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Structural and Mechanistic Insights into the Tropism of Epstein-Barr Virus
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  • Journal title : Molecules and Cells
  • Volume 39, Issue 4,  2016, pp.286-291
  • Publisher : Korea Society for Molecular and Cellular Biology
  • DOI : 10.14348/molcells.2016.0066
 Title & Authors
Structural and Mechanistic Insights into the Tropism of Epstein-Barr Virus
Mohl, Britta S.; Chen, Jia; Sathiyamoorthy, Karthik; Jardetzky, Theodore S.; Longnecker, Richard;
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Epstein-Barr virus (EBV) is the prototypical -herpesvirus and an obligate human pathogen that infects mainly epithelial cells and B cells, which can result in malignancies. EBV infects these target cells by fusing with the viral and cellular lipid bilayer membranes using multiple viral factors and host receptor(s) thus exhibiting a unique complexity in its entry machinery. To enter epithelial cells, EBV requires minimally the conserved core fusion machinery comprised of the glycoproteins gH/gL acting as the receptor-binding complex and gB as the fusogen. EBV can enter B cells using gp42, which binds tightly to gH/gL and interacts with host HLA class II, activating fusion. Previously, we published the individual crystal structures of EBV entry factors, such as gH/gL and gp42, the EBV/host receptor complex, gp42/HLA-DR1, and the fusion protein EBV gB in a postfusion conformation, which allowed us to identify structural determinants and regions critical for receptor-binding and membrane fusion. Recently, we reported different low resolution models of the EBV B cell entry triggering complex (gHgL/gp42/HLA class II) in "open" and "closed" states based on negative-stain single particle electron microscopy, which provide further mechanistic insights. This review summarizes the current knowledge of these key players in EBV entry and how their structures impact receptor-binding and the triggering of gB-mediated fusion.
entry;Epstein-Barr virus;fusion;herpesvirus;tropism;
 Cited by
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