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Biomolecules 2018, 8(2), 25; https://doi.org/10.3390/biom8020025

Structural Transition and Antibody Binding of EBOV GP and ZIKV E Proteins from Pre-Fusion to Fusion-Initiation State

1
Los Alamos National Laboratory, Los Alamos, NM 87545, USA
2
New Mexico Consortium, Los Alamos, NM 87545, USA
3
College of Public Health, University of Georgia, Athens, GA 30602, USA
*
Author to whom correspondence should be addressed.
Received: 4 April 2018 / Revised: 4 May 2018 / Accepted: 7 May 2018 / Published: 10 May 2018
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Abstract

Membrane fusion proteins are responsible for viral entry into host cells—a crucial first step in viral infection. These proteins undergo large conformational changes from pre-fusion to fusion-initiation structures, and, despite differences in viral genomes and disease etiology, many fusion proteins are arranged as trimers. Structural information for both pre-fusion and fusion-initiation states is critical for understanding virus neutralization by the host immune system. In the case of Ebola virus glycoprotein (EBOV GP) and Zika virus envelope protein (ZIKV E), pre-fusion state structures have been identified experimentally, but only partial structures of fusion-initiation states have been described. While the fusion-initiation structure is in an energetically unfavorable state that is difficult to solve experimentally, the existing structural information combined with computational approaches enabled the modeling of fusion-initiation state structures of both proteins. These structural models provide an improved understanding of four different neutralizing antibodies in the prevention of viral host entry.
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Keywords: EBOV GP; ZIKV E; pre-fusion-to-fusion transition; antibody binding EBOV GP; ZIKV E; pre-fusion-to-fusion transition; antibody binding
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Lappala, A.; Nishima, W.; Miner, J.; Fenimore, P.; Fischer, W.; Hraber, P.; Zhang, M.; McMahon, B.; Tung, C.-S. Structural Transition and Antibody Binding of EBOV GP and ZIKV E Proteins from Pre-Fusion to Fusion-Initiation State. Biomolecules 2018, 8, 25.

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