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Mechanistic basis for potent neutralization of Sin Nombre hantavirus by a human monoclonal antibody
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Mechanistic basis for potent neutralization of Sin Nombre hantavirus by a human monoclonal antibody
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Journal Article
Mechanistic basis for potent neutralization of Sin Nombre hantavirus by a human monoclonal antibody
2023
Overview
Rodent-borne hantaviruses are prevalent worldwide and upon spillover to human populations, cause severe disease for which no specific treatment is available. A potent antibody response is key for recovery from hantavirus infection. Here we study a highly neutralizing human monoclonal antibody, termed SNV-42, which was derived from a memory B cell isolated from an individual with previous Sin Nombre virus (SNV) infection. Crystallographic analysis demonstrates that SNV-42 targets the Gn subcomponent of the tetrameric (Gn−Gc)
4
glycoprotein assembly that is relevant for viral entry. Integration of our 1.8 Å structure with the (Gn−Gc)
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ultrastructure arrangement indicates that SNV-42 targets the membrane-distal region of the virus envelope. Comparison of the SNV-42 paratope encoding variable genes with inferred germline gene segments reveals high sequence conservation, suggesting that germline-encoded antibodies inhibit SNV. Furthermore, mechanistic assays reveal that SNV-42 interferes with both receptor recognition and fusion during host-cell entry. This work provides a molecular-level blueprint for understanding the human neutralizing antibody response to hantavirus infection.
Structural analysis reveals how a potent human monoclonal antibody neutralizes Sin Nombre virus by binding the Gn–Gc heterodimer lattice.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
