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The copyright holder for this preprint (which was not peer-reviewed) is the author/funder.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 enhancement (83). Thus, it cannot be excluded that the deficient trimerization of VP7 is due 420 to altered calcium homeostasis. The catalytically inactive mutants of GBF1 (GBF1/795/E794K and GBF1/795/7A) failed to 436 support replication of the virus, suggesting that GBF1 activity is essential for rotavirus 437 progeny production. Although the catalytic activity of GBF1 appears essential for rotavirus 438 replication, we found that the activation of Arf1 is not required, since knocking-down the 439 expression of this factor does not affect the production of infectious virus. Thus, it is likely 440 that rotavirus replication requires the activation of other GBF1 substrates, such as Arf4 or 441 All rights reserved. No reuse allowed without permission.