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. 2022 Mar 8;38(10):110434. doi: 10.1016/j.celrep.2022.110434

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© 2022 The Authors

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DHX16 interacts with unanchored Ub and RNA to promote IFN-I production

(A) The IsoT de-ubiquitination assay.

(B) De-coupling of unanchored K48-poly-Ub from DHX16 following co-expression of IsoT in HEK293Ts (coIP).

(C) IFN-β expression following co-expression of DHX16 and IsoT in HEK293Ts infected with IAV for 24 h (PR8 MOI = 0.1) (qRT-PCR).

(D) In vitro interactions between DHX16 and RIG-I ± recombinant poly-Ub chains (coIP).

(E) Effects of recombinant poly-Ub (1 μg) and purified IAV vRNA (100 ng) on DHX16 ATPase activity in an in vitro ATPase assay.

(F) Interaction between DHX16 and unanchored K48-poly-Ub following co-expression in HEK293Ts in the presence of RNase A (100 μg/mL) (coIP).

(G) Immunoblot quantification of K48-Ub in (F) (densitometry).

(H) Interactions between DHX16 and RIG-I following co-expression in HEK293Ts in the presence of RNase A (0–100 μg/mL) (coIP).

(I) DHX16-RIG-I complex formation mediated through vRNA and unanchored poly-Ub.

Data are expressed as means (n = 3) ± SD. ^∗p < 0.05; ^∗∗p < 0.01; ^∗∗∗p < 0.001 (one-way ANOVA with Tukey's multiple comparisons). Data are representative of 2–3 independent experiments.