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The Human papillomavirus type 58 major capsid protein L1 is the primary structural protein forming the icosahedral capsid of the HPV58 virion. The capsid is constructed from 72 L1 pentamers linked by disulfide bonds, encapsidating the circular double-stranded viral DNA[7][8]. L1 self-assembles to create virus-like particles (VLPs) that are highly immunogenic, forming the basis for current prophylactic HPV vaccines, which include HPV58 as a covered genotype in the 9-valent formulation[2][5]. L1 mediates the first steps of infection through attachment of the virion to cell surface components of epithelial target cells, followed by conformational changes that expose or release the minor capsid protein L2 and allow genome delivery[2][4]. Antibodies targeting surface-exposed conformational epitopes of L1 efficiently neutralize viral entry, thereby preventing infection[2][3][4]. No small molecule inhibitors are known to interact with L1, but monoclonal neutralizing antibodies and vaccines based on L1 play a critical role in infection control and prevention[2][4].
Neutralizing antibodies block virion attachment and entry by targeting conformational epitopes on L1
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