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Chapter 4 : Antibody Interactions with Rhinovirus

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Abstract:

This chapter discusses the possible mechanisms of antibody-mediated neutralization of human rhinovirus to better understand how antibodies recognize their targets and neutralize viral infectivity. Understanding these fundamental processes is crucial for future vaccine development and new antibody therapeutics. This is especially true for viruses like the human immunodeficiency virus (HIV), where the more traditional approach of using attenuated viral strains appears to be risky and insufficiently efficacious. The rhinoviruses, of which there are more than 100 serotypes, are major causative agents of the common cold in humans. The major difference in human rhinovirus 14 (HRV14) preparation between two crystals is the polyethylene glycol (PEG) 400 that was added as a cryoprotectant. This strongly suggests that the pocket factor found in the HRV14-Fab complex came from PEG 400. Since there has been no direct evidence that pocket factors are derived from the host cell, these results further suggest that pocket factors found in the other viruses might also be compounds used in purification or crystallization. For poliovirus and rhinovirus, interactions with their receptors appear to be essential for the proper release of the genomic RNA into the cytoplasm of the host cell. When antibody-poliovirus complexes enter cells, the viral RNA is quickly digested. Vaccine design strategies might, therefore, benefit by focusing on the production of high-affinity antibodies rather than on a particular in vitro neutralization property.

Citation: Smith T. 2002. Antibody Interactions with Rhinovirus, p 39-49. In Semler B, Wimmer E (ed), Molecular Biology of Picornavirus. ASM Press, Washington, DC. doi: 10.1128/9781555817916.ch4

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FIGURE 1

Aggregation and neutralization profiles for several ΝΙm-IΑ antibodies. Panel A shows the neutralization profile of mAb17 and mAb12 at increasing concentrations of antibody. Panel Β shows the amount of virus that is aggregated and pelleted upon addition of antibody. Neither of these strongly neutralizing antibodies precipitates the virions. The aggregation and neutralization profiles of other NIm-IA antibodies are shown in panels C to E. Reprinted from the ( ) with permission from publisher.

Citation: Smith T. 2002. Antibody Interactions with Rhinovirus, p 39-49. In Semler B, Wimmer E (ed), Molecular Biology of Picornavirus. ASM Press, Washington, DC. doi: 10.1128/9781555817916.ch4
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Tables

Generic image for table
Table 1

Residual infectivity (% of residual plaques) of HRV14 wild-type and mutant viruses after treatment with NIm-IA antibodies

Citation: Smith T. 2002. Antibody Interactions with Rhinovirus, p 39-49. In Semler B, Wimmer E (ed), Molecular Biology of Picornavirus. ASM Press, Washington, DC. doi: 10.1128/9781555817916.ch4
Generic image for table
Table 2

Fab17-HRV14 contacts

Citation: Smith T. 2002. Antibody Interactions with Rhinovirus, p 39-49. In Semler B, Wimmer E (ed), Molecular Biology of Picornavirus. ASM Press, Washington, DC. doi: 10.1128/9781555817916.ch4

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