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Instruments / Technical Area	Publication Details	Published
	Hand-foot-and-mouth disease virus receptor KREMEN1 binds the canyon of Coxsackie Virus A10 Yuguang Zhao , Daming Zhou , Tao Ni , Dimple Karia , Abhay Kotecha , Xiangxi Wang , Zihe Rao , E. Yvonne Jones , Elizabeth E. Fry , Jingshan Ren , David I. Stuart Nature Communications 11 DOI: 10.1038/s41467-019-13936-2 Open Access Show Abstract ▼ Abstract: Coxsackievirus A10 (CV-A10) is responsible for an escalating number of severe infections in children, but no prophylactics or therapeutics are currently available. KREMEN1 (KRM1) is the entry receptor for the largest receptor-group of hand-foot-and-mouth disease causing viruses, which includes CV-A10. We report here structures of CV-A10 mature virus alone and in complex with KRM1 as well as of the CV-A10 A-particle. The receptor spans the viral canyon with a large footprint on the virus surface. The footprint has some overlap with that seen for the neonatal Fc receptor complexed with enterovirus E6 but is larger and distinct from that of another enterovirus receptor SCARB2. Reduced occupancy of a particle-stabilising pocket factor in the complexed virus and the presence of both unbound and expanded virus particles suggests receptor binding initiates a cascade of conformational changes that produces expanded particles primed for viral uncoating.	Jan 2020
Krios I-Titan Krios I at Diamond	Atomic structure of the Epstein-Barr virus portal Cristina Machon , Montserrat Fàbrega-ferrer , Daming Zhou , Ana Cuervo , José L. Carrascosa , David I. Stuart , Miquel Coll Nature Communications 10 DOI: 10.1038/s41467-019-11706-8 Diamond Proposal Number(s): [18360] Open Access Show Abstract ▼ Abstract: Herpesviridae is a vast family of enveloped DNA viruses that includes eight distinct human pathogens, responsible for diseases that range from almost asymptomatic to severe and life-threatening. Epstein-Barr virus infects B-cells and epithelial cells, causing infectious mononucleosis, as well as a number of cancers. Epstein-Barr infection cannot be cured since neither vaccine nor antiviral drug treatments are available. All herpesviruses contain a linear double-stranded DNA genome, enclosed within an icosahedral capsid. Viral portal protein plays a key role in the procapsid assembly and DNA packaging. The portal is the entrance and exit pore for the viral genome, making it an attractive pharmacological target for the development of new antivirals. Here we present the atomic structure of the portal protein of Epstein-Barr virus, solved by cryo-electron microscopy at 3.5 Å resolution. The detailed architecture of this protein suggests that it plays a functional role in DNA retention during packaging.	Aug 2019
	Unexpected mode of engagement between enterovirus 71 and its receptor SCARB2 Daming Zhou , Yuguang Zhao , Abhay Kotecha , Elizabeth E. Fry , James T. Kelly , Xiangxi Wang , Zihe Rao , David J. Rowlands , Jingshan Ren , David I. Stuart Nature Microbiology 25 DOI: 10.1038/s41564-018-0319-z Show Abstract ▼ Abstract: Enterovirus 71 (EV71) is a common cause of hand, foot and mouth disease—a disease endemic especially in the Asia-Pacific region1. Scavenger receptor class B member 2 (SCARB2) is the major receptor of EV71, as well as several other enteroviruses responsible for hand, foot and mouth disease, and plays a key role in cell entry2. The isolated structures of EV71 and SCARB2 are known3,4,5,6, but how they interact to initiate infection is not. Here, we report the EV71–SCARB2 complex structure determined at 3.4 Å resolution using cryo-electron microscopy. This reveals that SCARB2 binds EV71 on the southern rim of the canyon, rather than across the canyon, as predicted3,7,8. Helices 152–163 (α5) and 183–193 (α7) of SCARB2 and the viral protein 1 (VP1) GH and VP2 EF loops of EV71 dominate the interaction, suggesting an allosteric mechanism by which receptor binding might facilitate the low-pH uncoating of the virus in the endosome/lysosome. Remarkably, many residues within the binding footprint are not conserved across SCARB2-dependent enteroviruses; however, a conserved proline and glycine seem to be key residues. Thus, although the virus maintains antigenic variability even within the receptor-binding footprint, the identification of binding ‘hot spots’ may facilitate the design of receptor mimic therapeutics less likely to quickly generate resistance.	Dec 2018

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