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J Gen Virol 75 (1994), 809-818; DOI 10.1099/0022-1317-75-4-809
© 1994 Society for General Microbiology
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The nucleoprotein of Marburg virus is phosphorylated

Stephan Becker, Sabine Huppertz, Hans-Dieter Klenk and Heinz Feldmann{dagger}

Institut für Virologie, Robert-Koch-Straße 17, 35037 Marburg, Germany

The nucleoprotein (NP) of Marburg virus (MBG), a filovirus, is encoded by the gene closest to the 3' end of the non-segmented negative-strand RNA genome. Sequence comparison has indicated that NP is the functional equivalent to the nucleoproteins of paramyxoviruses and rhabdoviruses. Expression of recombinant NP in two eukaryotic systems using vaccinia virus and baculovirus (vectors pSC11 and pAcYMB1, respectively) and analysis of MBG-specific proteins have demonstrated that the NP of MBG is phosphorylated. The NP appeared in two forms differing in Mr by about 2K (94K and 92K respectively). Dephosphorylation clearly demonstrated that the 94K form is phosphorylated whereas the 92K form is unphosphorylated. In virion particles NP was exclusively present in the phosphorylated form. These findings suggest that only the phosphorylated NP can form nucleocapsid complexes and interact with the genomic RNA.

{dagger} Present address: Special Pathogens Branch, Centers for Disease Control, 1600 Clifton Road, Mail Stop G14, Atlanta, Georgia 30333, U.S.A.

Received 26 July 1993; accepted 1 November 1993.


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