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Neither phosphorylation nor the amino-terminal part of rabies virus phosphoprotein is required for its oligomerization

Laboratoire d’Enzymologie et Biochimie Structurales (LEBS), CNRS, 91198 Gif sur Yvette, France¹
EMBL Grenoble Outstation c/o ILL PB156, 38042 Grenoble cedex, France²
Laboratoire de génétique des virus, CNRS, 91198 Gif sur Yvette, France³

Author for correspondence: Danielle Blondel. Fax +33 1 69 82 43 08. e-mail Danielle.Blondel{at}gv.cnrs-gif.fr

Rabies virus (PV strain) phosphoprotein (P) was expressed in bacteria. This recombinant protein binds specifically to the nucleoprotein–RNA complex purified from infected cells. Chemical cross-linking and gel-filtration studies indicated that the P protein forms oligomers. Analytical centrifugation data demonstrated the co-existence of monomeric and oligomeric forms of rabies virus P protein and suggested that there is an equilibrium between these species. As P expressed in bacteria is not phosphorylated, this result indicates that P phosphorylation is not required for its oligomerization. Although an alignment of several rhabdovirus P sequences revealed that the amino-terminal domain of P has a conserved predicted propensity to form helical coiled coils, an amino-terminally truncated form of P protein, lacking the first 52 residues, was also shown to be oligomeric. Therefore, the amino-terminal domain of rabies virus P is not necessary for its oligomerization.

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