TY - JOUR
T1 - Measles virus phosphoprotein retains the nucleocapsid protein in the cytoplasm
AU - Huber, Marion
AU - Cattaneo, Roberto
AU - Spielhofer, Pius
AU - Örvell, Claes
AU - Norrby, Erling
AU - Messerli, Marius
AU - Perriard, Jean Claude
AU - Billeter, Martin A.
N1 - Funding Information:
We thank Michael Bavand and Martina Metzler for technical advice and Karin Kaelin for critically reading the manuscript. This work was supported by Grant 31-9434.88 of the Schweizerische Nation-alfonds and the Kanton of Zurich.
PY - 1991/11
Y1 - 1991/11
N2 - 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.
AB - 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.
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U2 - 10.1016/0042-6822(91)90777-9
DO - 10.1016/0042-6822(91)90777-9
M3 - Article
C2 - 1656588
AN - SCOPUS:0026007048
SN - 0042-6822
VL - 185
SP - 299
EP - 308
JO - Virology
JF - Virology
IS - 1
ER -