Vaccinia virus A27L protein (A27L)

The Vaccinia virus A27L protein is a 110-amino-acid viral envelope protein conserved in the Orthopoxvirus genus, located on the surface of intracellular mature virions. It comprises a heparin-binding domain (residues 21-34), coiled-coil domain (residues 43-84) for oligomerization, and leucine zipper domain for A17 binding. The protein forms trimers as basic units that stack into hexamers via N-terminal and C-terminal interfaces, critical for self-assembly, disulfide-linked complex formation with A26, and biological functions including heparan sulfate binding for cell attachment, A26 packaging, mature virus egress, and modulation of plasma membrane fusion during entry. Mutations disrupting oligomerization impair plaque formation, virus egress, and A26 interaction, leading to increased fusion activity. As a neutralizing antibody target, its structure supports inhibitor development against poxvirus infection.

Other names

A27 proteinA2714-kilodalton fusion protein