Abstract
Human herpesvirus 8 (HHV-8) is an oncogenic virus that enters cells by fusion of the viral and endosomal cellular membranes in a process mediated by viral surface glycoproteins. One of the cellular receptors hijacked by HHV-8 to gain access to cells is the EphA2 tyrosine kinase receptor. Here we solve the crystal structure of the HHV-8 envelope glycoprotein complex gH/gL, bound to EphA2, to reveal a pivotal role for the conserved gH residue E52 and the amino-terminal peptide of gL. Using quantitative Förster Resonance Energy transfer measurements and cell contraction assays, we demonstrate that the gH/gL complex functionally mimics ephrin ligand by inducing EphA2 receptor association via its dimerization interface, thus triggering receptor signaling for cytoskeleton remodeling.
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