9Q1Z

Structure of the Measles virus Hemagglutinin ectodomain in complex with neutralizing antibody 1C02

Summary for 9Q1Z

• Entry DOI: 10.2210/pdb9q1z/pdb
• EMDB information: 72146
• Descriptor: 1C02 Fab Heavy chain, 1C02 Fab Light chain, Hemagglutinin glycoprotein, ... (6 entities in total)
• Functional Keywords: viral protein, glycoprotein, immune system, measles, high-resolution, ectodomain, attachment, antibody, complex, viral protein-immune system complex, viral protein/immune system
• Biological source: Homo sapiens; More
• Total number of polymer chains: 6
• Total formula weight: 244647.11

Authors

Zyla, D.,Acciani, M.,Niemeyer, G.,Saphire, E.O. (deposition date: 2025-08-14, release date: 2026-07-01)

Primary citation

Acciani, M.,Zyla, D.,Niemeyer, G.,Harkins, S.,Parekh, D.,Pawlack, E.,Lacarbonara, D.,Kansara, D.,Ackerman, M.E.,Niewiesk, S.,Porotto, M.,Hastie, K.M.,Saphire, E.O.
Human neutralizing antibodies targeting the measles virus hemagglutinin and fusion surface proteins.
Cell Host Microbe, 34:1067-1081.e12, 2026

PubMed 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 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.

PubMed: 42102820
DOI: 10.1016/j.chom.2026.04.010

Experimental method

ELECTRON MICROSCOPY (3.05 Å)