The guanine nucleotide exchange factor GBF1 participates in rotavirus replication

José L. Martínez; Francesca Arnoldi; Elisabeth M. Schraner; Catherine Eichwald; Daniela Silva-Ayala; Eunjoo Lee; Elizabeth Sztul; Óscar R. Burrone; Susana López; Carlos F. Arias

The copyright holder for this preprint (which was not peer-reviewed) is the author/funder. . https://doi.org/10.1101/619924 doi: bioRxiv preprint cells, typical electro-dense viroplasm structures were observed near the ER membrane. 195 Furthermore, viral particles, presumably DLPs, appear to be budding into the lumen of the 196 ER leading to the formation of membrane-enveloped particles. Many of the viral particles 197 within the ER seem to have lost their lipid envelope and look like mature TLPs (Fig 4A) . We 198 found that neither BFA nor GCA prevented the budding of DLPs into the ER to form 199 membrane-enveloped particles; however, the assembly pathway seems to be arrested at this The electrophoretic mobility of VP7 and NSP4 is altered during the inhibition of GBF1 206 activity. Since it has been reported that BFA alters the electrophoretic mobility of VP7 and 207 NSP4 (21), we decided to investigate if the effect of GCA in virus assembly was related to a 208 modification of these viral proteins. MA104 cells were infected with RRV in the presence of 209 the inhibitors as described above, and at 7.5 hpi, the cellular proteins were pulse-labeled with The copyright holder for this preprint (which was not peer-reviewed) is the author/funder. . https://doi.org/10.1101/619924 doi: bioRxiv preprint