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TitleNgR1 binding to reovirus reveals an unusual bivalent interaction and a new viral attachment protein.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 120, Issue 24, Page e2219404120, Year 2023
Publish dateJun 13, 2023
AuthorsDanica M Sutherland / Michael Strebl / Melanie Koehler / Olivia L Welsh / Xinzhe Yu / Liya Hu / Rita Dos Santos Natividade / Jonathan J Knowlton / Gwen M Taylor / Rodolfo A Moreno / Patrick Wörz / Zachery R Lonergan / Pavithra Aravamudhan / Camila Guzman-Cardozo / Sukhleen Kour / Udai Bhan Pandey / David Alsteens / Zhao Wang / B V Venkataram Prasad / Thilo Stehle / Terence S Dermody /
PubMed AbstractNogo-66 receptor 1 (NgR1) binds a variety of structurally dissimilar ligands in the adult central nervous system to inhibit axon extension. Disruption of ligand binding to NgR1 and subsequent ...Nogo-66 receptor 1 (NgR1) binds a variety of structurally dissimilar ligands in the adult central nervous system to inhibit axon extension. Disruption of ligand binding to NgR1 and subsequent signaling can improve neuron outgrowth, making NgR1 an important therapeutic target for diverse neurological conditions such as spinal crush injuries and Alzheimer's disease. Human NgR1 serves as a receptor for mammalian orthoreovirus (reovirus), but the mechanism of virus-receptor engagement is unknown. To elucidate how NgR1 mediates cell binding and entry of reovirus, we defined the affinity of interaction between virus and receptor, determined the structure of the virus-receptor complex, and identified residues in the receptor required for virus binding and infection. These studies revealed that central NgR1 surfaces form a bridge between two copies of viral capsid protein σ3, establishing that σ3 serves as a receptor ligand for reovirus. This unusual binding interface produces high-avidity interactions between virus and receptor to prime early entry steps. These studies refine models of reovirus cell-attachment and highlight the evolution of viruses to engage multiple receptors using distinct capsid components.
External linksProc Natl Acad Sci U S A / PubMed:37276413 / PubMed Central
MethodsEM (single particle)
Resolution7.2 - 8.9 Å
Structure data

EMDB-13149: Mammalian orthoreovirus T3SA- in complex with the neural receptor NgR1
Method: EM (single particle) / Resolution: 8.9 Å

EMDB-13150: Mammalian orthoreovirus T3SA-
Method: EM (single particle) / Resolution: 7.2 Å

Source
  • Mammalian orthoreovirus 3 Dearing
  • Homo sapiens (human)

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