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Hepatitis A virus (HAV) antibody is not a therapeutic target; rather, it is an antibody molecule itself, serving as a product of the host's immune system or as a therapeutic agent when administered exogenously. These antibodies are generated by the immune system in response to HAV infection or vaccination to neutralize and eliminate the virus. When developed as therapeutic agents (e.g., monoclonal antibodies such as R10, F4, F6, F7, and F9), they function by binding to the HAV capsid proteins (VP1, VP2, VP3) and blocking viral attachment to host cell receptors, thereby preventing infection. The actual therapeutic targets for drug development against HAV are the viral capsid proteins themselves (especially at the single conserved antigenic site located on VP2 and VP3) or the host cell receptor, T-cell immunoglobulin and mucin domain 1 (TIM-1), which HAV utilizes for cellular entry.
As an immune molecule or therapeutic agent, it binds to specific epitopes on the HAV capsid proteins (e.g., VP1, VP2, VP3), which are located at the viral surface. This binding blocks the virus's ability to attach to host cell receptors, particularly T-cell immunoglobulin and mucin domain 1 (TIM-1), thereby preventing cellular entry and neutralizing the infection.
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