: P1, P2, and P3, representing genes for precursor proteins. An impressive feature of rhinovirus pathogenesis is that the nonspecific defense mechanisms of the nose are unable to prevent infection in the nonimmune individual and may, in fact, contribute to the pathogenesis of rhinovirus-associated illness. The major clinical syndrome associated with rhinovirus infection is rhinosinusitis, which is traditionally characterized as “the common cold”. Two clinical presentations of acute bacterial sinusitis can be recognized. First, the classical features of acute bacterial sinusitis include fever and facial pain, swelling, or tenderness. The current treatment of rhinovirus-associated illness relies on remedies directed at specific symptoms. The second and more common presentation of acute bacterial sinusitis is that of an acute respiratory illness which begins as a cold or ‘‘flu’’ but lasts longer than expected. Antiviral chemoprophylaxis for rhinovirus colds may have practical value, but no commercial product of proven efficacy is available. Alpha interferon applied topically in the nose is effective in reducing the incidence of colds in persons who are exposed to a family member with a fresh cold.

Citation: Turner R, Lee W. 2009. Rhinovirus, p 1063-1082. In Richman D, Whitley R, Hayden F (ed), Clinical Virology, Third Edition. ASM Press, Washington, DC. doi: 10.1128/9781555815981.ch46

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Image of FIGURE 1

Classification of human rhinovirus serotypes into two receptor groups. HRV87 has been reclassified as an enterovirus.

Citation: Turner R, Lee W. 2009. Rhinovirus, p 1063-1082. In Richman D, Whitley R, Hayden F (ed), Clinical Virology, Third Edition. ASM Press, Washington, DC. doi: 10.1128/9781555815981.ch46
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Image of FIGURE 2

(A) Schematic drawing of ICAM-1, the receptor used by the major group of rhinoviruses. S-S represents disulfide bridges, and small circles represent sites of glycosylation. (B) Key features of the structure of a human rhinovirus. The virion shell consists of 12 pentamers, 1 of which has been removed to show the approximate location of the RNA packed tightly into a central cavity. Each pentamer, in turn, consists of five wedge-shaped protomer subunits. The canyon (shaded) is shown encircling the fivefold axis of the pentamer; the hydrophobic (drug-binding) pocket is indicated below the floor of the canyon in VP1. (C) Side view of the pentamer showing the spatial relationship between the receptor-binding site and the hydrophobic pocket. An ion, located at each pentamer center in serotypes 1A, 14, and 16, is tentatively identified as calcium.

Citation: Turner R, Lee W. 2009. Rhinovirus, p 1063-1082. In Richman D, Whitley R, Hayden F (ed), Clinical Virology, Third Edition. ASM Press, Washington, DC. doi: 10.1128/9781555815981.ch46
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Image of FIGURE 3

(A) RNA genome of an HRV. P1, P2, and P3 are precursor proteins which are subsequently processed to produce 11 end products. (B) Cleavage of the polyprotein is accomplished by two viral proteases, 2A and 3C. The 2A protease cotranslationally releases the coat precursor, P1, from nascent polyprotein, whereas the 3C (or precursor 3CD) protease cleaves all the remaining precursors and intermediates except for VP0. Cleavage of VP0 to VP4 and VP2 (maturation cleavage) occurs only after the RNA has been packaged in the protein shell. The VP0 cleavage site lies buried inside the shell near the RNA; the active site for this cleavage is not yet precisely known and might include bases in the RNA genome. The amino termini of coat proteins P1 and 1A are blocked by a myristoyl group. cleavage of the N terminus of 2A is shown by an arrow; black triangles indicate 3C cleavage sites.

Citation: Turner R, Lee W. 2009. Rhinovirus, p 1063-1082. In Richman D, Whitley R, Hayden F (ed), Clinical Virology, Third Edition. ASM Press, Washington, DC. doi: 10.1128/9781555815981.ch46
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Image of FIGURE 4

(A) Diagram representing virion architecture and assembly. (B) The mature virion contains four major proteins (VP1, -2, -3, and -4) plus traces of VP0, representing residual precursor following the maturation cleavage required for acquisition of infectivity. SDS, sodium dodecyl sulfate.

Citation: Turner R, Lee W. 2009. Rhinovirus, p 1063-1082. In Richman D, Whitley R, Hayden F (ed), Clinical Virology, Third Edition. ASM Press, Washington, DC. doi: 10.1128/9781555815981.ch46
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Image of FIGURE 5

Overview of the rhinovirus infection cycle.

Citation: Turner R, Lee W. 2009. Rhinovirus, p 1063-1082. In Richman D, Whitley R, Hayden F (ed), Clinical Virology, Third Edition. ASM Press, Washington, DC. doi: 10.1128/9781555815981.ch46
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Image of FIGURE 6

Cytopathic effect of HRV16 on H1 HeLa cells (ATCC CRL 1958) and WI-38 human diploid embryonic lung cells (ATCC CCL75). Cells were exposed to 100 PFU per cell and incubated at 35°C. Cytopathic effect in HeLa cells was apparent by 12 h but required about 48 h in WI-38 cells.

Citation: Turner R, Lee W. 2009. Rhinovirus, p 1063-1082. In Richman D, Whitley R, Hayden F (ed), Clinical Virology, Third Edition. ASM Press, Washington, DC. doi: 10.1128/9781555815981.ch46
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Image of FIGURE 7

Proposed pathogenesis of symptoms associated with rhinovirus infection.

Citation: Turner R, Lee W. 2009. Rhinovirus, p 1063-1082. In Richman D, Whitley R, Hayden F (ed), Clinical Virology, Third Edition. ASM Press, Washington, DC. doi: 10.1128/9781555815981.ch46
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