As obligate parasites, viruses exploit host cell organelles and molecular components to complete their life cycle. Among which, viruses firstly hijack the cytoskeleton of host cells to ensure their efficiently cell entry and replication. Although formin family members play a key role in both microfilament and microtubule cytoskeletal remodeling, few studies addressed the detailed function and mechanism of formins in the process of viral infection. Here, we showed that sus scrofa DIAPH1 was involved in the regulation of cytoskeletal dynamics during PRV replication. Firstly, we found that DIAPH1 showed significant changes in the expression level and intracellular localization during PRV infection of PK-15 cells. Next, inhibition of DIAPH1 by RNA interference or small molecular inhibitor SMIFH2 was found to diminish the outcome of PRV infection. Besides, DIAPH1 partially co-localized with actin and tubulin in PRV-infected cells. Cross-talk occurred between microfilaments and microfilaments, which also had an influence on the intracellular localization of DIAPH1. What's more, inhibition of DIAPH1 induced the reorganization of microfilament and the stability of microtubule. These results suggested that DIAPH1 regulated PRV infection by remodeling microfilament and microtubule cytoskeletal dynamics.
Keywords: Actin; Cytoskeleton; DIAPH1; Microtubule; Pseudorabivirus replication.
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