NP:P and NP:V interactions of the paramyxovirus simian virus 5 examined using a novel protein:protein capture assay

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Abstract

Using recombinant proteins extracted from mammalian cells, in a novel protein:protein binding assay, direct interaction of the nucleoprotein (NP) of simian virus 5 with the phosphoprotein (P) and V protein (V) was demonstrated. The amount of NP bound by V was found to be significantly less than that bound by P. Furthermore, preabsorption of NP with P removed the fraction of NP that could be bound by V, but preabsorption of NP with V did not remove all the NP that could be bound by P. These results suggested that V bound a subpopulation of the NP recognised by P. Further analysis revealed that P bound both soluble and homopolymeric forms of NP, while V bound only the soluble form; thus demonstrating that the binding sites on P and V, for soluble NP, are located within the N-terminal domain common to both P and V proteins. A monoclonal antibody, which recognised an epitope in the unique C-terminus of P, blocked the binding of P to polymeric NP but not to soluble NP. These results also suggest that there are two binding sites on NP for P; the site that interacts with the P/V common domain being either hidden or conformationally altered in polymeric NP. (C) 1996 Academic Press, Inc.

Original languageEnglish
Pages (from-to)121-9
Number of pages9
JournalVirology
Volume224
Issue number1
Publication statusPublished - 1 Oct 1996

Keywords

  • NUCLEOCAPSID-LIKE STRUCTURES
  • RNA-SYNTHESIS
  • GENOME REPLICATION
  • PHOSPHOPROTEIN P
  • INCLUSION-BODIES
  • TERMINAL DOMAINS
  • NUCLEOPROTEIN N
  • MESSENGER-RNA
  • RABIES VIRUS
  • CELLS

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