Additional file 7: figure S7. of Biochemical and biophysical characterization of cell-free synthesized Rift Valley fever virus nucleoprotein capsids enables in vitro screening to identify novel antivirals

Autor: Broce, Sean, Hensley, Lisa, Tomoharu Sato, Lehrer-Graiwer, Joshua, Essrich, Christian, Edwards, Katie, Pajda, Jacqueline, Davis, Christopher, Bhadresh, Rami, Hurt, Clarence, Freeman, Beverly, Vishwanath Lingappa, Kelleher, Colm, Karpuj, Marcela
Rok vydání: 2016
DOI: 10.6084/m9.figshare.c.3611000_d6
Popis: Conversion of the IOAS into IHOS by nonradioactive CFPS-products is not affected by Apyrase. Glycerol-gradient fractionation profiles of the radioactive material generated in CFPs under conditions favoring intermediate-assembly structures and “chased” by the addition of nonradioactive products for 120 min and carried out in the presence or absence of the ATP inhibitor Apyrase (final concentration of 0.5 U/μl in the cell-free reaction mixture) at 37 °C. Note that in all cases, in addition to the chase at 26 °°C, the material in peak I (intermediate assembly structures) was converted to the highly ordered assembly structures (Peak II), indicating that the process of RVFV NP assembly is indeed independent of energy but is temperature dependent. (PDF 88 kb)
Databáze: OpenAIRE