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

Research output: Contribution to journalArticleAcademicpeer-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 languageEnglish
Pages (from-to)1396-1405
Number of pages10
JournalStructure with Folding & design
Volume21
Issue number8
DOIs
Publication statusPublished - 6 Aug 2013
Externally publishedYes

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