Rescue of recombinant Marburg virus from cDNA is dependent on nucleocapsid protein VP30.
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.
Enterlein
Sven
S
Department of Virology, Philipps University Marburg, Robert-Koch-Str. 17, 35037 Marburg, Germany.
Volchkov
Viktor
V
Weik
Michael
M
Kolesnikova
Larissa
L
Volchkova
Valentina
V
Klenk
Hans-Dieter
HD
Mühlberger
Elke
E
D018076:DNA, Complementary / Q000378:metabolism*; D029043:Ebolavirus / Q000737:chemistry / Q000254:growth & development; D016679:Genome, Viral; D008379:Marburg Virus Disease / Q000821:virology; D029024:Marburgvirus / Q000737:chemistry / Q000254:growth & development / Q000502:physiology*; D008969:Molecular Sequence Data; D011995:Recombination, Genetic; D014157:Transcription Factors / Q000737:chemistry / Q000502:physiology*; D014764:Viral Proteins / Q000737:chemistry / Q000502:physiology*; D015032:Zinc / Q000502:physiology
D018076:DNA, Complementary; D014157:Transcription Factors; C479897:VP30 protein, ebola virus; D014764:Viral Proteins; D015032:Zinc