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Instruments / Technical Area	Publication Details	Published	Actions
Krios II-Titan Krios II at Diamond Krios IV-Titan Krios IV at Diamond	Assessing the mobility of severe acute respiratory syndrome coronavirus-2 spike protein glycans by structural and computational methods Soledad Stagnoli , Francesca Peccati , Sean R. Connell , Ane Martinez-Castillo , Diego Charro , Oscar Millet , Chiara Bruzzone , Asis Palazon , Ana Ardá , Jesús Jiménez-Barbero , June Ereño-Orbea , Nicola G. A. Abrescia , Gonzalo Jiménez-Osés Frontiers In Microbiology 13 DOI: 10.3389/fmicb.2022.870938 Diamond Proposal Number(s): [23872] Open Access Show Abstract ▼ Abstract: Two years after its emergence, the coronavirus disease-2019 (COVID-19) pandemic caused by severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) remains difficult to control despite the availability of several vaccines. The extensively glycosylated SARS-CoV-2 spike (S) protein, which mediates host cell entry by binding to the angiotensin converting enzyme 2 (ACE2) through its receptor binding domain (RBD), is the major target of neutralizing antibodies. Like to many other viral fusion proteins, the SARS-CoV-2 spike protein utilizes a glycan shield to thwart the host immune response. To grasp the influence of chemical signatures on carbohydrate mobility and reconcile the cryo-EM density of specific glycans we combined our cryo-EM map of the S ectodomain to 4.1 Å resolution, reconstructed from a limited number of particles, and all-atom molecular dynamics simulations. Chemical modifications modeled on representative glycans (defucosylation, sialylation and addition of terminal LacNAc units) show no significant influence on either protein shielding or glycan flexibility. By estimating at selected sites the local correlation between the full density map and atomic model-based maps derived from molecular dynamics simulations, we provide insight into the geometries of the α-Man-(1→3)-[α-Man-(1→6)-]-β-Man-(1→4)-β-GlcNAc(1→4)-β-GlcNAc core common to all N-glycosylation sites.	Apr 2022
I24-Microfocus Macromolecular Crystallography	Bacteriophage PRD1 as a nanoscaffold for drug loading Helen M. E. Duyvesteyn , Isaac Santos-Perez , Francesca Peccati , Ane Martinez-Castillo , Thomas S. Walter , David Reguera , Felix M. Goñi , Gonzalo Jiménez-Osés , Hanna M. Oksanen , David I. Stuart , Nicola G. A. Abrescia Nanoscale 156 DOI: 10.1039/D1NR04153C Diamond Proposal Number(s): [14744] Open Access Show Abstract ▼ Abstract: Viruses are very attractive biomaterials owing to their capability as nanocarriers of genetic material. Efforts have been made to functionalize self-assembling viral protein capsids on their exterior or interior to selectively take up different payloads. PRD1 is a double-stranded DNA bacteriophage comprising an icosahedral protein outer capsid and an inner lipidic vesicle. Here, we report the three-dimensional structure of PRD1 in complex with the antipsychotic drug chlorpromazine (CPZ) by cryo-electron microscopy. We show that the jellyrolls of the viral major capsid protein P3, protruding outwards from the capsid shell, serve as scaffolds for loading heterocyclic CPZ molecules. Additional X-ray studies and molecular dynamics simulations show the binding modes and organization of CPZ molecules when complexed with P3 only and onto the virion surface. Collectively, we provide a proof of concept for the possible use of the lattice-like organisation and the quasi-symmetric morphology of virus capsomers for loading heterocyclic drugs with defined properties.	Dec 2021

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