Neither phosphorylation nor the amino-terminal part of rabies virus phosphoprotein is required for its oligomerization - Archive ouverte HAL Access content directly
Journal Articles Journal of General Virology Year : 2000

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

Abstract

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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hal-02118375 , version 1 (03-05-2019)

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Benoît Gigant, Frédéric Iseni, Yves Gaudin, Marcel Knossow, Danielle Blondel. Neither phosphorylation nor the amino-terminal part of rabies virus phosphoprotein is required for its oligomerization. Journal of General Virology, 2000, 81 (7), pp.1757-1761. ⟨10.1099/0022-1317-81-7-1757⟩. ⟨hal-02118375⟩
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