Hostname: page-component-586b7cd67f-rdxmf Total loading time: 0 Render date: 2024-11-27T00:32:41.227Z Has data issue: false hasContentIssue false

From Kenema to Our Krios: Medical Defense Against Lassa Virus and Emerging Infectious Disease

Published online by Cambridge University Press:  30 July 2020

Erica Saphire
Affiliation:
La Jolla Institute for Immunology, La Jolla, California, United States
Haoyang Li
Affiliation:
La Jolla Institute for Immunology, La Jolla, California, United States
Kathryn Hastie
Affiliation:
La Jolla Institute for Immunology, La Jolla, California, United States
Luis Branco
Affiliation:
Zalgen Labs, Gerrmantown, Maryland, United States
Robert Garry
Affiliation:
Tulane University School of Medicine, New Orleans, Louisiana, United States
Stephanie Harkins
Affiliation:
La Jolla Institute for Immunology, La Jolla, California, United States
Adrian Enriquez
Affiliation:
La Jolla Institute for Immunology, La Jolla, California, United States
Tierra Buck
Affiliation:
La Jolla Institute for Immunology, La Jolla, California, United States
Michelle Zandonatti
Affiliation:
La Jolla Institute for Immunology, La Jolla, California, United States

Abstract

Image of the first page of this content. For PDF version, please use the ‘Save PDF’ preceeding this image.'
Type
3D Structures: From Macromolecular Assemblies to Whole Cells (3DEM FIG)
Copyright
Copyright © Microscopy Society of America 2020

References

Hastie, K.M., Zadonatti, M.A., Kleinfelter, L.M., Heinrich, M.L., Rowland, M.M., Chandran, K., Branco, L.M., Robinson, J.E., Garry, R.F. and Saphire, E.O. (2017) Structural basis for antibody-mediated neutralization of Lassa virus. Science, 356:923-928.10.1126/science.aam7260CrossRefGoogle ScholarPubMed
Robinson, J.E., et al. for the Viral Hemorrhagic Fever Consortium. (2016) Most neutralizing human monoclonal antibodies target novel epitopes requiring both Lassa virus glycoprotein subunits. Nature Comm. May 10;7:1154410.1038/ncomms11544CrossRefGoogle ScholarPubMed