The cellular receptor to human rhinovirus 2 binds around the 5-fold axis and not in the canyon: a structural view

Hewat, E.A.

doi:10.1093/emboj/19.23.6317

Cited by 131 publications

(118 citation statements)

References 60 publications

Supporting

Mentioning

115

Contrasting

Order By: Relevance

“…In this virion, this depression is filled with a loop of the N-terminal extension of VP1 [residues [44][45][46][47][48][49][50][51][52][53][54][55][56], which is covered on the inner surface by residues from the C terminus of VP4 (Figure 6c). Interactions of this loop of VP1 with the inner surface of VP2 and VP3 would be expected to contribute significantly to the stability of the capsid.…”

Section: How Does Vp0 Cleavage Trap the Virus In A Metastable State?mentioning

confidence: 99%

Poliovirus Cell Entry: Common Structural Themes in Viral Cell Entry Pathways

Hogle

2002

Annu. Rev. Microbiol.

310

305

View full text Add to dashboard Cite

Structural studies of polio-and closely related viruses have provided a series of snapshots along their cell entry pathways. Based on the structures and related kinetic, biochemical, and genetic studies, we have proposed a model for the cell entry pathway for polio-and closely related viruses. In this model a maturation cleavage of a capsid protein precursor locks the virus in a metastable state, and the receptor acts like a transition-state catalyst to overcome an energy barrier and release the mature virion from the metastable state. This initiates a series of conformational changes that allow the virus to attach to membranes, form a pore, and finally release its RNA genome into the cytoplasm. This model has striking parallels with emerging models for the maturation and cell entry of more complex enveloped viruses such as influenza virus and HIV.

show abstract

Section: How Does Vp0 Cleavage Trap the Virus In A Metastable State?mentioning

confidence: 99%

Poliovirus Cell Entry: Common Structural Themes in Viral Cell Entry Pathways

Hogle

2002

Annu. Rev. Microbiol.

310

305

View full text Add to dashboard Cite

show abstract

“…The minor receptor group rhinoviruses, for example, bind the very low density lipoprotein receptor (12). This interaction does not lead to the irreversible conformational changes outlined above, and recent studies demonstrate that this receptor binds to the virion around the 5-fold symmetry axes, not in the canyon (13). The lack of virus uncoating upon receptor binding suggests the existence of another, as yet unknown receptor or co-factor that induces uncoating.…”

mentioning

confidence: 99%

“…Similarly, receptor binding to hyper-variable epitopes has been demonstrated for the minor group rhinoviruses and foot and mouth disease virus. In these viruses a strategy is employed whereby conserved receptor binding domains are embedded in hyper-variable regions capable of mutation to escape the host immune response (13,31). In the EV7-receptor complex, bound DAF is located close to and lies across the 2-fold symmetry axes such that symmetry-related molecules are in steric collision (30).…”

mentioning

confidence: 99%

The Structure of Echovirus Type 12 Bound to a Two-domain Fragment of Its Cellular Attachment Protein Decay-accelerating Factor (CD 55)

Bhella

Goodfellow

Roversi

et al. 2004

Journal of Biological Chemistry

View full text Add to dashboard Cite

Echovirus type 12 (EV12), an Enterovirus of the Picornaviridae family, uses the complement regulator decayaccelerating factor (DAF, CD55) as a cellular receptor. We have calculated a three-dimensional reconstruction of EV12 bound to a fragment of DAF consisting of short consensus repeat domains 3 and 4 from cryo-negative stain electron microscopy data (EMD code 1057). This shows that, as for an earlier reconstruction of the related echovirus type 7 bound to DAF, attachment is not within the viral canyon but occurs close to the 2-fold symmetry axes. Despite this general similarity our reconstruction reveals a receptor interaction that is quite different from that observed for EV7. Fitting of the crystallographic co-ordinates for DAF 34 and EV11 into the reconstruction shows a close agreement between the crystal structure of the receptor fragment and the density for the virus-bound receptor, allowing unambiguous positioning of the receptor with respect to the virion (PDB code 1UPN). Our finding that the mode of virusreceptor interaction in EV12 is distinct from that seen for EV7 raises interesting questions regarding the evolution and biological significance of the DAF binding phenotype in these viruses.

show abstract

“…Receptor binding occurs at a surface exposed structure near the 5-fold axis, distinct from the canyons used by major HRV for binding to ICAM-1 [20]. HRV-2 reaches late endosomes and undergoes antigenic conversion at pH 5.4 [21,22].…”

Section: Chemical Cuesmentioning

confidence: 99%

Uncoating of non-enveloped viruses

Suomalainen¹,

Greber²

2013

Current Opinion in Virology

104

View full text Add to dashboard Cite

Non-enveloped viruses enclose their genome in capsids built of repetitive polypeptides interlinked with cementing proteins, divalent cations or disulphides. Interactions are broken in a stepwise manner during entry into cells leading to genome uncoating. Receptor or proteases induce conformational changes in case of rhinovirus, poliovirus or adenovirus, and thereby provide direct uncoating cues. Chemical cues from low endosomal pH activate rhinovirus or aphtovirus, and oxido-reductases mediate disulphide reshuffling of polyomavirus. Cellular motors provide a third class of cues as shown by adenoviruses. These examples highlight the diversity of cellular factors triggering virus uncoating, and offer new perspectives for the development of antivirals.

show abstract

The cellular receptor to human rhinovirus 2 binds around the 5-fold axis and not in the canyon: a structural view

Cited by 131 publications

References 60 publications

Poliovirus Cell Entry: Common Structural Themes in Viral Cell Entry Pathways

Poliovirus Cell Entry: Common Structural Themes in Viral Cell Entry Pathways

The Structure of Echovirus Type 12 Bound to a Two-domain Fragment of Its Cellular Attachment Protein Decay-accelerating Factor (CD 55)

Uncoating of non-enveloped viruses

Contact Info

Product

Resources

About