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Journal of Virology, March 2003, p. 3334-3338, Vol. 77, No. 5
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.5.3334-3338.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Ebola Virus Transcription Activator VP30 Is a Zinc-Binding Protein

Jens Modrof, Stephan Becker, and Elke Mühlberger*

Institut für Virologie der Philipps-Universität Marburg, 35037 Marburg, Germany

Received 12 September 2002/ Accepted 20 November 2002

Ebola virus VP30 is an essential activator of viral transcription. In viral particles, VP30 is closely associated with the nucleocapsid complex. A conspicuous structural feature of VP30 is an unconventional zinc-binding Cys3-His motif comprising amino acids 68 to 95. By using a colorimetric zinc-binding assay we found that the VP30-specific Cys3-His motif stoichiometrically binds zinc ions in a one-to-one relationship. Substitution of the conserved cysteines and the histidine within the motif led to a complete loss of the capacity for zinc binding. Functional analyses revealed that none of the tested mutations of the proposed zinc-coordinating residues influenced binding of VP30 to nucleocapsid-like particles but, concerning its role in activating viral transcription, all resulted in a protein that was inactive.

* Corresponding author. Mailing address: Institut für Virologie der Philipps-Universität Marburg, Robert-Koch-Str. 17, 35037 Marburg, Germany. Phone: 49 6421-2864314. Fax: 49 6421-2865482. E-mail: muehlber{at}mailer.uni-marburg.de.

Journal of Virology, March 2003, p. 3334-3338, Vol. 77, No. 5
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.5.3334-3338.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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