This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Hewat, E. A. Articles by Blaas, D. Search for Related Content PubMed PubMed Citation Articles by Hewat, E. A. Articles by Blaas, D.

 Previous Article  |  Next Article 

Journal of Virology, March 2004, p. 2935-2942, Vol. 78, No. 6
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.6.2935-2942.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Cryoelectron Microscopy Analysis of the Structural Changes Associated with Human Rhinovirus Type 14 Uncoating

Institut de Biologie Structurale Jean-Pierre Ebel, 38027 Grenoble, France,¹ Max F. Perutz Laboratories, University Departments at the Vienna Biocenter, Department of Medical Biochemistry, University of Vienna, A-1030 Vienna, Austria²

Received 19 August 2003/ Accepted 12 November 2003

Release of the human rhinovirus (HRV) genome into the cytoplasm of the cell involves a concerted structural modification of the viral capsid. The intracellular adhesion molecule 1 (ICAM-1) cellular receptor of the major-group HRVs and the low-density lipoprotein (LDL) receptor of the minor-group HRVs have different nonoverlapping binding sites. While ICAM-1 binding catalyzes uncoating, LDL receptor binding does not. Uncoating of minor-group HRVs is initiated by the low pH of late endosomes. We have studied the conformational changes concomitant with uncoating in the major-group HRV14 and compared them with previous results for the minor-group HRV2. The structure of empty HRV14 was determined by cryoelectron microscopy, and the atomic structure of native HRV14 was used to examine the conformational changes of the capsid and its constituent viral proteins. For both HRV2 and HRV14, the transformation from full to empty capsid involves an overall 4% expansion and an iris type of movement of viral protein VP1 to open up a 10-Å-diameter channel on the fivefold axis to allow exit of the RNA genome. The ß-cylinders formed by the N termini of the VP3 molecules inside the capsid on the fivefold axis all open up in HRV2, but we propose that only one opens up in HRV14. The release of VP4 is less efficient in HRV14 than in HRV2, and the N termini of VP1 may exit at different points. The N-terminal loop of VP2 is modified in both viruses, probably to detach the RNA, but it bends only inwards in HRV2.

This article has been cited by other articles:

• Davis, M. P., Bottley, G., Beales, L. P., Killington, R. A., Rowlands, D. J., Tuthill, T. J. (2008). Recombinant VP4 of Human Rhinovirus Induces Permeability in Model Membranes. J. Virol. 82: 4169-4174 [Abstract] [Full Text]  
• Berryman, S., Clark, S., Monaghan, P., Jackson, T. (2005). Early Events in Integrin {alpha}v{beta}6-Mediated Cell Entry of Foot-and-Mouth Disease Virus. J. Virol. 79: 8519-8534 [Abstract] [Full Text]  
• Bubeck, D., Filman, D. J., Cheng, N., Steven, A. C., Hogle, J. M., Belnap, D. M. (2005). The Structure of the Poliovirus 135S Cell Entry Intermediate at 10-Angstrom Resolution Reveals the Location of an Externalized Polypeptide That Binds to Membranes. J. Virol. 79: 7745-7755 [Abstract] [Full Text]  
• Wang, L., Smith, D. L. (2005). Capsid structure and dynamics of a human rhinovirus probed by hydrogen exchange mass spectrometry. Protein Sci. 14: 1661-1672 [Abstract] [Full Text]  
• Li, Y., Zhou, Z., Post, C. B. (2005). From the Cover: Dissociation of an antiviral compound from the internal pocket of human rhinovirus 14 capsid. Proc. Natl. Acad. Sci. USA 102: 7529-7534 [Abstract] [Full Text]  
• Bleker, S., Sonntag, F., Kleinschmidt, J. A. (2005). Mutational Analysis of Narrow Pores at the Fivefold Symmetry Axes of Adeno-Associated Virus Type 2 Capsids Reveals a Dual Role in Genome Packaging and Activation of Phospholipase A2 Activity. J. Virol. 79: 2528-2540 [Abstract] [Full Text]