BodyText2
In the teams latest work, they reveal structural features of
the viruss coiled protein shell, or nucleocapsid, that may be
promising therapeutic targets, more easily destabilized and knocked out
by an antiviral treatment.
The research is highlighted in the Tuesday, Oct. 20 issue of the Journal of Chemical Physics,
which is published by the American Institute of Physics, a federation
of societies in the physical sciences representing more than 120,000
members.
The Ebola nucleocapsid looks like a
Slinky walking spring, whose neighboring rings are connected, Perilla
said. We tried to find what factors control the stability of this
spring in our computer simulations.
The life cycle of Ebola is highly dependent on this coiled
nucleocapsid, which surrounds the viruss genetic material consisting of
a single strand of ribonucleic acid (ssRNA). Nucleoproteins protect
this RNA from being recognized by cellular defense mechanisms. Through
interactions with different viral proteins, such as VP24 and VP30, these
nucleoproteins form a minimal functional unit a copy machine for
viral transcription and replication.
While nucleoproteins are important to the nucleocapsids stability,
the teams most surprising finding, Perilla said, is that in the absence
of single-stranded RNA, the nucleocapsid quickly becomes disordered.