Ddx23, also known as PRP28, is a spliceosomal RNA helicase. It is crucial for pre-mRNA splicing, specifically for the pre-B to B spliceosome complex transition and release of U1 snRNP from the 5' splice site [1]. It also participates in maintaining genome stability and sensing double-stranded RNA. Moreover, Ddx23 is involved in multiple biological processes such as the innate immune response, and its functions are essential for normal cellular activities [2,3,6].

In black carp, bcDDX23 targets bcMAVS and suppresses MAVS-mediated IFN signaling, indicating its role in antiviral innate immunity [2]. In human cells, knockdown of DDX23 enhanced the replication of VSV and reduced the activation of the NF-κB and IRF3, suggesting its importance in the innate antiviral response [3]. In ovarian cancer, DDX23 was upregulated, and its silencing impeded cell proliferation/invasion in vitro and tumor growth in vivo, regulating the mRNA processing of FOXM1 [5]. In addition, in the context of foot-and-mouth disease virus, DDX23 negatively affects virus IRES-dependent translation [4].

In summary, Ddx23 plays essential roles in pre-mRNA splicing, innate immune responses, and in certain disease conditions such as ovarian cancer and viral infections. Functional studies, including those using knockdown models, have revealed its importance in regulating biological processes and its potential as a target for antiviral drugs and cancer therapies [2,3,4,5].