Both the P and V proteins of the porcine rubulavirus LPMV interact with the NP protein via their respective C-terminal unique parts.
In this paper we show that the porcine rubulavirus LPMV phosphoprotein (P) and V protein (V) both interact with the nucleoprotein (NP). There are also indications for an interaction between P and V with L protein. Further analysis of the domains of the P and V which are necessary for interaction with the NP protein demonstrates that the interaction is not mediated from their common part but instead from their unique C-terminal parts, respectively. The common N-terminus of P and V appear to mediate the interaction with L. We also map the regions of NP that are necessary for interaction with P and V, respectively. Both P and V interact with regions of NP, which reside in the N-terminal part but appear not to overlap.
Svenda
Martin
M
Department of Veterinary Microbiology, Section of Virology, Swedish University of Agricultural Sciences, Uppsala, Sweden. martin-s@xray.bmc.uu.se
Hjertner
Bernt
B
Linné
Tommy
T
Berg
Mikael
M
D000818:Animals; D001665:Binding Sites; D015870:Gene Expression; D005982:Glutathione Transferase / Q000235:genetics / Q000378:metabolism; D019590:Nucleocapsid Proteins / Q000235:genetics / Q000378:metabolism*; D009698:Nucleoproteins / Q000235:genetics / Q000378:metabolism*; D010750:Phosphoproteins / Q000235:genetics / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism; D019213:Rubulavirus / Q000235:genetics / Q000378:metabolism*; D013552:Swine; D014758:Viral Core Proteins / Q000235:genetics / Q000378:metabolism*; D014764:Viral Proteins / Q000235:genetics / Q000378:metabolism*
D019590:Nucleocapsid Proteins; D009698:Nucleoproteins; C455099:P protein, Porcine rubulavirus; C055859:P protein, Sendai virus; D010750:Phosphoproteins; D011993:Recombinant Fusion Proteins; D014758:Viral Core Proteins; D014764:Viral Proteins; C074576:V protein, Porcine rubulavirus; D005982:Glutathione Transferase