Journal
SCIENCE
Volume 362, Issue 6414, Pages 598-+Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aaq0620
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Funding
- NIH [R56 AI117675, R56 AI127371]
- Janssen
- Defense Advanced Research Projects Agency, Department of Defense [64047-LS-DRP. 02]
- Theme-based Research Scheme, Research Grants Council of the Hong Kong [T11-705/14N]
- U.S. Department of Energy (DOE), Basic Energy Sciences, Office of Science [DE-AC02-06CH11357]
- National Cancer Institute [Y1-CO-1020]
- NIGMS [Y1-GM-1104, P41GM103393]
- U.S. DOE, Office of Science, Office of Basic Energy Sciences [DE-AC02-76SF00515]
- DOE Office of Biological and Environmental Research
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [R56AI117675, UM1AI100663, R56AI127371, T32AI007354] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [P41GM103393] Funding Source: NIH RePORTER
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Broadly neutralizing antibodies against highly variable pathogens have stimulated the design of vaccines and therapeutics. We report the use of diverse camelid single-domain antibodies to influenza virus hemagglutinin to generate multidomain antibodies with impressive breadth and potency. Multidomain antibody MD3606 protects mice against influenza A and B infection when administered intravenously or expressed locally from a recombinant adeno-associated virus vector. Crystal and single-particle electron microscopy structures of these antibodies with hemagglutinins from influenza A and B viruses reveal binding to highly conserved epitopes. Collectively, our findings demonstrate that multidomain antibodies targeting multiple epitopes exhibit enhanced virus cross-reactivity and potency. In combination with adeno-associated virus-mediated gene delivery, they may provide an effective strategy to prevent infection with influenza virus and other highly variable pathogens.
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