S. Waggoner et P. Sarnow, VIRAL RIBONUCLEOPROTEIN COMPLEX-FORMATION AND NUCLEOLAR-CYTOPLASMIC RELOCALIZATION OF NUCLEOLIN IN POLIOVIRUS-INFECTED CELLS, Journal of virology, 72(8), 1998, pp. 6699-6709
The poliovirus 3' noncoding region (3'NCR) is involved in the efficien
t synthesis of viral negative-stranded RNA molecules. A strong interac
tion between a 105-kDa host protein and the wild-type 3'NCR, but not w
ith a replication-defective mutant 3'NCR was detected. This 105-kDa pr
otein was identified as nucleolin which predominantly resides in the n
ucleolus and has been proposed to function in the folding of rRNA prec
ursor molecules. A functional role for nucleolin in viral genome ampli
fication was examined in a cell-free extract which has been shown to s
upport the assembly of infectious virus from virion RNA. At early time
s of viral gene expression, extracts depleted of nucleolin produced le
ss infectious virus than extracts depleted of fibrillarin, another res
ident of the nucleolus, indicating a functional role of nucleolin in t
he early stages of the viral life cycle in this in vitro system. Immun
ofluorescence analysis of uninfected and infected cells showed a nucle
ocytoplasmic relocalization of nucleolin, but not of fibrillarin, in p
oliovirus-infected cells. Relocalization of nucleolin was not simply a
consequence of virally induced inhibition of translation or transcrip
tion, because inhibitors of translation or transcription did not induc
e nucleolar-cytoplasmic relocalization of nucleolin. These findings su
ggest a novel virus-induced mechanism by which certain nucleolar prote
ins are selectively redistributed in infected cells.