Human adenovirus C serotype 5 hexon protein (HAdV-5 hexon)

The Human adenovirus C serotype 5 (HAdV-5) hexon protein is the major structural component of the viral capsid, which is composed of 240 hexon trimers that form the icosahedral shell. In addition to its structural role, the hexon protein is critical for viral entry and intracellular trafficking, interacting with host dynein for microtubule-dependent transport to the nucleus and with lactoferrin for entry into respiratory epithelial cells. In the field of gene therapy and vaccinology, the hexon protein is a central target for engineering because it is the primary site for neutralizing antibody binding and the driver of natural liver tropism. This tropism is mediated by the high-affinity binding of blood coagulation factor X (FX) to the hexon's hypervariable regions (HVRs), which facilitates hepatocyte transduction and shields the virus from innate immune detection. Therapeutic strategies often involve the modification or 'detargeting' of these HVRs to evade pre-existing immunity and reduce off-target liver toxicity in adenovirus-based vectors.

Other names

Protein IIMajor capsid proteinL3 proteinAd5 hexon

Neutralization of viral infection through hypervariable region binding; manipulation of viral tropism by inhibiting Factor X-mediated hepatocyte binding.