Structural characterization of a protective epitope spanning A(H1N1)pdm09 influenza virus neuraminidase monomers
Abstract
A(H1N1)pdm09 influenza A viruses predominated in the 2013–2014 USA influenza season, and although most of these viruses remain sensitive to Food and Drug Administration-approved neuraminidase (NA) inhibitors, alternative therapies are needed. Here we show that monoclonal antibody CD6, selected for binding to the NA of the prototypic A(H1N1)pdm09 virus, A/California/07/2009, protects mice against lethal virus challenge. The crystal structure of NA in complex with CD6 Fab reveals a unique epitope, where the heavy-chain complementarity determining regions (HCDRs) 1 and 2 bind one NA monomer, the light-chain CDR2 binds the neighbouring monomer, whereas HCDR3 interacts with both monomers. This 30-amino-acid epitope spans the lateral face of an NA dimer and is conserved among circulating A(H1N1)pdm09 viruses. These results suggest that the large, lateral CD6 epitope may be an effective target of antibodies selected for development as therapeutic agents against circulating H1N1 influenza viruses.
- Authors:
-
- Food and Drug Administration, Silver Springs, MD (United States)
- Centers for Disease Control and Prevention, Atlanta, GA (United States)
- Publication Date:
- Research Org.:
- Argonne National Laboratory (ANL), Argonne, IL (United States)
- Sponsoring Org.:
- USDOE Office of Science (SC), Basic Energy Sciences (BES); Food and Drug Administration and the Centers for Disease Control and Prevention
- OSTI Identifier:
- 1245874
- Grant/Contract Number:
- AC02-06CH11357
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Nature Communications
- Additional Journal Information:
- Journal Volume: 6; Journal Issue: 1; Journal ID: ISSN 2041-1723
- Publisher:
- Nature Publishing Group
- Country of Publication:
- United States
- Language:
- ENGLISH
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; Drug development; Influenza virus; Molecularly targeted therapy
Citation Formats
Wan, Hongquan, Yang, Hua, Shore, David A., Garten, Rebecca J., Couzens, Laura, Gao, Jin, Jiang, Lianlian, Carney, Paul J., Villanueva, Julie, Stevens, James, and Eichelberger, Maryna C. Structural characterization of a protective epitope spanning A(H1N1)pdm09 influenza virus neuraminidase monomers. United States: N. p., 2015.
Web. doi:10.1038/ncomms7114.
Wan, Hongquan, Yang, Hua, Shore, David A., Garten, Rebecca J., Couzens, Laura, Gao, Jin, Jiang, Lianlian, Carney, Paul J., Villanueva, Julie, Stevens, James, & Eichelberger, Maryna C. Structural characterization of a protective epitope spanning A(H1N1)pdm09 influenza virus neuraminidase monomers. United States. https://doi.org/10.1038/ncomms7114
Wan, Hongquan, Yang, Hua, Shore, David A., Garten, Rebecca J., Couzens, Laura, Gao, Jin, Jiang, Lianlian, Carney, Paul J., Villanueva, Julie, Stevens, James, and Eichelberger, Maryna C. Tue .
"Structural characterization of a protective epitope spanning A(H1N1)pdm09 influenza virus neuraminidase monomers". United States. https://doi.org/10.1038/ncomms7114. https://www.osti.gov/servlets/purl/1245874.
@article{osti_1245874,
title = {Structural characterization of a protective epitope spanning A(H1N1)pdm09 influenza virus neuraminidase monomers},
author = {Wan, Hongquan and Yang, Hua and Shore, David A. and Garten, Rebecca J. and Couzens, Laura and Gao, Jin and Jiang, Lianlian and Carney, Paul J. and Villanueva, Julie and Stevens, James and Eichelberger, Maryna C.},
abstractNote = {A(H1N1)pdm09 influenza A viruses predominated in the 2013–2014 USA influenza season, and although most of these viruses remain sensitive to Food and Drug Administration-approved neuraminidase (NA) inhibitors, alternative therapies are needed. Here we show that monoclonal antibody CD6, selected for binding to the NA of the prototypic A(H1N1)pdm09 virus, A/California/07/2009, protects mice against lethal virus challenge. The crystal structure of NA in complex with CD6 Fab reveals a unique epitope, where the heavy-chain complementarity determining regions (HCDRs) 1 and 2 bind one NA monomer, the light-chain CDR2 binds the neighbouring monomer, whereas HCDR3 interacts with both monomers. This 30-amino-acid epitope spans the lateral face of an NA dimer and is conserved among circulating A(H1N1)pdm09 viruses. These results suggest that the large, lateral CD6 epitope may be an effective target of antibodies selected for development as therapeutic agents against circulating H1N1 influenza viruses.},
doi = {10.1038/ncomms7114},
journal = {Nature Communications},
number = 1,
volume = 6,
place = {United States},
year = {Tue Feb 10 00:00:00 EST 2015},
month = {Tue Feb 10 00:00:00 EST 2015}
}
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