Role of the transmembrane domain of Marburg virus surface protein GP in assembly of the viral envelope

Eva-Maria Mittler, Larissa Kolesnikova, Thomas Strecker, Wolfgang Garten, Stephan Becker

Research output: Contribution to journalArticle

32 Citations (Scopus)

Abstract

The major protein constituents of the filoviral envelope are the matrix protein VP40 and the surface transmembrane protein GP. While 7P40 is recruited to the sites of budding via the late retrograde endosomal transport route, GP is suggested to be transported via the classical secretory pathway involving the endoplasmic reticulum, Golgi apparatus, and trans-Golgi network until it reaches the plasma membrane where most filoviral budding takes place. Since both transport routes target the plasma membrane, it was thought that GP and VP40 join there to form the viral envelope. However, it was recently shown that, upon coexpression of both proteins, GP is partially recruited into peripheral VP40-enriched multivesicular bodies, which contained markers of the late endosome. Accumulation of GP and VP40 in this compartment was presumed to play an important role in the formation of the filoviral envelope. Using a domain-swapping approach, we were able to show that the transmembrane domain of GP was essential and sufficient for (i) partial recruitment of chimeric glycoproteins into VP40-enriched multivesicular bodies and (ii) incorporation into virus-like particles (VLPs) that were released upon expression of VP40. Only those chimeric glycoproteins which were targeted to VP40-enriched endosomal multivesicular bodies were subsequently recruited into VLPs. These data show that the transmembrane domain of GP is critical for the mixing of VP40 and GP in multivesicular bodies and incorporation of GP into the viral envelope. Results further suggest that trapping of GP in the VP40-enriched late endosomal compartment is important for the formation of the viral envelope.

Original languageEnglish (US)
Pages (from-to)3942-3948
Number of pages7
JournalJournal of Virology
Volume81
Issue number8
DOIs
StatePublished - Apr 1 2007
Externally publishedYes

Fingerprint

Marburg virus
Marburgvirus
Multivesicular Bodies
Virus Assembly
surface proteins
Membrane Proteins
virus-like particles
glycoproteins
plasma membrane
Virion
Glycoproteins
endosomes
transmembrane proteins
proteins
Cell Membrane
Golgi apparatus
trans-Golgi Network
endoplasmic reticulum
Proteins
trapping

ASJC Scopus subject areas

  • Microbiology
  • Immunology
  • Insect Science
  • Virology

Cite this

Role of the transmembrane domain of Marburg virus surface protein GP in assembly of the viral envelope. / Mittler, Eva-Maria; Kolesnikova, Larissa; Strecker, Thomas; Garten, Wolfgang; Becker, Stephan.

In: Journal of Virology, Vol. 81, No. 8, 01.04.2007, p. 3942-3948.

Research output: Contribution to journalArticle

Mittler, Eva-Maria ; Kolesnikova, Larissa ; Strecker, Thomas ; Garten, Wolfgang ; Becker, Stephan. / Role of the transmembrane domain of Marburg virus surface protein GP in assembly of the viral envelope. In: Journal of Virology. 2007 ; Vol. 81, No. 8. pp. 3942-3948.
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