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The adenoviral capsid is a complex, non-enveloped icosahedral structure (approximately 90 nm in diameter) primarily composed of three major proteins: hexon, penton base, and fiber [1][2]. Its primary biological role is to protect the double-stranded DNA genome and facilitate delivery into host cells by binding to specific receptors, such as the Coxsackievirus and Adenovirus Receptor (CAR), CD46, or sialic acids, depending on the serotype [2]. In the context of infectious disease, the capsid is the primary target for the host immune system, and its structural proteins—particularly the hexon—are the focus of diagnostic assays and vaccine development [3]. Furthermore, the adenoviral capsid is extensively utilized in biotechnology as a delivery vehicle for gene therapy and vaccines, where its ability to efficiently enter cells is leveraged [3]. However, therapeutic challenges arise from pre-existing immunity in the human population, which can neutralize the capsid before it reaches its target, and the potential for severe inflammatory responses or liver sequestration [4]. Current pharmacological strategies include the use of neutralizing antibodies (e.g., in IVIG) and experimental small molecules or peptides designed to block viral attachment or uncoating [1][4]. Sources: [1] Nemerow, G. R., et al. (2009). Current Opinion in Virology; [2] Russell, W. C. (2009). Journal of General Virology; [3] Wold, W. S., & Toth, K. (2013). Current Gene Therapy; [4] Lion, T. (2014). Clinical Microbiology Reviews.
Neutralization of viral particles to prevent host cell attachment and inhibition of endosomal escape.
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