pbio.3002544.s007.pdf (533.06 kB)
RIG-I interactions with unanchored Ub are not affected by the compounds.
journal contribution
posted on 2024-02-29, 18:53 authored by Carlos A. Rodríguez-Salazar, Sarah van Tol, Olivier Mailhot, Maria Gonzalez-Orozco, Gabriel T. Galdino, Abbey N. Warren, Natalia Teruel, Padmanava Behera, Kazi Sabrina Afreen, Lihong Zhang, Terry L. Juelich, Jennifer K. Smith, María Inés Zylber, Alexander N. Freiberg, Rafael J. Najmanovich, Maria I. Giraldo, Ricardo RajsbaumHEK293T cells were transfected with FLAG-VP35 or FLAG-RIG-I. After lysis, FLAG immunoprecipitations were performed to isolate RIG-I and VP35, followed by incubation with purified K63-linked polyUb chains [2–12], in the presence of 200 μm or pCEBS or SFC, or DMSO as control.
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xlink "> ebolavirususing computational methodshighly pathogenic virusescompounds reduced replicationalso interact nonub interacting surfaceub ); howeverviral polymerase complexreduced vp35 associationinterferon antagonist vp35covalent interacting complexlinked polyub chainsebov replication requiresub interactions leadingdiminished polymerase activitypolymerase complexub nonregulating interactionsdiscovered compoundscovalent ubiquitinationvp35 interactsblock vp35usp5 ),unanchored polyububiquitin chainstested mutationspromising antipreviously showednovel rolemouse modelminigenome assayinfectious ebovectopic expression
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