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The adenoviral capsid surface is a complex, non-enveloped icosahedral structure primarily composed of three major proteins: hexon, penton base, and fiber [1]. It serves as the critical interface between the virus and the host, mediating initial attachment to cellular receptors such as the Coxsackievirus and Adenovirus Receptor (CAR) and facilitating subsequent internalization and endosomal escape [2]. In clinical contexts, the capsid is the primary target for the host's neutralizing antibody response, which can limit the effectiveness of adenoviral vectors used in gene therapy and vaccines [3]. Therapeutic approaches targeting the capsid include the administration of intravenous immunoglobulins for passive immunity and the development of engineered "stealth" capsids that evade immune detection [4]. Additionally, the capsid's structural proteins are targets for experimental small molecules and monoclonal antibodies designed to inhibit viral uncoating or block cell entry [5]. Understanding the molecular architecture of the capsid surface is essential for both treating natural infections and optimizing adenovirus-based delivery systems [6].
Neutralization of viral infectivity by blocking receptor binding sites or preventing the conformational changes required for endosomal escape and uncoating.
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