Detection Methods for Foodborne Viruses: Current State-of-Art and Future Perspectives.

Foodborne viruses have been recognized as important threats to food safety and human health. Rapid and accurate detection is one of the most crucial measures for food safety control. With the development of biology, chemistry, nanoscience, and related interdisciplines, detection strategies have been devised and advanced continuously. This review mainly focuses on the progress of detection methods for foodborne viruses. The current detection methods for foodborne viruses are summarized, including traditional electron microscopy and cultural isolation, immunoassay, molecular technology, biosensors, and newly emerging CRISPR/Cas-based detection technology. Furthermore, a comparison of the detection methods was objectively discussed. This review provides a comprehensive account of foodborne virus detection methods from fundamentals to state-of-the-art and illustrates the advantages and disadvantages of the current methods and proposes the future trends and directions for foodborne virus detection. It is hoped that this review can update current knowledge and present blueprints in order to accelerate futuristic development.

The Ubiquitin Ligase RNF125 Targets Innate Immune Adaptor Protein TRIM14 for Ubiquitination and Degradation.

Tripartite motif-containing 14 (TRIM14) is a mitochondrial adaptor that facilitates innate immune signaling. Upon virus infection, the expression of TRIM14 is significantly induced, which stimulates the production of type-I IFNs and proinflammatory cytokines. As excessive immune responses lead to harmful consequences, TRIM14-mediated signaling needs to be tightly balanced. In this study, we identify really interesting new gene-type zinc finger protein 125 (RNF125) as a negative regulator of TRIM14 in the innate antiviral immune response. Overexpression of RNF125 inhibits TRIM14-mediated antiviral response, whereas knockdown of RNF125 has the opposite effect. RNF125 interacts with TRIM14 and acts as an E3 ubiquitin ligase that catalyzes TRIM14 ubiquitination. RNF125 promotes K48-linked polyubiquitination of TRIM14 and mediates its degradation via the ubiquitin-proteasome pathway. Consequently, wild-type mouse embryonic fibroblasts show significantly reduced TRIM14 protein levels in late time points of viral infection, whereas TRIM14 protein is retained in RNF125-deficient mouse embryonic fibroblasts. Collectively, our data suggest that RNF125 plays a new role in innate immune response by regulating TRIM14 ubiquitination and degradation.