title: Herpesvirus gB: A Finely Tuned Fusion Machine.
abstract: Enveloped viruses employ a class of proteins known as fusogens to orchestrate the merger of their surrounding envelope and a target cell membrane. Most fusogens accomplish this task alone, by binding cellular receptors and subsequently catalyzing the membrane fusion process. Surprisingly, in herpesviruses, these functions are distributed among multiple proteins: the conserved fusogen gB, the conserved gH/gL heterodimer of poorly defined function, and various non-conserved receptor-binding proteins. We summarize what is currently known about gB from two closely related herpesviruses, HSV-1 and HSV-2, with emphasis on the structure of the largely uncharted membrane interacting regions of this fusogen. We propose that the unusual mechanism of herpesvirus fusion could be linked to the unique architecture of gB.
authors.affiliation: Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, MA 02111, USA. rebecca.cooper@tufts.edu.
authors.forename: Rebecca S
authors.initials: RS
authors.lastname: Cooper
authors.affiliation: Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, MA 02111, USA. katya.heldwein@tufts.edu.
authors.forename: Ekaterina E
authors.initials: EE
authors.lastname: Heldwein
mesh_terms: D018259:Herpesvirus 1, Human / Q000502:physiology*; D018258:Herpesvirus 2, Human / Q000502:physiology*; D006801:Humans; D014759:Viral Envelope Proteins / Q000378:metabolism*; D053586:Virus Internalization
chemical_list: D014759:Viral Envelope Proteins; C044525:glycoprotein B, herpes simplex virus type 2; C562160:glycoprotein B, human herpesvirus 1
keywords: X-ray crystallography; cell entry; electron microscopy; electron tomography; glycoproteins; herpesviruses; membrane fusion; virions