English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  The Structure of Herpesvirus Fusion Glycoprotein B-Bilayer Complex Reveals the Protein-Membrane and Lateral Protein-Protein Interaction

Maurer, U. E., Zeev-Ben-Mordehai, T., Pandurangan, A. P., Cairns, T. M., Hannah, B. P., Whitbeck, J. C., et al. (2013). The Structure of Herpesvirus Fusion Glycoprotein B-Bilayer Complex Reveals the Protein-Membrane and Lateral Protein-Protein Interaction. STRUCTURE, 21(8), 1396-1405. doi:10.1016/j.str.2013.05.018.

Item is

Files

show Files
hide Files
:
1-s2.0-S0969212613002050-main.pdf (Any fulltext), 3MB
Name:
1-s2.0-S0969212613002050-main.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
open access arcticle
License:
-

Locators

show

Creators

show
hide
 Creators:
Maurer, Ulrike E.1, Author              
Zeev-Ben-Mordehai, Tzviya2, Author
Pandurangan, Arun Prasad2, Author
Cairns, Tina M.2, Author
Hannah, Brian P.2, Author
Whitbeck, J. Charles2, Author
Eisenberg, Roselyn J.2, Author
Cohen, Gary H.2, Author
Topf, Maya2, Author
Huiskonen, Juha T.1, Author              
Grünewald, Kay3, Author              
Affiliations:
1Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142              
2external, ou_persistent22              
3Former Research Groups, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565145              

Content

show
hide
Free keywords: SIMPLEX-VIRUS TYPE-1; ELECTRON-MICROSCOPE TOMOGRAPHY; CRYSTAL-STRUCTURE; TARGET MEMBRANES; LOW-PH; ENTRY; GB; CELLS; MUTANT; GD
 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.

Details

show
hide
Language(s): eng - English
 Dates: 2013
 Publication Status: Published in print
 Pages: 10
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: ISI: 000322927900015
DOI: 10.1016/j.str.2013.05.018
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: STRUCTURE
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: 600 TECHNOLOGY SQUARE, 5TH FLOOR, CAMBRIDGE, MA 02139 USA : CELL PRESS
Pages: - Volume / Issue: 21 (8) Sequence Number: - Start / End Page: 1396 - 1405 Identifier: ISSN: 0969-2126