Membrane fusion during herpesvirus entry into host cells is a complex process where multiple glycoproteins interact to relay the triggering signal from a receptor-binding protein to the conserved fusogen gB through the conserved heterodimer gH/gL. Crystal structures of individual glycoproteins are available, yet high-order 'supercomplexes' have been elusive. Recent structures of complexes between gH/gL from human cytomegalovirus or Epstein-Barr virus and the receptor-binding proteins that form at early stages of herpesviral entry highlighted mechanisms that control tropism and revealed dynamic intermediate complexes containing gH/gL that may directly participate in membrane deformation and juxtaposition. Determining how the triggering signal reaches the fusogen gB represents the next frontier in structural biology of herpesvirus entry.
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