Measles virus phosphoprotein retains the nucleocapsid protein in the cytoplasm

Marion Huber, Roberto Cattaneo, Pius Spielhofer, Claes Örvell, Erling Norrby, Marius Messerli, Jean Claude Perriard, Martin A. Billeter

Research output: Contribution to journalArticlepeer-review

113 Scopus citations


Measles virus (MV) proteins were efficiently expressed in COS and Vero cells from vectors based on the strong cytomegalovirus enhancer-promoter and the simian virus 40 origin of replication. When expressed alone, nucleocapsid protein (N) migrates predominantly into the nucleus whereas phosphoprotein (P) is located in the cytoplasm. Coexpression of N and P proteins results in retention of the N protein in the cytoplasm, as seen also in infected cells. The retention of N protein is due to specific interactions with the P protein since coexpression of N with either the matrix or the hemagglutinin protein had no effect. Mapping of the regions of NP interactions on P protein revealed that the carboxy-terminal 40% of P was sufficient for specific binding to N; however, the carboxy-terminal 60% of P was required for retention of N in the cytoplasm. Thus, the V and C proteins encoded within the first half of the P gene are not involved in the cytoplasmic retention of N protein. N protein might be fortuitously targeted to the nucleus as a result of its many basic amino acids, presumably destined to interact with the MV genome. However, this set of experiments has allowed to analyze in vivo the interactions between the N and P proteins.

Original languageEnglish (US)
Pages (from-to)299-308
Number of pages10
Issue number1
StatePublished - Nov 1991

ASJC Scopus subject areas

  • Virology


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