ArticleJournal of molecular biology2008
Complex of a protective antibody with its Ebola virus GP peptide epitope: unusual features of a V lambda x light chain.
Article in Journal of molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
38 citing papers in PubMed, 56 citations in OpenAlex.
- Trial
- Treatment of Ebola Virus Disease: From Serotherapy to the Use of Monoclonal Antibodies.Antibodies (Basel, Switzerland) · 2025Review
- Fully human monoclonal antibodies against Ebola virus possess complete protection in a hamster model.Emerging microbes & infections · 2024Article
- Article
- Development and Structural Analysis of Antibody Therapeutics for Filoviruses.Pathogens (Basel, Switzerland) · 2022Review
- Potential neutralizing antibodies discovered for novel corona virus using machine learning.Scientific reports · 2021Article
- Structural Biology Illuminates Molecular Determinants of Broad Ebolavirus Neutralization by Human Antibodies for Pan-Ebolavirus Therapeutic Development.Frontiers in immunology · 2021Review
- A Virion-Based Assay for Glycoprotein Thermostability Reveals Key Determinants of Filovirus Entry and Its Inhibition.Journal of virology · 2020Article
- Article
- Article
- Dissociation of the Dimer of the Intrinsically Disordered Domain of RNase Y upon Antibody Binding.Biophysical journal · 2018Article
- Antibody Repertoires to the Same Ebola Vaccine Antigen Are Differentially Affected by Vaccine Vectors.Cell reports · 2018Article
- Epitope mapping of Ebola virus dominant and subdominant glycoprotein epitopes facilitates construction of an epitope-based DNA vaccine able to focus the antibody response in mice.Human vaccines & immunotherapeutics · 2017Article
- Combinatorial peptide-based epitope mapping from Ebola virus DNA vaccines and infections reveals residue-level determinants of antibody binding.Human vaccines & immunotherapeutics · 2017Article
- Article
- De novo protein sequencing, humanization and in vitro effects of an antihuman CD34 mouse monoclonal antibody.Biochemistry and biophysics reports · 2017Article
- Both Epistasis and Diversifying Selection Drive the Structural Evolution of the Ebola Virus Glycoprotein Mucin-Like Domain.Journal of virology · 2016Article
- Structural and molecular basis for Ebola virus neutralization by protective human antibodies.Science (New York, N.Y.) · 2016Article
- Mechanism of Binding to Ebola Virus Glycoprotein by the ZMapp, ZMAb, and MB-003 Cocktail Antibodies.Journal of virology · 2015Article
- Comparative Analysis of Host Cell Entry of Ebola Virus From Sierra Leone, 2014, and Zaire, 1976.The Journal of infectious diseases · 2015Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
13F6-1-2 is a murine monoclonal antibody that recognizes the heavily glycosylated mucin-like domain of the Ebola virus virion-attached glycoprotein (GP) and protects animals against lethal viral challenge. Here we present the crystal structure, at 2.0 A, of 13F6-1-2 in complex with its Ebola virus GP peptide epitope. The GP peptide binds in an extended conformation, anchored primarily by interactions with the heavy chain. Two GP residues, Gln P406 and Arg P409, make extensive side-chain hydrogen bond and electrostatic interactions with the antibody and are likely critical for recognition and affinity. The 13F6-1-2 antibody utilizes a rare V lambda(x) light chain. The three light-chain complementarity-determining regions do not adopt canonical conformations and represent new classes of structures distinct from V kappa and other V lambda light chains. In addition, although V lambda(x) had been thought to confer specificity, all light-chain contacts are mediated through germ-line-encoded residues. This structure of an antibody that protects against the Ebola virus now provides a framework for humanization and development of a postexposure immunotherapeutic.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.