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Peer-reviewedCC BY-NC 4.0Cell Reports Medicine

Potently neutralizing and protective human monoclonal antibodies against the measles fusion protein trimer

  • Laura S. Handal1,2
  • Elad Binshtein2
  • Nurgun Kose2
  • Naveenchandra Suryadevara2
  • Seth J. Zost2,3
  • Andrew Trivette2
  • Kah-Whye Peng4
  • Breandan Quinn4
  • Silvia Ravera2
  • Mark T. Menghini1,2
  • Chandrahaas Kona2
  • James Martinez2
5 more authors
  • Stacey A. Rutherford2
  • Jorge C.G. Blanco5
  • Marina S. Boukhvalova5
  • Miguel Á. Muñoz-Alía4,6
  • James E. Crowe1,2,3
6 affiliations
  1. 1Department of Pathology, Microbiology, and Immunology, Vanderbilt University Medical Center, Nashville, TN 37232, USA
  2. 2Vanderbilt Center for Antibody Therapeutics, Vanderbilt University Medical Center, Nashville, TN 37232, USA
  3. 3Department of Pediatrics, Vanderbilt University Medical Center, Nashville, TN 37232, USA
  4. 4Mayo Clinic, Rochester, MN 55901, USA
  5. 5Sigmovir Biosystems, Inc., Rockville, MD 20850, USA
  6. 6Vyriad, Inc., Rochester, MN 55901, USA
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Abstract

Measles remains a significant source of morbidity and mortality globally. There are currently no licensed treatments for patients at high risk of severe disease. There is limited knowledge about the human antibody response to a measles infection or vaccination or the structural determinants of antibody-mediated neutralization on the measles virus surface hemagglutinin (H) and fusion (F) glycoproteins. Here, we describe a panel of human monoclonal antibodies isolated from individuals who had been naturally infected with the measles virus. Several antibodies that recognized a prefusion-stabilized F protein potently neutralized the virus in vitro. We determined the structural basis of molecular recognition and virus neutralization using cryo-electron microscopy (cryo-EM) for two antibodies that recognize distinct sites of the F protein, MeV-15 and MeV-104. These antibodies also strongly inhibited viral replication in vivo when administered prophylactically in a murine transgenic model and when administered therapeutically in a cotton rat model of established infection.

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Cite

BibTeXRIS
BibTeX
@article{handal2026potently,
  title = {{Potently neutralizing and protective human monoclonal antibodies against the measles fusion protein trimer}},
  author = {Laura S. Handal and Elad Binshtein and Nurgun Kose and Naveenchandra Suryadevara and Seth J. Zost and Andrew Trivette and Kah-Whye Peng and Breandan Quinn and Silvia Ravera and Mark T. Menghini and Chandrahaas Kona and James Martinez and Stacey A. Rutherford and Jorge C.G. Blanco and Marina S. Boukhvalova and Miguel Á. Muñoz-Alía and James E. Crowe},
  journal = {Cell Reports Medicine},
  year = {2026},
  month = sep,
  doi = {10.1016/j.xcrm.2026.103081},
  url = {https://doi.org/10.1016/j.xcrm.2026.103081},
  note = {CC BY-NC 4.0},
}
RIS
TY  - JOUR
TI  - Potently neutralizing and protective human monoclonal antibodies against the measles fusion protein trimer
AU  - Laura S. Handal
AU  - Elad Binshtein
AU  - Nurgun Kose
AU  - Naveenchandra Suryadevara
AU  - Seth J. Zost
AU  - Andrew Trivette
AU  - Kah-Whye Peng
AU  - Breandan Quinn
AU  - Silvia Ravera
AU  - Mark T. Menghini
AU  - Chandrahaas Kona
AU  - James Martinez
AU  - Stacey A. Rutherford
AU  - Jorge C.G. Blanco
AU  - Marina S. Boukhvalova
AU  - Miguel Á. Muñoz-Alía
AU  - James E. Crowe
PY  - 2026
DA  - 2026/09/28
JO  - Cell Reports Medicine
DO  - 10.1016/j.xcrm.2026.103081
UR  - https://doi.org/10.1016/j.xcrm.2026.103081
AB  - Measles remains a significant source of morbidity and mortality globally. There are currently no licensed treatments for patients at high risk of severe disease. There is limited knowledge about the human antibody response to a measles infection or vaccination or the structural determinants of antibody-mediated neutralization on the measles virus surface hemagglutinin (H) and fusion (F) glycoproteins. Here, we describe a panel of human monoclonal antibodies isolated from individuals who had been naturally infected with the measles virus. Several antibodies that recognized a prefusion-stabilized F protein potently neutralized the virus in vitro. We determined the structural basis of molecular recognition and virus neutralization using cryo-electron microscopy (cryo-EM) for two antibodies that recognize distinct sites of the F protein, MeV-15 and MeV-104. These antibodies also strongly inhibited viral replication in vivo when administered prophylactically in a murine transgenic model and when administered therapeutically in a cotton rat model of established infection.
SN  - 2666-3791
ER  -