CUL4A (Human-Hepadnavirus)¶

Figure Legend: HBV-HBX Inhibition of SMC5/6 via DDB1/CUL4A Ubiquitin Ligase Pathway

This diagram illustrates how the Hepatitis B Virus (HBV) X protein (HBX) disrupts host antiviral mechanisms. Within the nucleus of a human hepatocyte, HBX functions as an adaptor that recruits the host's DDB1 protein. DDB1 binds to CUL4A, which activates RBX1, forming a complete ubiquitin ligase complex. This complex targets the SMC5/6 DNA repair complex (consisting of SMC5 and SMC6 proteins) for ubiquitination and subsequent degradation. By eliminating SMC5/6, which normally acts as a restriction factor against viral DNA, HBV enhances its genome replication and persistence in infected cells. This mechanism represents a key viral strategy to evade host defense mechanisms and promote HBV pathogenesis.

Feedback from AI on figure:

{"feedback":"The diagram effectively communicates the HBV-HBX inhibition pathway with clear visual hierarchy and organization. The cellular context is well-established with the hepatocyte outline and nuclear boundary. Protein interactions are logically presented with directional flow from the viral HBX protein through the host ubiquitin ligase complex to the targeted SMC5/6 DNA repair proteins. The use of consistent styling, appropriate colors for different protein categories, and well-labeled interactions enhances understanding of the biological process. The inclusion of a concise legend and pathway summary provides essential context for interpreting the diagram.","necessary_changes":null,"optional_changes":null}