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Peptide Scanning-assisted Identification of a Monoclonal Antibody-recognized Linear B-cell Epitope
Published on: March 24, 2017
Structural and genetic basis for broad antibody recognition of a protective epitope on orthomarburgvirus GP2
Aurelie Niyongabo1, Benjamin M Janus1, Fabrizio G Gonzalez1
1Department of Cell Biology and Molecular Genetics, University of Maryland, College Park, MD 20742, USA; Institute for Bioscience and Biotechnology Research, University of Maryland, Rockville, MD 20850, USA.
Abstract:
Orthomarburgviruses are the etiological agents of human Marburg virus disease, with case fatality rates reaching up to 90%. Of the limited known targets for protective antibodies on the orthomarburgvirus surface glycoprotein (GP), the GP2 wing region is undefined structurally, and its recognition by antibodies is poorly understood. We report a comprehensive genetic and structural analysis of four independent broadly reactive antibody lineages that target a common epitope within the GP2 wing, including macaque antibodies CM10, CM11.1, and CM12.1 and murine antibody 30G4. Co-crystal structures reveal the recognition of conserved structural determinants within the wing by all four antibodies. Immunogenetic analyses uncover common antibody sequence signatures that underlie interactions with the wing, leading in some cases to nearly identical modes of antibody binding. Our study advances the structural understanding of the GP2 wing protective region and defines conserved immunogenetic and structural features for broad antibody recognition, informing the development of vaccines and antibody countermeasures.
Insights
Researchers identified key features of the Marburg virus glycoprotein (GP) wing region targeted by broadly protective antibodies. This structural and genetic understanding is crucial for developing effective vaccines and antibody treatments against Marburg virus disease.
Area of Science:
- Virology
- Immunology
- Structural Biology
Background:
- Orthomarburgviruses cause Marburg virus disease with high fatality rates.
- The GP2 wing region of the orthomarburgvirus surface glycoprotein is a target for protective antibodies but is poorly understood structurally.
- Limited knowledge exists regarding antibody recognition of the GP2 wing region.
Purpose of the Study:
- To conduct a comprehensive genetic and structural analysis of broadly reactive antibody lineages targeting the orthomarburgvirus GP2 wing region.
- To elucidate the structural basis of antibody recognition within the GP2 wing.
- To identify conserved immunogenetic and structural features for broad antibody recognition.
Main Methods:
- Co-crystal structure determination of antibodies bound to the GP2 wing region.
- Comprehensive genetic analysis of antibody lineages.
- Immunogenetic analyses of antibody sequence signatures.
Main Results:
- Four independent, broadly reactive antibody lineages (three from macaques, one murine) target a common epitope in the GP2 wing.
- Co-crystal structures reveal conserved structural determinants within the wing recognized by all antibodies.
- Immunogenetic analyses identified common antibody sequence signatures associated with wing recognition and similar binding modes.
Conclusions:
- The study advances structural understanding of the protective GP2 wing region of orthomarburgviruses.
- Conserved immunogenetic and structural features enabling broad antibody recognition have been defined.
- Findings inform the development of vaccines and antibody countermeasures against Marburg virus.
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