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

Autor: David Gil-Cantero, Carlos P. Mata, Luis Valiente, Alicia Rodríguez-Huete, Alejandro Valbuena, Reidun Twarock, Peter G. Stockley, Mauricio G. Mateu, José R. Castón

Publikováno v: Communications Biology, Vol 7, Iss 1, Pp 1-10 (2024)

Abstract 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 (~12% of the ssRNA gen

Externí odkaz: https://doaj.org/article/947dff4d4c24426db0aa5d6dad9abe91

Structural basis for biologically relevant mechanical stiffening of a virus capsid by cavity-creating or spacefilling mutations

Autor: Pablo Guerra, Alejandro Valbuena, Jordi Querol-Audí, Cristina Silva, Milagros Castellanos, Alicia Rodríguez-Huete, Damià Garriga, Mauricio G. Mateu, Nuria Verdaguer

Publikováno v: Scientific Reports, Vol 7, Iss 1, Pp 1-13 (2017)

Abstract Recent studies reveal that the mechanical properties of virus particles may have been shaped by evolution to facilitate virus survival. Manipulation of the mechanical behavior of virus capsids is leading to a better understanding of viral in

Externí odkaz: https://doaj.org/article/c9d7f16ea8e4443481a989e5fc02d4df

Equilibrium Dynamics of a Biomolecular Complex Analyzed at Single-amino Acid Resolution by Cryo-electron Microscopy

Autor: Daniel Luque, Alvaro Ortega-Esteban, Alejandro Valbuena, Jose Luis Vilas, Alicia Rodríguez-Huete, Mauricio G. Mateu, José R. Castón

Publikováno v: Journal of Molecular Biology. 435:168024

The biological function of macromolecular complexes depends not only on large-scale transitions between conformations, but also on small-scale conformational fluctuations at equilibrium. This study shows that detailed information on the equilibrium d

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c9a4ee4ec990e6921aa3c12566f9c286
https://doi.org/10.1016/j.jmb.2023.168024

Negatively charged amino acids at the foot-and-mouth disease virus capsid reduce the virion-destabilizing effect of viral RNA at acidic pH

Autor: Elisa Torres, Miguel A. Martín-Acebes, Rodrigo Cañas-Arranz, Silvia López-Argüello, Alicia Rodríguez-Huete, María J. Bustos, Mauricio G. Mateu, Flavia Caridi, Francisco Sobrino

Publikováno v: Scientific Reports
Digital.CSIC. Repositorio Institucional del CSIC
instname
Biblos-e Archivo. Repositorio Institucional de la UAM
Scientific Reports, Vol 10, Iss 1, Pp 1-8 (2020)
Biblos-e Archivo: Repositorio Institucional de la UAM
Universidad Autónoma de Madrid

Elucidation of the molecular basis of the stability of foot-and-mouth disease virus (FMDV) particles is relevant to understand key aspects of the virus cycle. Residue N17D in VP1, located at the capsid inner surface, modulates the resistance of FMDV

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3df5f8a29f46185941a92b4881dbb1a0
http://europepmc.org/articles/PMC6997383

Rationally designed interfacial peptides are efficient in vitro inhibitors of HIV-1 capsid assembly with antiviral activity.

Autor: Rebeca Bocanegra, María Nevot, Rosa Doménech, Inmaculada López, Olga Abián, Alicia Rodríguez-Huete, Claudio N Cavasotto, Adrián Velázquez-Campoy, Javier Gómez, Miguel Ángel Martínez, José Luis Neira, Mauricio G Mateu

Publikováno v: PLoS ONE, Vol 6, Iss 9, p e23877 (2011)

Virus capsid assembly constitutes an attractive target for the development of antiviral therapies; a few experimental inhibitors of this process for HIV-1 and other viruses have been identified by screening compounds or by selection from chemical lib

Externí odkaz: https://doaj.org/article/f05692aa4e6b4c5689ff07931322ec5e