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Instruments / Technical Area	Publication Details	Published	Actions
B21-High Throughput SAXS I02-Macromolecular Crystallography I04-Macromolecular Crystallography	Crystal structure and solution state of the C-terminal head region of the narmovirus receptor binding protein Alice J. Stelfox , Kasopefoluwa Y. Oguntuyo , Ilona Rissanen , Karl Harlos , Robert Rambo , Benhur Lee , Thomas Bowden Mbio DOI: 10.1128/mbio.01391-23 Diamond Proposal Number(s): [10627, 14744] Open Access Show Abstract ▼ Abstract: Increased viral surveillance has led to the isolation and identification of numerous uncharacterized paramyxoviruses, rapidly expanding our understanding of paramyxoviral diversity beyond the bounds of known genera. Despite this diversity, a key feature that unites paramyxoviruses is the presence of a receptor-binding protein (RBP), which facilitates host-cell attachment and plays a fundamental role in determining host range. Here, we study the RBP presented on the surface of rodent-borne paramyxoviruses Mossman and Nariva (MosV and NarV, respectively), viruses that constitute founding members of the recently defined Narmovirus genus within the Paramyxoviridae family. Crystallographic analysis of the C-terminal head region of the dimeric MosV and NarV RBPs demonstrates that while these glycoproteins retain the canonical six-bladed β-propeller fold found in other paramyxoviral RBPs, they lack the structural motifs associated with established paramyxovirus host-cell receptor entry pathways. Consistent with MosV-RBP and NarV-RBP undergoing a distinct entry pathway from other characterized paramyxoviruses, structure-based phylogenetic analysis demonstrates that these six-bladed β-propeller head domains form a singular structural class that is distinct from other paramyxoviral RBPs. Additionally, using an integrated crystallographic and small-angle X-ray scattering analysis, we confirm that MosV-RBP and NarV-RBP form homodimeric arrangements that are distinct from those adopted by other paramyxovirus RBPs. Altogether, this investigation provides a molecular-level blueprint of the narmovirus RBP that broadens our understanding of the structural space and functional diversity available to paramyxovirus RBPs.	Sep 2023

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B21-High Throughput SAXS
I02-Macromolecular Crystallography
I04-Macromolecular Crystallography

Crystal structure and solution state of the C-terminal head region of the narmovirus receptor binding protein

Alice J. Stelfox , Kasopefoluwa Y. Oguntuyo , Ilona Rissanen , Karl Harlos , Robert Rambo , Benhur Lee , Thomas Bowden

Mbio

DOI: 10.1128/mbio.01391-23

Diamond Proposal Number(s): [10627, 14744]