Cryo-EM of human rhinovirus reveals capsid-RNA duplex interactions that provide insights into virus assembly and genome uncoating

被引:3
作者
Gil-Cantero, David [1 ]
Mata, Carlos P. [2 ,7 ]
Valiente, Luis [3 ]
Rodriguez-Huete, Alicia [3 ]
Valbuena, Alejandro [3 ]
Twarock, Reidun [4 ,5 ]
Stockley, Peter G. [2 ]
Mateu, Mauricio G. [3 ]
Caston, Jose R. [1 ,6 ]
机构
[1] Ctr Nacl Biotecnol CNB CSIC, Dept Struct Macromol, Campus Cantoblanco, Madrid, Spain
[2] Univ Leeds, Fac Biol Sci, Astbury Ctr Struct Mol Biol, Leeds, England
[3] Univ Autonoma Madrid, Ctr Biol Mol Severo Ochoa CSIC UAM, Madrid, Spain
[4] Univ York, Dept Math, York, England
[5] Univ York, Dept Biol, York, England
[6] Nanobiotechnol Associated Unit CNB CSIC IMDEA, Campus Cantoblanco, Madrid, Spain
[7] Ctr Nacl Biotecnol CNB CSIC, Dept Struct Macromol, Biocomp Unit, Campus Cantoblanco, Madrid, Spain
基金
英国工程与自然科学研究理事会; 英国惠康基金;
关键词
COMMON COLD VIRUS; VALIDATION; MOLPROBITY; MICROSCOPY; RESOLUTION; MECHANISM; BINDING; ENTRY;
D O I
10.1038/s42003-024-07213-2
中图分类号
Q [生物科学];
学科分类号
07 ; 0710 ; 09 ;
摘要
The cryo-EM structure of the human rhinovirus B14 determined in this study reveals 13-bp RNA duplexes symmetrically bound to regions around each of the 30 two-fold axes in the icosahedral viral capsid. The RNA duplexes (similar to 12% of the ssRNA genome) define a quasi-dodecahedral cage that line a substantial part of the capsid interior surface. The RNA duplexes establish a complex network of non-covalent interactions with pockets in the capsid inner wall, including coulombic interactions with a cluster of basic amino acid residues that surround each RNA duplex. A direct comparison was made between the cryo-EM structure of RNA-filled virions and that of RNA-free (empty) capsids that resulted from genome release from a small fraction of viruses. The comparison reveals that some specific residues involved in capsid-duplex RNA interactions in the virion undergo remarkable conformational rearrangements upon RNA release from the capsid. RNA release is also associated with the asynchronous opening of channels at the 30 two-fold axes. The results provide further insights into the molecular mechanisms leading to assembly of rhinovirus particles and their genome uncoating during infection. They may also contribute to development of novel antiviral strategies aimed at interfering with viral capsid-genome interactions during the infectious cycle.
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页数:10
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