Investigation of the lipid binding properties of the Marburg virus matrix protein VP40

Kaveesha J. Wijesinghe, Robert Stahelin

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

Marburg virus (MARV), which belongs to the virus family Filoviridae, causes hemorrhagic fever in humans and nonhuman primates that is often fatal. MARV is a lipid-enveloped virus that during the replication process extracts its lipid coat from the plasma membrane of the host cell it infects. MARV carries seven genes, one of which encodes its matrix protein VP40 (mVP40), which regulates the assembly and budding of the virions. Currently, little information is available on mVP40 lipid binding properties. Here, we have investigated the in vitro and cellular mechanisms by which mVP40 associates with lipid membranes. mVP40 associates with anionic membranes in a nonspecific manner that is dependent upon the anionic charge density of the membrane. These results are consistent with recent structural determination of mVP40, which elucidated an mVP40 dimer with a flat and extensive cationic lipid binding interface.

Original languageEnglish (US)
Pages (from-to)3074-3085
Number of pages12
JournalJournal of Virology
Volume90
Issue number6
DOIs
StatePublished - 2016

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Marburg virus
Marburgvirus
binding properties
Lipids
lipids
Proteins
proteins
Filoviridae
Membranes
Membrane Lipids
Virus Replication
virus replication
virion
Virion
Primates
fever
Fever
plasma membrane
Cell Membrane
Viruses

ASJC Scopus subject areas

  • Immunology
  • Virology

Cite this

Investigation of the lipid binding properties of the Marburg virus matrix protein VP40. / Wijesinghe, Kaveesha J.; Stahelin, Robert.

In: Journal of Virology, Vol. 90, No. 6, 2016, p. 3074-3085.

Research output: Contribution to journalArticle

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