Phosphorylation of Marburg virus matrix protein VP40 triggers assembly of nucleocapsids with the viral envelope at the plasma membrane

Larissa Kolesnikova, Eva Mittler, Gordian Schudt, Hosam Shams-Eldin, Stephan Becker

Research output: Contribution to journalArticle

26 Scopus citations


Marburg virus (MARV) matrix protein VP40 plays a key role in virus assembly, recruiting nucleocapsids and the surface protein GP to filopodia, the sites of viral budding. In addition, VP40 is the only MARV protein able to induce the release of filamentous virus-like particles (VLPs) indicating its function in MARV budding. Here, we demonstrated that VP40 is phosphorylated and that tyrosine residues at positions 7, 10, 13 and 19 represent major phosphorylation acceptor sites. Mutagenesis of these tyrosine residues resulted in expression of a non-phosphorylatable form of VP40 (VP40 mut). VP40 mut was able to bind to cellular membranes, produce filamentous VLPs, and inhibit interferon-induced gene expression similarly to wild-type VP40. However, VP40 mut was specifically impaired in its ability to recruit nucleocapsid structures into filopodia, and released infectious VLPs (iVLPs) had low infectivity. These results indicated that tyrosine phosphorylation of VP40 is important for triggering the recruitment of nucleocapsids to the viral envelope.

Original languageEnglish (US)
Pages (from-to)182-197
Number of pages16
JournalCellular Microbiology
Issue number2
StatePublished - Feb 1 2012
Externally publishedYes


ASJC Scopus subject areas

  • Microbiology
  • Immunology
  • Virology

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