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Instruments / Technical Area	Publication Details	Published	Actions
I02-Macromolecular Crystallography	Characterization of a potent and highly unusual minimally enhancing antibody directed against dengue virus Max Renner , Aleksandra Flanagan , Wanwisa Dejnirattisai , Chunya Puttikhunt , Watchara Kasinrerk , Piyada Supasa , Wiyada Wongwiwat , Kriangkrai Chawansuntati , Thaneeya Duangchinda , Alison Cowper , Claire M. Midgley , Prida Malasit , Juha T. Huiskonen , Juthathip Mongkolsapaya , Gavin R. Screaton , Jonathan M. Grimes Nature Immunology 496 DOI: 10.1038/s41590-018-0227-7 Diamond Proposal Number(s): [8423] Show Abstract ▼ Abstract: Dengue virus is a major pathogen, and severe infections can lead to life-threatening dengue hemorrhagic fever. Dengue virus exists as four serotypes, and dengue hemorrhagic fever is often associated with secondary heterologous infections. Antibody-dependent enhancement (ADE) may drive higher viral loads in these secondary infections and is purported to result from antibodies that recognize dengue virus but fail to fully neutralize it. Here we characterize two antibodies, 2C8 and 3H5, that bind to the envelope protein. Antibody 3H5 is highly unusual as it not only is potently neutralizing but also promotes little if any ADE, whereas antibody 2C8 has strong capacity to promote ADE. We show that 3H5 shows resilient binding in endosomal pH conditions and neutralizes at low occupancy. Immunocomplexes of 3H5 and dengue virus do not efficiently interact with Fcγ receptors, which we propose is due to the binding mode of 3H5 and constitutes the primary mechanism of how ADE is avoided.	Oct 2018
I03-Macromolecular Crystallography I24-Microfocus Macromolecular Crystallography	Diversity of oligomerization in Drosophila semaphorins suggests a mechanism of functional fine-tuning Daniel Rozbesky , Ross A. Robinson , Vitul Jain , Max Renner , Tomas Malinauskas , Karl Harlos , Christian Siebold , E. Yvonne Jones Nature Communications 10 DOI: 10.1038/s41467-019-11683-y Diamond Proposal Number(s): [14744, 10627] Open Access Show Abstract ▼ Abstract: Semaphorin ligands and their plexin receptors are one of the major cell guidance factors that trigger localised changes in the cytoskeleton. Binding of semaphorin homodimer to plexin brings two plexins in close proximity which is a prerequisite for plexin signalling. This model appears to be too simplistic to explain the complexity and functional versatility of these molecules. Here, we determine crystal structures for all members of Drosophila class 1 and 2 semaphorins. Unlike previously reported semaphorin structures, Sema1a, Sema2a and Sema2b show stabilisation of sema domain dimer formation via a disulfide bond. Unexpectedly, our structural and biophysical data show Sema1b is a monomer suggesting that semaphorin function may not be restricted to dimers. We demonstrate that semaphorins can form heterodimers with members of the same semaphorin class. This heterodimerization provides a potential mechanism for cross-talk between different plexins and co-receptors to allow fine-tuning of cell signalling.	Aug 2019

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