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

Ulrike E. Maurer; Tzviya Zeev-Ben-Mordehai; Arun Prasad Pandurangan; Tina M. Cairns; Brian P. Hannah; J. Charles Whitbeck; Roselyn J. Eisenberg; Gary H. Cohen; Maya Topf; Juha T. Huiskonen; Kay Gruenewald

doi:10.1016/j.str.2013.05.018

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

Ulrike E. Maurer
, Tzviya Zeev-Ben-Mordehai
, Arun Prasad Pandurangan
, Tina M. Cairns
, Brian P. Hannah
, J. Charles Whitbeck
, Roselyn J. Eisenberg
, Gary H. Cohen
, Maya Topf
, Juha T. Huiskonen
, Kay Gruenewald

extern

Research output: Contribution to journal › Article › Academic › peer-review

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.

Original language	English
Pages (from-to)	1396-1405
Number of pages	10
Journal	Structure with Folding & design
Volume	21
Issue number	8
DOIs	https://doi.org/10.1016/j.str.2013.05.018
Publication status	Published - 6 Aug 2013
Externally published	Yes

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Maurer, U. E., Zeev-Ben-Mordehai, T., Pandurangan, A. P., Cairns, T. M., Hannah, B. P., Whitbeck, J. C., Eisenberg, R. J., Cohen, G. H., Topf, M., Huiskonen, J. T., & Gruenewald, K. (2013). The Structure of Herpesvirus Fusion Glycoprotein B-Bilayer Complex Reveals the Protein-Membrane and Lateral Protein-Protein Interaction. Structure with Folding & design, 21(8), 1396-1405. https://doi.org/10.1016/j.str.2013.05.018

@article{6ece46607bf945ae923e293db06c2bee,

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.",

author = "Maurer, \{Ulrike E.\} and Tzviya Zeev-Ben-Mordehai and Pandurangan, \{Arun Prasad\} and Cairns, \{Tina M.\} and Hannah, \{Brian P.\} and Whitbeck, \{J. Charles\} and Eisenberg, \{Roselyn J.\} and Cohen, \{Gary H.\} and Maya Topf and Huiskonen, \{Juha T.\} and Kay Gruenewald",

year = "2013",

month = aug,

day = "6",

doi = "10.1016/j.str.2013.05.018",

language = "English",

volume = "21",

pages = "1396--1405",

journal = "Structure with Folding \& design",

issn = "0969-2126",

publisher = "Cell Press",

number = "8",

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Maurer, UE, Zeev-Ben-Mordehai, T, Pandurangan, AP, Cairns, TM, Hannah, BP, Whitbeck, JC, Eisenberg, RJ, Cohen, GH, Topf, M, Huiskonen, JT & Gruenewald, K 2013, 'The Structure of Herpesvirus Fusion Glycoprotein B-Bilayer Complex Reveals the Protein-Membrane and Lateral Protein-Protein Interaction', Structure with Folding & design, vol. 21, no. 8, pp. 1396-1405. https://doi.org/10.1016/j.str.2013.05.018

The Structure of Herpesvirus Fusion Glycoprotein B-Bilayer Complex Reveals the Protein-Membrane and Lateral Protein-Protein Interaction. / Maurer, Ulrike E.; Zeev-Ben-Mordehai, Tzviya; Pandurangan, Arun Prasad et al.
In: Structure with Folding & design, Vol. 21, No. 8, 06.08.2013, p. 1396-1405.

Research output: Contribution to journal › Article › Academic › peer-review

TY - JOUR

T1 - The Structure of Herpesvirus Fusion Glycoprotein B-Bilayer Complex Reveals the Protein-Membrane and Lateral Protein-Protein Interaction

AU - Maurer, Ulrike E.

AU - Zeev-Ben-Mordehai, Tzviya

AU - Pandurangan, Arun Prasad

AU - Cairns, Tina M.

AU - Hannah, Brian P.

AU - Whitbeck, J. Charles

AU - Eisenberg, Roselyn J.

AU - Cohen, Gary H.

AU - Topf, Maya

AU - Huiskonen, Juha T.

AU - Gruenewald, Kay

PY - 2013/8/6

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N2 - 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.

AB - 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.

U2 - 10.1016/j.str.2013.05.018

DO - 10.1016/j.str.2013.05.018

M3 - Article

SN - 0969-2126

VL - 21

SP - 1396

EP - 1405

JO - Structure with Folding & design

JF - Structure with Folding & design

IS - 8

ER -

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

Abstract

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