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Instruments / Technical Area	Publication Details	Published	Actions
I03-Macromolecular Crystallography	Structural basis for inhibition of Plasmodium vivax invasion by a broadly neutralizing vaccine-induced human antibody Thomas. A. Rawlinson , Natalie M. Barber , Franziska Mohring , Jee Sun Cho , Varakorn Kosaisavee , Samuel F. Gerard , Daniel G. W. Alanine , Geneviève M. Labbé , Sean C. Elias , Sarah E. Silk , Doris Quinkert , Jing Jin , Jennifer M. Marshall , Ruth O. Payne , Angela M. Minassian , Bruce Russell , Laurent Rénia , François H. Nosten , Robert W. Moon , Matthew K. Higgins , Simon J. Draper Nature Microbiology 6 DOI: 10.1038/s41564-019-0462-1 Diamond Proposal Number(s): [18069] Show Abstract ▼ Abstract: The most widespread form of malaria is caused by Plasmodium vivax. To replicate, this parasite must invade immature red blood cells through a process requiring interaction of the P. vivax Duffy binding protein (PvDBP) with its human receptor, the Duffy antigen receptor for chemokines. Naturally acquired antibodies that inhibit this interaction associate with clinical immunity, suggesting PvDBP as a leading candidate for inclusion in a vaccine to prevent malaria due to P. vivax. Here, we isolated a panel of monoclonal antibodies from human volunteers immunized in a clinical vaccine trial of PvDBP. We screened their ability to prevent PvDBP from binding to the Duffy antigen receptor for chemokines, and their capacity to block red blood cell invasion by a transgenic Plasmodium knowlesi parasite genetically modified to express PvDBP and to prevent reticulocyte invasion by multiple clinical isolates of P. vivax. This identified a broadly neutralizing human monoclonal antibody that inhibited invasion of all tested strains of P. vivax. Finally, we determined the structure of a complex of this antibody bound to PvDBP, indicating the molecular basis for inhibition. These findings will guide future vaccine design strategies and open up possibilities for testing the prophylactic use of such an antibody.	May 2019
I02-Macromolecular Crystallography	Structural basis for therapeutic inhibition of complement C5 Matthijs Jore , Steven Johnson , Devon Sheppard , Natalie Barber , Yang I Li , Miles A Nunn , Hans Elmlund , Susan Lea Nature Structural & Molecular Biology DOI: 10.1038/nsmb.3196 Diamond Proposal Number(s): [9306] Show Abstract ▼ Abstract: Activation of complement C5 generates the potent anaphylatoxin C5a and leads to pathogen lysis, inflammation and cell damage. The therapeutic potential of C5 inhibition has been demonstrated by eculizumab, one of the world's most expensive drugs. However, the mechanism of C5 activation by C5 convertases remains elusive, thus limiting development of therapeutics. Here we identify and characterize a new protein family of tick-derived C5 inhibitors. Structures of C5 in complex with the new inhibitors, the phase I and phase II inhibitor OmCI, or an eculizumab Fab reveal three distinct binding sites on C5 that all prevent activation of C5. The positions of the inhibitor-binding sites and the ability of all three C5–inhibitor complexes to competitively inhibit the C5 convertase conflict with earlier steric-inhibition models, thus suggesting that a priming event is needed for activation.	Mar 2016

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