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Virologica Sinica, 26 (3) : 156-170, 2011
Characterization of the Receptor-binding Domain of Ebola Glycoprotein in Viral Entry
1.Department of Microbiology and Immunology, College of Medicine, University of Illinois at Chicago, Chicago, IL 60612, USA
2.Department of Biochemistry and Molecular Genetics, College of Medicine, University of Illinois at Chicago, Chicago, IL 60607 USA
3. Current address for B. M: Department of Microbiology,Mount Sinai School of Medicine,1 Gustave L. Levy Place, Box 1124 New York, NY 10029, USA
 Correspondence: lijun@uic.edu
(886.98KB)  
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.
Received: 25 Apr 2011  Accepted: 31 Mar 2011  Published online: 5 Jun 2011
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