National Institutes of Health/National Institute of Neurological Disorders and Stroke (NIH/NINDS)
NS105699
United States
National Institutes of Health/National Institute of Neurological Disorders and Stroke (NIH/NINDS)
NS091263
United States
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)
AI176833
United States
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)
1R56AI183536-01A1
United States
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)
5R21AI180456-02
United States
Citation
Journal: Cell Host Microbe / Year: 2026 Title: Human neutralizing antibodies targeting the measles virus hemagglutinin and fusion surface proteins. Authors: Marissa Acciani / Dawid Zyla / Gele Niemeyer / Stephanie Harkins / Diptiben Parekh / Emily Pawlack / Davide Lacarbonara / Dhvanir Kansara / Margaret E Ackerman / Stefan Niewiesk / Matteo ...Authors: Marissa Acciani / Dawid Zyla / Gele Niemeyer / Stephanie Harkins / Diptiben Parekh / Emily Pawlack / Davide Lacarbonara / Dhvanir Kansara / Margaret E Ackerman / Stefan Niewiesk / Matteo Porotto / Kathryn M Hastie / Erica Ollmann Saphire / Abstract: 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 ...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.
Supramolecule #1: Structure of the Measles virus Fusion glycoprotein ectodomain in ...
Supramolecule
Name: Structure of the Measles virus Fusion glycoprotein ectodomain in complex with two neutralizing antibodies 4F09 and 3A12 type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#4
Model: Quantifoil R2/2 / Material: COPPER / Mesh: 200 / Support film - Material: GRAPHENE OXIDE / Support film - topology: CONTINUOUS / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 15 sec. / Pretreatment - Atmosphere: AIR
Vitrification
Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 298 K / Instrument: FEI VITROBOT MARK IV
-
Electron microscopy
Microscope
TFS KRIOS
Specialist optics
Energy filter - Name: GIF Bioquantum / Energy filter - Slit width: 20 eV
Software
Name: EPU
Image recording
Film or detector model: GATAN K3 (6k x 4k) / Digitization - Dimensions - Width: 5760 pixel / Digitization - Dimensions - Height: 4092 pixel / Number grids imaged: 3 / Number real images: 18982 / Average exposure time: 2.0 sec. / Average electron dose: 70.0 e/Å2
Electron beam
Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
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