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Journal of Virology, January 2006, p. 1038-1043, Vol. 80, No. 2
0022-538X/06/$08.00+0 doi:10.1128/JVI.80.2.1038-1043.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.
Department of Virology, Philipps University Marburg, Robert-Koch-Str. 17, 35037 Marburg, Germany,1 Filovirus Laboratory, INSERM U412, Claude Bernard University Lyon 1, IFR 128, BioSciences Lyon-Gerland, 21 av Tony Garnier, 69365 Lyon Cedex 07, France,2 Dade Behring Marburg GmbH, Marburg, Germany3
Received 18 July 2005/ Accepted 13 October 2005
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.
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