RT Journal Article
ID 76d273ac504e7c32
A1 Piraino, Frank F.
A1 Liu, Xuyang 
T1 Implication of ICP0 Translocation and Peroxisome Functions in the Inhibition of HSV-1 by the Antiviral Protein RC28 from the Higher Basidiomycetes Mushroom <i>Rozites caperata</i>
JF International Journal of Medicinal Mushrooms
JO IJM
YR 2014
FD 2014-10-13
VO 16
IS 6
SP 509
OP 517
K1 Medicinal mushrooms
K1 <i>Rozites caperata</i>
K1 HSV-1 strain KOS
K1 HSV-2
K1 ICP0 (HSV-1 infected-cell protein 0)
K1 ICPO translocation
K1 peroxisomes
K1 PPAR receptors (peroxisome proliferator nuclear receptors)
K1 PPAR receptor
AB RC28 an antiviral protein of MW 28.25 kD isolated from the edible mushroom <i>Rozites caperata</i> (RC) (<i>&#61;Cortinarius caperatus</i>), was tested for its ability to block HSV-1 functions. The protein blocked the translocation of the immediate early protein ICP0 from the nucleus to the cytoplasm. Target studies using an array of yeast proteins revealed that the protein binds preferentially to some yeast peroxisome proteins. An antagonist of the peroxisome proliferator nuclear receptor complex (PPAR) &#91;2-chloro-5-nitro-(N-pyridyl) benzamide (MW 277.7)&#93; was inhibitory to both HSV-1 and HSV-2 at EC<sub>50</sub> values of 5.8 and 10 &#181;M, respectively. Prevention of the cytoplasmic functions of ICP0 and perturbations of peroxisomal metabolism utilized by HSV-1 are likely antiviral targets of the mushroom protein.
PB Begell House
LK https://www.dl.begellhouse.com/journals/708ae68d64b17c52,077f1bbb3fcde585,76d273ac504e7c32.html