4.7 Article

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

期刊

BIOMOLECULES
卷 8, 期 2, 页码 -

出版社

MDPI
DOI: 10.3390/biom8020025

关键词

EBOV GP; ZIKV E; pre-fusion-to-fusion transition; antibody binding

资金

  1. U.S. Department of Energy through the LANL/LDRD Program [20170509DR]
  2. NIAID Centers of Excellence for Influenza Research and Surveillance (CEIRS) [HHSN272201400004C]

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Membrane fusion proteins are responsible for viral entry into host cellsa 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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