9q20

Structure of the Measles virus Hemagglutinin ectodomain in complex with neutralizing antibody 1C08

spinqualitylabelsall models 9q20, resolution 3.25Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9q20 is a 6 chain structure with sequence from Homo sapiens and Measles virus strain Ichinose-B95a. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.25Å Ligands: NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function HEMA_MEASC Attaches the virus to cell receptors and thereby initiating infection. Binding of H protein to the receptor induces a conformational change that allows the F protein to trigger virion/cell membranes fusion. May use human CD46 and/or SLAMF1 as receptors for viral entry into the cell. The high degree of interaction between H and MCP/CD46 results in down-regulation of the latter from the surface of infected cells, rendering them more sensitive to c3b-mediated complement lysis (By similarity). Publication Abstract from PubMed Measles virus (MeV), a highly transmissible paramyxovirus, can cause severe complications and death, particularly in infants and young children. How and where human antibodies target and neutralize MeV remain unclear. Here, we report a panel of human monoclonal antibodies (mAbs) specific for MeV hemagglutinin (H) and fusion (F) surface proteins, derived from the memory B cells of a Measles-Mumps-Rubella (MMR) vaccinee. We mapped four and five major epitope clusters on H and F, respectively, and structurally characterized representative mAbs from each epitope cluster. MAbs against both H and F offer broad, potent, picomolar-level neutralization and substantially reduce viral loads in vivo when delivered before or after viral exposure. High-resolution cryo-electron microscopy of mAb complexes with H and F reveal highly conserved contact sites of the most protective antibodies. Characterization of these fully human mAbs provides avenues for prophylactic or therapeutic intervention against re-emerging MeV. Human neutralizing antibodies targeting the measles virus hemagglutinin and fusion surface proteins.,Acciani M, Zyla D, Niemeyer G, Harkins S, Parekh D, Pawlack E, Lacarbonara D, Kansara D, Ackerman ME, Niewiesk S, Porotto M, Hastie KM, Saphire EO Cell Host Microbe. 2026 Jun 10;34(6):1067-1081.e12. doi: , 10.1016/j.chom.2026.04.010. Epub 2026 May 7. PMID:42102820 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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