Rescue of Recombinant Marburg Virus from cDNA Is Dependent on Nucleocapsid Protein VP30

Author:

Enterlein Sven1,Volchkov Viktor2,Weik Michael13,Kolesnikova Larissa1,Volchkova Valentina2,Klenk Hans-Dieter1,Mühlberger Elke1

Affiliation:

1. Department of Virology, Philipps University Marburg, Robert-Koch-Str. 17, 35037 Marburg, Germany

2. Filovirus Laboratory, INSERM U412, Claude Bernard University Lyon 1, IFR 128, BioSciences Lyon-Gerland, 21 av Tony Garnier, 69365 Lyon Cedex 07, France

3. Dade Behring Marburg GmbH, Marburg, Germany

Abstract

ABSTRACT Here we report recovery of infectious Marburg virus (MARV) from a full-length cDNA clone. Compared to the wild-type virus, recombinant MARV showed no difference in terms of morphology of virus particles, intracellular distribution in infected cells, and growth kinetics. The nucleocapsid protein VP30 of MARV and Ebola virus (EBOV) contains a Zn-binding motif which is important for the function of VP30 as a transcriptional activator in EBOV, whereas its role for MARV is unclear. It has been reported previously that MARV VP30 is able to support transcription in an EBOV-specific minigenome system. When the Zn-binding motif was destroyed, MARV VP30 was shown to be inactive in the EBOV system. While it was not possible to rescue recombinant MARV when the VP30 plasmid was omitted from transfection, MARV VP30 with a destroyed Zn-binding motif and EBOV VP30 were able to mediate virus recovery. In contrast, rescue of recombinant EBOV was not supported by EBOV VP30 containing a mutated Zn-binding domain.

Publisher

American Society for Microbiology

Subject

Virology,Insect Science,Immunology,Microbiology

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