Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	ICAM-1 induced rearrangements of capsid and genome prime rhinovirus 14 for activation and uncoating.
Journal, issue, pages	Proc Natl Acad Sci U S A, Vol. 118, Issue 19, Year 2021
Publish date	May 11, 2021
Authors	Dominik Hrebík / Tibor Füzik / Mária Gondová / Lenka Šmerdová / Athanassios Adamopoulos / Ondrej Šedo / Zbyněk Zdráhal / Pavel Plevka /
PubMed Abstract	Most rhinoviruses, which are the leading cause of the common cold, utilize intercellular adhesion molecule-1 (ICAM-1) as a receptor to infect cells. To release their genomes, rhinoviruses convert to ...Most rhinoviruses, which are the leading cause of the common cold, utilize intercellular adhesion molecule-1 (ICAM-1) as a receptor to infect cells. To release their genomes, rhinoviruses convert to activated particles that contain pores in the capsid, lack minor capsid protein VP4, and have an altered genome organization. The binding of rhinoviruses to ICAM-1 promotes virus activation; however, the molecular details of the process remain unknown. Here, we present the structures of virion of rhinovirus 14 and its complex with ICAM-1 determined to resolutions of 2.6 and 2.4 Å, respectively. The cryo-electron microscopy reconstruction of rhinovirus 14 virions contains the resolved density of octanucleotide segments from the RNA genome that interact with VP2 subunits. We show that the binding of ICAM-1 to rhinovirus 14 is required to prime the virus for activation and genome release at acidic pH. Formation of the rhinovirus 14-ICAM-1 complex induces conformational changes to the rhinovirus 14 capsid, including translocation of the C termini of VP4 subunits, which become poised for release through pores that open in the capsids of activated particles. VP4 subunits with altered conformation block the RNA-VP2 interactions and expose patches of positively charged residues. The conformational changes to the capsid induce the redistribution of the virus genome by altering the capsid-RNA interactions. The restructuring of the rhinovirus 14 capsid and genome prepares the virions for conversion to activated particles. The high-resolution structure of rhinovirus 14 in complex with ICAM-1 explains how the binding of uncoating receptors enables enterovirus genome release.
External links	Proc Natl Acad Sci U S A / PubMed:33947819 / PubMed Central
Methods	EM (single particle)
Resolution	2.4 - 22.0 Å
Structure data	12171 7bg6 EMDB-12171: HRV14 native particle PDB-7bg6: HRV14 native particle solved by cryoEM Method: EM (single particle) / Resolution: 2.6 Å 12172 7bg7 EMDB-12172, PDB-7bg7: HRV14 in complex with its receptor ICAM-1 Method: EM (single particle) / Resolution: 2.4 Å 12594 7nul EMDB-12594, PDB-7nul: Rhinovirus-14 ICAM-1 activated particle at pH 6.2 Method: EM (single particle) / Resolution: 4.0 Å 12595 7num EMDB-12595, PDB-7num: Rhinovirus-14 ICAM-1 empty particle at pH 6.2 Method: EM (single particle) / Resolution: 3.9 Å 12596 7nun EMDB-12596, PDB-7nun: Rhinovirus 14 ICAM-1 virion-like particle at pH 6.2 Method: EM (single particle) / Resolution: 3.6 Å 12597 7nuo EMDB-12597, PDB-7nuo: Rhinovirus 14 empty particle at pH 6.2 Method: EM (single particle) / Resolution: 3.9 Å EMDB-12598: RV14 ICAM-1 pH 6.2 open particle Method: EM (single particle) / Resolution: 22.0 Å 12599 7nuq EMDB-12599, PDB-7nuq: Rhinovirus 14 virion-like at pH 6.2 Method: EM (single particle) / Resolution: 2.8 Å
Chemicals	ChemComp-HOH: WATER / Water
Source	rhinovirus b14 HRV-14 (virus) human rhinovirus 14 homo sapiens (human)
Keywords	VIRUS / enterovirus / rhinovirus 14 / HRV14 / RV14 / native particle / receptor / virus-receptor complex / ICAM-1 / acidification / pH 6.2 / genome release / A particle / activated / emptu / empty particle