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@article{1831250,
author = {Hrebík, Dominik and Füzik, Tibor and Gondová, Mária and Šmerdová, Lenka and Adamopoulos, Athanasios and Šedo, Ondrej and Zdráhal, Zbyněk and Plevka, Pavel},
article_number = {19},
doi = {http://dx.doi.org/10.1073/pnas.2024251118},
keywords = {virus; structure; receptor; cryo-electron microscopy; genome release},
language = {eng},
issn = {0027-8424},
journal = {Proceedings of the National Academy of Sciences of the United States of America},
title = {ICAM-1 induced rearrangements of capsid and genome prime rhinovirus 14 for activation and uncoating},
url = {https://www.pnas.org/content/118/19/e2024251118},
volume = {118},
year = {2021}
}
TY - JOUR
ID - 1831250
AU - Hrebík, Dominik - Füzik, Tibor - Gondová, Mária - Šmerdová, Lenka - Adamopoulos, Athanasios - Šedo, Ondrej - Zdráhal, Zbyněk - Plevka, Pavel
PY - 2021
TI - ICAM-1 induced rearrangements of capsid and genome prime rhinovirus 14 for activation and uncoating
JF - Proceedings of the National Academy of Sciences of the United States of America
VL - 118
IS - 19
SP - "e2024251118"
EP - "e2024251118"
PB - National Academy of Sciences
SN - 00278424
KW - virus
KW - structure
KW - receptor
KW - cryo-electron microscopy
KW - genome release
UR - https://www.pnas.org/content/118/19/e2024251118
N2 - 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 angstrom, respectively. The cryoelectron 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.
ER -
HREBÍK, Dominik, Tibor FÜZIK, Mária GONDOVÁ, Lenka ŠMERDOVÁ, Athanasios ADAMOPOULOS, Ondrej ŠEDO, Zbyněk ZDRÁHAL and Pavel PLEVKA. ICAM-1 induced rearrangements of capsid and genome prime rhinovirus 14 for activation and uncoating. \textit{Proceedings of the National Academy of Sciences of the United States of America}. National Academy of Sciences, 2021, vol.~118, No~19, p.~''e2024251118'', 10 pp. ISSN~0027-8424. Available from: https://dx.doi.org/10.1073/pnas.2024251118.
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