Structural basis for broad neutralization of ebolaviruses by an antibody targeting the glycoprotein fusion loop

The Ebola virus glycoprotein is a target for cross-protective antibodies. Here, Janus et al. report the crystal structure of the antigen-binding fragment of a pan-reactive antibody bound to a conserved epitope of the glycoprotein, facilitating rational design of cross-protective vaccines and therape...

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Main Authors:	Benjamin M. Janus, Nydia van Dyk, Xuelian Zhao, Katie A. Howell, Cinque Soto, M. Javad Aman, Yuxing Li, Thomas R. Fuerst, Gilad Ofek
Format:	Article
Language:	English
Published:	Nature Publishing Group 2018-09-01
Series:	Nature Communications
Online Access:	https://doi.org/10.1038/s41467-018-06113-4

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spelling	doaj-20e66fb349b04412a89f063ca2921f9c2021-05-11T10:20:27ZengNature Publishing GroupNature Communications2041-17232018-09-019111210.1038/s41467-018-06113-4Structural basis for broad neutralization of ebolaviruses by an antibody targeting the glycoprotein fusion loopBenjamin M. Janus0Nydia van Dyk1Xuelian Zhao2Katie A. Howell3Cinque Soto4M. Javad Aman5Yuxing Li6Thomas R. Fuerst7Gilad Ofek8Institute for Bioscience and Biotechnology Research, University of MarylandInstitute for Bioscience and Biotechnology Research, University of MarylandInstitute for Bioscience and Biotechnology Research, University of MarylandIntegrated BioTherapeuticsThe Vanderbilt Vaccine Center, Vanderbilt University Medical CenterIntegrated BioTherapeuticsInstitute for Bioscience and Biotechnology Research, University of MarylandInstitute for Bioscience and Biotechnology Research, University of MarylandInstitute for Bioscience and Biotechnology Research, University of MarylandThe Ebola virus glycoprotein is a target for cross-protective antibodies. Here, Janus et al. report the crystal structure of the antigen-binding fragment of a pan-reactive antibody bound to a conserved epitope of the glycoprotein, facilitating rational design of cross-protective vaccines and therapeutics.https://doi.org/10.1038/s41467-018-06113-4
collection	DOAJ
language	English
format	Article
sources	DOAJ
author	Benjamin M. Janus Nydia van Dyk Xuelian Zhao Katie A. Howell Cinque Soto M. Javad Aman Yuxing Li Thomas R. Fuerst Gilad Ofek
spellingShingle	Benjamin M. Janus Nydia van Dyk Xuelian Zhao Katie A. Howell Cinque Soto M. Javad Aman Yuxing Li Thomas R. Fuerst Gilad Ofek Structural basis for broad neutralization of ebolaviruses by an antibody targeting the glycoprotein fusion loop Nature Communications
author_facet	Benjamin M. Janus Nydia van Dyk Xuelian Zhao Katie A. Howell Cinque Soto M. Javad Aman Yuxing Li Thomas R. Fuerst Gilad Ofek
author_sort	Benjamin M. Janus
title	Structural basis for broad neutralization of ebolaviruses by an antibody targeting the glycoprotein fusion loop
title_short	Structural basis for broad neutralization of ebolaviruses by an antibody targeting the glycoprotein fusion loop
title_full	Structural basis for broad neutralization of ebolaviruses by an antibody targeting the glycoprotein fusion loop
title_fullStr	Structural basis for broad neutralization of ebolaviruses by an antibody targeting the glycoprotein fusion loop
title_full_unstemmed	Structural basis for broad neutralization of ebolaviruses by an antibody targeting the glycoprotein fusion loop
title_sort	structural basis for broad neutralization of ebolaviruses by an antibody targeting the glycoprotein fusion loop
publisher	Nature Publishing Group
series	Nature Communications
issn	2041-1723
publishDate	2018-09-01
description	The Ebola virus glycoprotein is a target for cross-protective antibodies. Here, Janus et al. report the crystal structure of the antigen-binding fragment of a pan-reactive antibody bound to a conserved epitope of the glycoprotein, facilitating rational design of cross-protective vaccines and therapeutics.
url	https://doi.org/10.1038/s41467-018-06113-4
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Structural basis for broad neutralization of ebolaviruses by an antibody targeting the glycoprotein fusion loop

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