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 Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Neumann, E. Articles by Hewat, E. A. Search for Related Content PubMed PubMed Citation Articles by Neumann, E. Articles by Hewat, E. A.

A Cellular Receptor of Human Rhinovirus Type 2, the Very-Low-Density Lipoprotein Receptor, Binds to Two Neighboring Proteins of the Viral Capsid

Emmanuelle Neumann,^1, Rosita Moser,² Luc Snyers,^2, Dieter Blaas,² and Elizabeth A. Hewat^1*

Institut de Biologie Structurale Jean-Pierre Ebel, 38027 Grenoble, France,¹ Institute of Medical Biochemistry, University of Vienna, Vienna Biocenter, A-1030 Vienna, Austria²

Received 3 March 2003/ Accepted 13 May 2003

The very-low-density lipoprotein receptor (VLDL-R) is a receptor for the minor-group human rhinoviruses (HRVs). Only two of the eight binding repeats of the VLDL-R bind to HRV2, and their footprints describe an annulus on the dome at each fivefold axis. By studying the complex formed between a selection of soluble fragments of the VLDL-R and HRV2, we demonstrate that it is the second and third repeats that bind. We also show that artificial concatemers of the same repeat can bind to HRV2 with the same footprint as that for the native receptor. In a 16-Å-resolution cryoelectron microscopy map of HRV2 in complex with the VLDL-R, the individual repeats are defined. The third repeat is strongly bound to charged and polar residues of the HI and BC loops of viral protein 1 (VP1), while the second repeat is more weakly bound to the neighboring VP1. The footprint of the strongly bound third repeat extends down the north side of the canyon. Since the receptor molecule can bind to two adjacent copies of VP1, we suggest that the bound receptor "staples" the VP1s together and must be detached before release of the RNA can occur. When the receptor is bound to neighboring sites on HRV2, steric hindrance prevents binding of the second repeat.

Present address: Wellcome Trust Centre, Division of Structural Biology, University of Oxford, Oxford OX3 7BN, United Kingdom.

Present address: Institute of Histology and Embryology, University of Vienna, A-1090 Vienna, Austria.

This article has been cited by other articles:

• Hafenstein, S., Bowman, V. D., Chipman, P. R., Kelly, C. M. B., Lin, F., Medof, M. E., Rossmann, M. G. (2007). Interaction of Decay-Accelerating Factor with Coxsackievirus B3. J. Virol. 81: 12927-12935 [Abstract] [Full Text]  
• Hewat, E. A., Blaas, D. (2006). Nonneutralizing Human Rhinovirus Serotype 2-Specific Monoclonal Antibody 2G2 Attaches to the Region That Undergoes the Most Dramatic Changes upon Release of the Viral RNA. J. Virol. 80: 12398-12401 [Abstract] [Full Text]  
• Laine, P., Blomqvist, S., Savolainen, C., Andries, K., Hovi, T. (2006). Alignment of capsid protein VP1 sequences of all human rhinovirus prototype strains: conserved motifs and functional domains. J. Gen. Virol. 87: 129-138 [Abstract] [Full Text]  
• Nizet, S., Wruss, J., Landstetter, N., Snyers, L., Blaas, D. (2005). A Mutation in the First Ligand-Binding Repeat of the Human Very-Low-Density Lipoprotein Receptor Results in High-Affinity Binding of the Single V1 Module to Human Rhinovirus 2. J. Virol. 79: 14730-14736 [Abstract] [Full Text]  
• Herdy, B., Snyers, L., Reithmayer, M., Hinterdorfer, P., Blaas, D. (2004). Identification of the Human Rhinovirus Serotype 1A Binding Site on the Murine Low-Density Lipoprotein Receptor by Using Human-Mouse Receptor Chimeras. J. Virol. 78: 6766-6774 [Abstract] [Full Text]  
• Kienberger, F., Zhu, R., Moser, R., Blaas, D., Hinterdorfer, P. (2004). Monitoring RNA Release from Human Rhinovirus by Dynamic Force Microscopy. J. Virol. 78: 3203-3209 [Abstract] [Full Text]