Characterization of the receptor-binding domain of Ebola glycoprotein in viral entry |
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Authors: | Jizhen Wang Balaji Manicassamy Michael Caffrey Lijun Rong |
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Institution: | (1) Department of Microbiology and Immunology, College of Medicine, University of Illinois at Chicago, Chicago, Illinois, USA;(2) Department of Microbiology, Mount Sinai School of Medicine, 1 Gustave L Levy Place, Box 1124, New York, New York, USA |
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Abstract: | Ebola virus infection causes severe hemorrhagic fever in human and non-human primates with high mortality. Viral entry/infection
is initiated by binding of glycoprotein GP protein on Ebola virion to host cells, followed by fusion of virus-cell membrane
also mediated by GP. Using an human immunodeficiency virus (HIV)-based pseudotyping system, the roles of 41 Ebola GP1 residues
in the receptor-binding domain in viral entry were studied by alanine scanning substitutions. We identified that four residues
appear to be involved in protein folding/structure and four residues are important for viral entry. An improved entry interference
assay was developed and used to study the role of these residues that are important for viral entry. It was found that R64
and K95 are involved in receptor binding. In contrast, some residues such as I170 are important for viral entry, but do not
play a major role in receptor binding as indicated by entry interference assay and/or protein binding data, suggesting that
these residues are involved in post-binding steps of viral entry. Furthermore, our results also suggested that Ebola and Marburg
viruses share a common cellular molecule for entry. |
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Keywords: | |
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