title: The structure of herpesvirus fusion glycoprotein B-bilayer complex reveals the protein-membrane and lateral protein-protein interaction.
abstract: Glycoprotein B (gB) is a key component of the complex herpesvirus fusion machinery. We studied membrane interaction of two gB ectodomain forms and present an electron cryotomography structure of the gB-bilayer complex. The two forms differed in presence or absence of the membrane proximal region (MPR) but showed an overall similar trimeric shape. The presence of the MPR impeded interaction with liposomes. In contrast, the MPR-lacking form interacted efficiently with liposomes. Lateral interaction resulted in coat formation on the membranes. The structure revealed that interaction of gB with membranes was mediated by the fusion loops and limited to the outer membrane leaflet. The observed intrinsic propensity of gB to cluster on membranes indicates an additional role of gB in driving the fusion process forward beyond the transient fusion pore opening and subsequently leading to fusion pore expansion.
authors.affiliation: Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, Martinsried 82152, Germany.
authors.forename: Ulrike E
authors.initials: UE
authors.lastname: Maurer
authors.forename: Tzviya
authors.initials: T
authors.lastname: Zeev-Ben-Mordehai
authors.forename: Arun Prasad
authors.initials: AP
authors.lastname: Pandurangan
authors.forename: Tina M
authors.initials: TM
authors.lastname: Cairns
authors.forename: Brian P
authors.initials: BP
authors.lastname: Hannah
authors.forename: J Charles
authors.initials: JC
authors.lastname: Whitbeck
authors.forename: Roselyn J
authors.initials: RJ
authors.lastname: Eisenberg
authors.forename: Gary H
authors.initials: GH
authors.lastname: Cohen
authors.forename: Maya
authors.initials: M
authors.lastname: Topf
authors.forename: Juha T
authors.initials: JT
authors.lastname: Huiskonen
authors.forename: Kay
authors.initials: K
authors.lastname: Grünewald
mesh_terms: D002478:Cells, Cultured; D020285:Cryoelectron Microscopy; D018360:Crystallography, X-Ray; D018259:Herpesvirus 1, Human / Q000648:ultrastructure*; D006801:Humans; D008051:Lipid Bilayers / Q000737:chemistry; D008081:Liposomes / Q000737:chemistry; D008958:Models, Molecular; D011485:Protein Binding; D054730:Protein Interaction Domains and Motifs; D020836:Protein Structure, Quaternary; D014759:Viral Envelope Proteins / Q000737:chemistry*; D053585:Virus Attachment
chemical_list: D008051:Lipid Bilayers; D008081:Liposomes; D014759:Viral Envelope Proteins; C562160:glycoprotein B, human herpesvirus 1