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Publication Abstract from PubMed

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 beta-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.

Crystal structure and solution state of the C-terminal head region of the narmovirus receptor binding protein.,Stelfox AJ, Oguntuyo KY, Rissanen I, Harlos K, Rambo R, Lee B, Bowden TA mBio. 2023 Oct 31;14(5):e0139123. doi: 10.1128/mbio.01391-23. Epub 2023 Sep 22. PMID:37737607^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.