title: Stuck in the middle: structural insights into the role of the gH/gL heterodimer in herpesvirus entry.
abstract: Enveloped viruses enter cells by fusing the viral and cellular membranes, and most use a single viral envelope protein that combines receptor-binding and fusogenic functions. In herpesviruses, these functions are distributed among multiple proteins: the conserved fusion protein gB, various non-conserved receptor-binding proteins, and the conserved gH/gL heterodimer that curiously lacks an apparent counterpart in other enveloped viruses. Recent structural studies of gH/gL from HSV-2 and EBV revealed a unique complex with no structural or functional similarity to other viral proteins. Here we analyzed gH/gL structures and highlighted important functional regions. We propose that gH/gL functions as an adaptor that transmits the triggering signals from various non-conserved inputs to the highly conserved fusion protein gB.
authors.affiliation: Department of Molecular Biology and Microbiology and Graduate Program in Biochemistry, Sackler School of Graduate Biomedical Sciences, Tufts University School of Medicine, Boston, MA 02111, United States.
authors.forename: Samuel D
authors.initials: SD
authors.lastname: Stampfer
authors.forename: Ekaterina E
authors.initials: EE
authors.lastname: Heldwein
mesh_terms: D018258:Herpesvirus 2, Human / Q000737:chemistry* / Q000502:physiology; D004854:Herpesvirus 4, Human / Q000737:chemistry* / Q000502:physiology; D006801:Humans; D008954:Models, Biological; D008958:Models, Molecular; D011487:Protein Conformation; D055503:Protein Multimerization; D014759:Viral Envelope Proteins / Q000737:chemistry* / Q000378:metabolism*; D053586:Virus Internalization
chemical_list: D014759:Viral Envelope Proteins