Key result
Cryo-electron microscopy revealed that human rhinovirus 2 A particles bind to liposome membranes around a 2-fold icosahedral symmetry axis.
This study reveals the structural mechanism by which human rhinovirus 2 A particles bind to lipid membranes during infection.
No clinical implications yet; leaves open targeted antiviral research on rhinovirus entry.
Minor group human rhinoviruses bind low-density lipoprotein (LDL) receptors for endocytosis. Once they are inside endosomes, the acidic pH triggers their dissociation from the receptors and conversion into hydrophobic subviral A particles; these attach to the membrane and transfer their single-strand, positive-sense RNA genome into the cytosol. Here, we allowed human rhinovirus 2 (HRV2) A particles, produced in vitro by incubation at pH 5.4, to attach to liposomes; cryo-electron microscopy 3-dimensional single-particle image reconstruction revealed that they bind to the membrane around a 2-fold icosahedral symmetry axis.
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Kumar et al. (2013) studied Human rhinovirus infection (in vitro model). Human rhinovirus 2 (HRV2) A particles was evaluated on Binding to liposome membranes. Cryo-electron microscopy revealed that human rhinovirus 2 A particles bind to liposome membranes around a 2-fold icosahedral symmetry axis.
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