Tuhkarokkovirus: Aitiotekijä

Genome

http://journals.plos.org/plosone/article/figure/image?size=medium&id=info:doi/10.1371/journal.pone.0143081.g001


https://www.ncbi.nlm.nih.gov/pubmed/1656588?dopt=Abstract
bmed/1656588?dopt=Abstract

Format: Abstract

Virology. 1991 Nov;185(1):299-308.

Measles virus phosphoprotein retains the nucleocapsid protein in the cytoplasm.

Huber M¹, Cattaneo R, Spielhofer P, Orvell C, Norrby E, Messerli M, Perriard JC, Billeter MA.

Abstract

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 N-P 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.

PMID:

1656588

[Indexed for MEDLINE]