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Instruments / Technical Area	Publication Details	Published	Actions
I03-Macromolecular Crystallography I04-Macromolecular Crystallography	Contrasting modes of new world arenavirus neutralization by immunization-elicited monoclonal antibodies Weng M. Ng , Mehmet Sahin , Stefanie A. Krumm , Jeffrey Seow , Antra Zeltina , Karl Harlos , Guido C. Paesen , Daniel D. Pinschewer , Katie J. Doores , Thomas A. Bowden Mbio DOI: 10.1128/mbio.02650-21 Diamond Proposal Number(s): [14744, 19946] Open Access Show Abstract ▼ Abstract: Transmission of the New World hemorrhagic fever arenaviruses Junín virus (JUNV) and Machupo virus (MACV) to humans is facilitated, in part, by the interaction between the arenavirus GP1 glycoprotein and the human transferrin receptor 1 (hTfR1). We utilize a mouse model of live-attenuated immunization with envelope exchange viruses to isolate neutralizing monoclonal antibodies (NAbs) specific to JUNV GP1 and MACV GP1. Structures of two NAbs, termed JUN1 and MAC1, demonstrate that they neutralize through disruption of hTfR1 recognition. JUN1 utilizes a binding mode common to all characterized infection- and vaccine-elicited JUNV-specific NAbs, which involves mimicking hTfR1 binding through the insertion of a tyrosine into the receptor-binding site. In contrast, MAC1 undergoes a tyrosine-mediated mode of antigen recognition distinct from that used by the reported anti-JUNV NAbs and the only other characterized anti-MACV NAb. These data reveal the varied modes of GP1-specific recognition among New World arenaviruses by the antibody-mediated immune response.	Mar 2022
I03-Macromolecular Crystallography I04-Macromolecular Crystallography I23-Long wavelength MX	Structure-based classification defines the discrete conformational classes adopted by the arenaviral GP1 Rhys Pryce , Weng M. Ng , Antra Zeltina , Yasunori Watanabe , Kamel El Omari , Armin Wagner , Thomas A. Bowden Journal Of Virology DOI: 10.1128/JVI.01048-18 Diamond Proposal Number(s): [14744] Open Access Show Abstract ▼ Abstract: The emergence of Old and New World arenaviruses from rodent reservoirs persistently threatens human health. The GP1 subunit of the envelope-displayed arenaviral glycoprotein spike complex, GPC, mediates host-cell recognition and is an important determinant of cross-species transmission. Previous structural analyses of Old World arenaviral GP1 glycoproteins, alone and in complex with a cognate GP2 subunit, have revealed that GP1 adopts two distinct conformational states, distinguished by differences in orientation of helical regions of the molecule. Here, through comparative study of the GP1 glycoprotein architectures of Old World Loei River virus and New World Whitewater Arroyo virus, we show that these rearrangements are restricted to Old World arenaviruses and are not solely induced by the pH change that is associated with virus endosomal trafficking. Our structure-based phylogenetic analysis of arenaviral GP1s provides a blueprint for understanding the discrete structural classes adopted by these therapeutically important targets.	Oct 2018

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