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Structural basis for antibody-mediated neutralization of Lassa virus
Kathryn M Hastie1, Michelle A Zandonatti1, Lara M Kleinfelter2
1Department of Immunology and Microbial Science, The Scripps Research Institute, La Jolla, CA 92037, USA.
Science (New York, N.Y.)
|June 3, 2017
Summary
Lassa virus glycoprotein (GPC) structure reveals how antibodies neutralize the virus. This finding provides a template for designing vaccines against Lassa hemorrhagic fever.
Area of Science:
- Virology
- Structural Biology
- Immunology
Background:
- Lassa virus causes severe hemorrhagic fever, posing a significant health burden in West Africa.
- The viral glycoprotein (GPC) is the primary target for neutralizing antibodies.
Purpose of the Study:
- To determine the crystal structure of the Lassa virus GPC in complex with a neutralizing antibody.
- To elucidate the mechanism of antibody-mediated viral neutralization.
Main Methods:
- X-ray crystallography at 3.2-angstrom resolution.
- Biochemical analysis of antibody-GPC interactions and functional inhibition.
Main Results:
- The crystal structure reveals an antibody binding extensively to the base of the trimeric GPC, anchoring two monomers.
- Biochemical data indicate neutralization occurs by blocking essential conformational changes for viral entry.
- The study illuminates pH-driven conformational changes within the GPC subunits.
Conclusions:
- The determined structure provides a detailed view of the arenavirus glycoprotein spike assembly.
- This research offers a crucial template for developing effective Lassa virus vaccines.
- Understanding the neutralization mechanism aids in designing strategies against Lassa virus threats.
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