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Journal of Virology, April 2007, p. 3942-3948, Vol. 81, No. 8
0022-538X/07/$08.00+0     doi:10.1128/JVI.02263-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Role of the Transmembrane Domain of Marburg Virus Surface Protein GP in Assembly of the Viral Envelope

Eva Mittler,^1,2, Larissa Kolesnikova,^1,2, Thomas Strecker,¹ Wolfgang Garten,¹ and Stephan Becker^1,2*

Institute of Virology, Philipps University Marburg, Hans-Meerwein Strasse, 35037 Marburg,¹ Robert Koch-Institute Berlin, Nordufer 20, 13353 Berlin, Germany²

Received 16 October 2006/ Accepted 19 January 2007

The major protein constituents of the filoviral envelope are the matrix protein VP40 and the surface transmembrane protein GP. While VP40 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.

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* Corresponding author. Mailing address: Robert Koch-Institut, Nordufer 20, 13353 Berlin, Germany. Phone: 49 30-45472372. Fax: 49 30-45472181. E-mail: beckerst{at}rki.de

Published ahead of print on 31 January 2007.

Equal contributors.

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Journal of Virology, April 2007, p. 3942-3948, Vol. 81, No. 8
0022-538X/07/$08.00+0     doi:10.1128/JVI.02263-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

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