The Large Groove Found in the gH/gL Structure Is an Important Functional Domain for Epstein-Barr Virus Fusion

The KGD Motif of Epstein-Barr Virus gH/gL Is Bifunctional, Orchestrating Infection of B Cells and Epithelial Cells

(2012) J. Chen et al.   mBio

Fusion of Epstein-Barr Virus with Epithelial Cells Can Be Triggered by  v 5 in Addition to  v 6 and  v 8, and Integrin Binding Triggers a Conformational Change in Glycoproteins gHgL

(2011) L. S. Chesnokova et al.   JOURNAL OF VIROLOGY

Fusing structure and function: a structural view of the herpesvirus entry machinery

(2011) Sarah A. Connolly et al.   NATURE REVIEWS MICROBIOLOGY

Investigation of the function of the putative self-association site of Epstein–Barr virus (EBV) glycoprotein 42 (gp42)

(2011) Cynthia L. Rowe et al.   VIROLOGY

Mapping the N-Terminal Residues of Epstein-Barr Virus gp42 That Bind gH/gL by Using Fluorescence Polarization and Cell-Based Fusion Assays

(2010) F. Liu et al.   JOURNAL OF VIROLOGY

Crystal structure of the conserved herpesvirus fusion regulator complex gH–gL

(2010) Tirumala K Chowdary et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Crystal structure of the Epstein-Barr virus (EBV) glycoprotein H/glycoprotein L (gH/gL) complex

(2010) H. Matsuura et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Integrins as triggers of Epstein-Barr virus fusion and epithelial cell infection

(2010) Lindsey M. Hutt-Fletcher et al.   Virulence