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The Human papillomavirus type 58 (HPV58) major capsid protein L1 is the primary structural component of the HPV58 virion, a high-risk genotype frequently associated with cervical cancer, particularly in East Asia [1, 11]. This protein has the intrinsic ability to self-assemble into virus-like particles (VLPs) that are morphologically and immunologically similar to the native virus but lack the viral genome [4, 11]. Biologically, the L1 protein mediates the initial attachment of the virus to host cell heparan sulfate proteoglycans, triggering conformational changes that allow for viral entry via endocytosis [1, 9]. During the viral life cycle, it also plays a crucial role in encapsidating the viral DNA and facilitating its release into the host nucleus [1, 4]. In the context of therapeutics, HPV58 L1 is a critical antigen in the 9-valent HPV vaccine (Gardasil 9), which induces the production of neutralizing antibodies that prevent viral infection [2, 16]. These antibodies block the interaction between the L1 protein and host receptors, thereby neutralizing the virus before it can infect keratinocytes [16]. Furthermore, the presence or absence of L1 protein expression in clinical samples serves as a significant biomarker; the loss of L1 expression is often correlated with the progression of cervical lesions to high-grade intraepithelial neoplasia and invasive cancer [12, 13]. Prophylactic vaccination targeting this protein remains the most effective strategy for preventing HPV58-related malignancies [11].
Induction of neutralizing antibodies that bind to the L1 protein, blocking viral attachment to host cell heparan sulfate proteoglycans and preventing viral entry.
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