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Akademický článek

Conformational transitions and allosteric modulation in a heteromeric glycine receptor

Autor: Eric Gibbs, Emily Klemm, David Seiferth, Arvind Kumar, Serban L. Ilca, Philip C. Biggin, Sudha Chakrapani

Publikováno v: Nature Communications, Vol 14, Iss 1, Pp 1-15 (2023)

Glycine receptors (GlyR) are a critical postsynaptic component of spinal neurons. Here, the auhtors present cryo-EM structures of a heteromeric GlyR in the presence of an antagonist, agonist and agonist with a positive allosteric modulator.

Externí odkaz: https://doaj.org/article/db781d0d4fdb4137a11e404a9029e982

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Akademický článek

Flavivirus maturation leads to the formation of an occupied lipid pocket in the surface glycoproteins

Autor: Max Renner, Wanwisa Dejnirattisai, Loïc Carrique, Itziar Serna Martin, Dimple Karia, Serban L. Ilca, Shu F. Ho, Abhay Kotecha, Jeremy R. Keown, Juthathip Mongkolsapaya, Gavin R. Screaton, Jonathan M. Grimes

Publikováno v: Nature Communications, Vol 12, Iss 1, Pp 1-9 (2021)

Here, the authors provide cryo-EM structures of mature and immature Spondweni virus, defining the furin recognition site at high resolution, and identifying a lipid that binds E upon capsid maturation and is also present in Zika and Dengue virions.

Externí odkaz: https://doaj.org/article/c1e60ed8086c474ea0ccecd7e38b5686

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Akademický článek

Assembly of complex viruses exemplified by a halophilic euryarchaeal virus

Autor: Luigi De Colibus, Elina Roine, Thomas S. Walter, Serban L. Ilca, Xiangxi Wang, Nan Wang, Alan M. Roseman, Dennis Bamford, Juha T. Huiskonen, David I. Stuart

Publikováno v: Nature Communications, Vol 10, Iss 1, Pp 1-9 (2019)

Here, the authors present the cryo-EM structure of the archaeal virus SH1 at 3.8 Å resolution and show how the major capsid proteins assemble into hetero-hexamers, providing insights into the assembly process of this and related PRD1-adeno lineage v

Externí odkaz: https://doaj.org/article/c49688e838814e378948c888e788bdd5

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Akademický článek

Rules of engagement between αvβ6 integrin and foot-and-mouth disease virus

Autor: Abhay Kotecha, Quan Wang, Xianchi Dong, Serban L. Ilca, Marina Ondiviela, Rao Zihe, Julian Seago, Bryan Charleston, Elizabeth E. Fry, Nicola G. A. Abrescia, Timothy A. Springer, Juha T. Huiskonen, David I. Stuart

Publikováno v: Nature Communications, Vol 8, Iss 1, Pp 1-8 (2017)

Foot-and-mouth disease virus binds αvβ6 integrin, via a conserved RGD motif in the flexible, exposed GH loop of capsid protein VP1, for cell entry. Here Kotechaet al.visualize this interaction with the VP1 GH loop extending away from the viral surf

Externí odkaz: https://doaj.org/article/7cc85a0a325f47d7981c002ee69ab865

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Akademický článek

Double-stranded RNA virus outer shell assembly by bona fide domain-swapping

Autor: Zhaoyang Sun, Kamel El Omari, Xiaoyu Sun, Serban L. Ilca, Abhay Kotecha, David I. Stuart, Minna M. Poranen, Juha T. Huiskonen

Publikováno v: Nature Communications, Vol 8, Iss 1, Pp 1-9 (2017)

Double-shelled bacteriophage φ6 is a well-studied model system used to understand assembly of dsRNA viruses. Here the authors report a near-atomic resolution cryo-EM structure of φ6 and propose a model for the structural transitions occurring in th

Externí odkaz: https://doaj.org/article/b16852baa490454d977d1b4fd2e495b0

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Akademický článek

Dual Role of a Viral Polymerase in Viral Genome Replication and Particle Self-Assembly

Autor: Xiaoyu Sun, Serban L. Ilca, Juha T. Huiskonen, Minna M. Poranen

Publikováno v: mBio, Vol 9, Iss 5 (2018)

ABSTRACT Double-stranded RNA (dsRNA) viruses package several RNA-dependent RNA polymerases (RdRp) together with their dsRNA genome into an icosahedral protein capsid known as the polymerase complex. This structure is highly conserved among dsRNA viru

Externí odkaz: https://doaj.org/article/3ef5ba89c76241b08573477c9dba8a72

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