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

Autor:	Stelfox AJ; Division of Structural Biology, Wellcome Centre for Human Genetics, University of Oxford , Oxford, United Kingdom.; European Molecular Biology Laboratory , Grenoble, France., Oguntuyo KY; Icahn School of Medicine at Mount Sinai , New York, New York, USA., Rissanen I; Division of Structural Biology, Wellcome Centre for Human Genetics, University of Oxford , Oxford, United Kingdom.; Institute of Biotechnology, Helsinki Institute of Life Science HiLIFE, University of Helsinki , Helsinki, Finland., Harlos K; Division of Structural Biology, Wellcome Centre for Human Genetics, University of Oxford , Oxford, United Kingdom., Rambo R; Diamond Light Source Ltd, Harwell Science & Innovation Campus , Oxford, United Kingdom., Lee B; Icahn School of Medicine at Mount Sinai , New York, New York, USA., Bowden TA; Division of Structural Biology, Wellcome Centre for Human Genetics, University of Oxford , Oxford, United Kingdom.
Jazyk:	angličtina
Zdroj:	MBio [mBio] 2023 Oct 31; Vol. 14 (5), pp. e0139123. Date of Electronic Publication: 2023 Sep 22.
DOI:	10.1128/mbio.01391-23
Abstrakt:	Importance: Genetically diverse paramyxoviruses are united in their presentation of a receptor-binding protein (RBP), which works in concert with the fusion protein to facilitate host-cell entry. The C-terminal head region of the paramyxoviral RBP, a primary determinant of host-cell tropism and inter-species transmission potential, forms structurally distinct classes dependent upon protein and glycan receptor specificity. Here, we reveal the architecture of the C-terminal head region of the RBPs from Nariva virus (NarV) and Mossman virus (MosV), two archetypal rodent-borne paramyxoviruses within the recently established genus Narmovirus , family Paramyxoviridae . Our analysis reveals that while narmoviruses retain the general architectural features associated with paramyxoviral RBPs, namely, a six-bladed β-propeller fold, they lack the structural motifs associated with known receptor-mediated host-cell entry pathways. This investigation indicates that the RBPs of narmoviruses exhibit pathobiological features that are distinct from those of other paramyxoviruses. Competing Interests: The authors declare no conflict of interest.
Databáze:	MEDLINE
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