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The adenovirus hexon protein is the major capsid protein forming 240 homotrimeric hexon capsomeres that constitute over 80% of the icosahedral capsid structure in non-enveloped dsDNA adenoviruses, providing stability and protection to the virion. Each hexon trimer features a pseudo-hexagonal base of double jelly-roll β-barrels and a triangular top with extended insertion loops exposed on the virus surface, containing type-specific neutralizing epitopes. It requires viral chaperone 100K for proper folding, trimerization, and prevention of aggregation. In human adenovirus species D types like HAdV-D56, hexon directly binds host receptor CD46 in the central cavity of trimers to mediate cell entry, and interacts with nuclear pore complexes for DNA import. The protein comprises ~950-970 amino acids, with conserved core regions for capsid formation and hypervariable loops for serotype specificity.
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