5wb0

Crystal structure of human metapneumovirus fusion glycoprotein stabilized in the prefusion state

spinqualitylabelsall models 5wb0, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5wb0 is a 1 chain structure with sequence from Hmpv. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BMA, MAN, NAG, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Human metapneumovirus (hMPV) is a frequent cause of bronchiolitis in young children. Its F glycoprotein mediates virus-cell membrane fusion and is the primary target of neutralizing antibodies. The inability to produce recombinant hMPV F glycoprotein in the metastable pre-fusion conformation has hindered structural and immunological studies. Here, we engineer a pre-fusion-stabilized hMPV F ectodomain and determine its crystal structure to 2.6 A resolution. This structure reveals molecular determinants of strain-dependent acid-induced fusion, as well as insights into refolding from pre- to post-fusion conformations. A dense glycan shield at the apex of pre-fusion hMPV F suggests that antibodies against this site may not be elicited by host immune responses, which is confirmed by depletion studies of human immunoglobulins and by mouse immunizations. This is a major difference with pre-fusion F from human respiratory syncytial virus (hRSV), and collectively our results should facilitate development of effective hMPV vaccine candidates. Structure and immunogenicity of pre-fusion-stabilized human metapneumovirus F glycoprotein.,Battles MB, Mas V, Olmedillas E, Cano O, Vazquez M, Rodriguez L, Melero JA, McLellan JS Nat Commun. 2017 Nov 16;8(1):1528. doi: 10.1038/s41467-017-01708-9. PMID:29142300 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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