The present study showed that the nuclear re-localization
of 3CD and 3C0 could be induced by 2Apro alone. It is
reported that 3CD and 3C0 of poliovirus have nuclear localization
signal, which only functions under poliovirus infection
[4]. Previously studies have indicated that NPCs were
altered during poliovirus infection [15,26] and this could
not be simply explained as virus-induced leakiness of the
NE because some functions of cellular NPCs remained
[26]. The degradation of Nup98, Nup153, and p62 by
2Apro has also been reported as important for poliovirus
infection [26,27]. It is likely that NPCs are altered by 2Apro
and then induce the re-localization of 3CD and 3C0 to the
cell nucleus. A variety of nucleo-cytoplasmic trafficking
pathways are inhibited in poliovirus-infected cells such as
importin a/b and transportin, which are the targets of the
SV40 large T antigen and heterogeneous nuclear ribonucleoprotein,
respectively. However, the transportation of
some other proteins that use the transportin-serine/
arginine-rich (SR) pathway, such as the SR protein SC35,
is not affected by poliovirus infection [26]. The
re-localization of 3CD and 3C0
, therefore, may be involved
in a special cytoplasmic–nucleic pathway that is induced
during poliovirus infection or 2Apro expression. Further
studies should be dedicated to determine the pathway used
by poliovirus 3CD and 3C0 to enter the nucleus.
Poliovirus 2Apro can cleave the eIF4G directly or
indirectly and suppress the cap-dependent translation
[28,29]. To overexpress Nup153-mCherry during investi
The present study showed that the nuclear re-localizationof 3CD and 3C0 could be induced by 2Apro alone. It isreported that 3CD and 3C0 of poliovirus have nuclear localizationsignal, which only functions under poliovirus infection[4]. Previously studies have indicated that NPCs werealtered during poliovirus infection [15,26] and this couldnot be simply explained as virus-induced leakiness of theNE because some functions of cellular NPCs remained[26]. The degradation of Nup98, Nup153, and p62 by2Apro has also been reported as important for poliovirusinfection [26,27]. It is likely that NPCs are altered by 2Aproand then induce the re-localization of 3CD and 3C0 to thecell nucleus. A variety of nucleo-cytoplasmic traffickingpathways are inhibited in poliovirus-infected cells such asimportin a/b and transportin, which are the targets of theSV40 large T antigen and heterogeneous nuclear ribonucleoprotein,respectively. However, the transportation ofsome other proteins that use the transportin-serine/arginine-rich (SR) pathway, such as the SR protein SC35,is not affected by poliovirus infection [26]. There-localization of 3CD and 3C0, therefore, may be involvedin a special cytoplasmic–nucleic pathway that is inducedduring poliovirus infection or 2Apro expression. Furtherstudies should be dedicated to determine the pathway usedby poliovirus 3CD and 3C0 to enter the nucleus.Poliovirus 2Apro can cleave the eIF4G directly orindirectly and suppress the cap-dependent translation[28,29]. To overexpress Nup153-mCherry during investi
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The Present Study showed that The Nuclear re-localization
of 3CD and 3C0 could be induced by 2Apro alone. It is
Reported that 3CD and 3C0 Nuclear localization of poliovirus Have
Signal, which only functions under poliovirus infection
[4]. Studies indicated that NPCs were previously Have
Altered during poliovirus infection [15.26] and this could
be Simply Not As explained Virus-induced leakiness of The
NE Because some functions of Cellular NPCs remained
[26]. The degradation of Nup98, Nup153, and P62 by
2Apro Reported As has also been important for poliovirus
infection [26,27]. It is likely that NPCs are Altered by 2Apro
and then induce re-localization of The 3CD and 3C0 to The
Cell Nucleus. A Variety of Nucleo-cytoplasmic trafficking
pathways in poliovirus-infected cells are Inhibited Such As
importin a / B and Transportin, which are The targets of The
SV40 Large T Antigen and heterogeneous ribonucleoprotein Nuclear,
respectively. However, The Transportation of
Other Proteins that some Transportin-Use The serine /
arginine-rich (SR) Pathway, Such As The SR protein SC35,
is Not affected by poliovirus infection [26]. The
re-localization of 3CD and 3C0
, Therefore, May be Involved
in a Special-cytoplasmic nucleic Pathway that is induced
during poliovirus infection or 2Apro Expression. Further
Studies should be Dedicated to Determine The Pathway Used
by poliovirus 3CD and 3C0 to enter The Nucleus.
Poliovirus 2Apro The EIF4G Can cleave directly or
indirectly and suppress The Cap-dependent Translation
[28,29]. To overexpress Nup153-mCherry during investi.
การแปล กรุณารอสักครู่..

The present study showed that the nuclear re-localization
of 3CD and 3C0 could be induced by 2Apro alone. It is
reported. That 3CD and 3C0 of poliovirus have nuclear localization
signal which only, functions under poliovirus infection
[4]. Previously. Studies have indicated that NPCs were
altered during poliovirus infection [,] and 15 26 this could
.Not be simply explained as virus-induced leakiness of the
NE because some functions of cellular NPCs remained
[26]. The. Degradation, of Nup98 Nup153 and p62, by
2Apro has also been reported as important for poliovirus
infection [,]. It 26 27. Is likely that NPCs are altered by 2Apro
and then induce the re-localization of 3CD and 3C0 to the
cell nucleus. A variety. Of nucleo-cytoplasmic trafficking
.Pathways are inhibited in poliovirus-infected cells such as
importin A / B and transportin which are, the targets of the
SV40. Large T antigen and heterogeneous, nuclear ribonucleoprotein
respectively. However the transportation, of
some other proteins. That use the transportin-serine /
arginine-rich (SR), pathway such as the SR, protein SC35
is not affected by poliovirus. Infection [26]. The
.Re-localization of 3CD and 3C0
, therefore may be, involved
in a special cytoplasmic - nucleic pathway that is induced
during. Poliovirus infection or 2Apro expression. Further
studies should be dedicated to determine the pathway used
by poliovirus. 3CD and 3C0 to enter the nucleus.
Poliovirus 2Apro can cleave the eIF4G directly or
indirectly and suppress the cap-dependent. 28 29 translation
[,].To overexpress Nup153-mCherry during investi.
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