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PDBsum entry 4l3b
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Contents |
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222 a.a.
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248 a.a.
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237 a.a.
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References listed in PDB file
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Key reference
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Title
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Uncoating of common cold virus is preceded by RNA switching as determined by X-Ray and cryo-Em analyses of the subviral a-Particle.
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Authors
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A.Pickl-Herk,
D.Luque,
L.Vives-Adrián,
J.Querol-Audí,
D.Garriga,
B.L.Trus,
N.Verdaguer,
D.Blaas,
J.R.Castón.
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Ref.
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Proc Natl Acad Sci U S A, 2013,
110,
20063-20068.
[DOI no: ]
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PubMed id
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Abstract
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During infection, viruses undergo conformational changes that lead to delivery
of their genome into host cytosol. In human rhinovirus A2, this conversion is
triggered by exposure to acid pH in the endosome. The first subviral
intermediate, the A-particle, is expanded and has lost the internal viral
protein 4 (VP4), but retains its RNA genome. The nucleic acid is subsequently
released, presumably through one of the large pores that open at the icosahedral
twofold axes, and is transferred along a conduit in the endosomal membrane; the
remaining empty capsids, termed B-particles, are shuttled to lysosomes for
degradation. Previous structural analyses revealed important differences between
the native protein shell and the empty capsid. Nonetheless, little is known of
A-particle architecture or conformation of the RNA core. Using 3D cryo-electron
microscopy and X-ray crystallography, we found notable changes in RNA-protein
contacts during conversion of native virus into the A-particle uncoating
intermediate. In the native virion, we confirmed interaction of nucleotide(s)
with Trp(38) of VP2 and identified additional contacts with the VP1 N terminus.
Study of A-particle structure showed that the VP2 contact is maintained, that
VP1 interactions are lost after exit of the VP1 N-terminal extension, and that
the RNA also interacts with residues of the VP3 N terminus at the fivefold axis.
These associations lead to formation of a well-ordered RNA layer beneath the
protein shell, suggesting that these interactions guide ordered RNA egress.
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