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The Human papillomavirus type 31 L2 protein is the minor capsid protein of the high-risk HPV31 virus, playing a vital role in the viral life cycle [1, 2]. It is involved in capsid stabilization, facilitating the entry of the virus into host cells, and escorting the viral genome from the endosome to the nucleus [2, 4]. Unlike the major capsid protein L1, L2 contains highly conserved N-terminal epitopes that can elicit cross-neutralizing antibodies against a wide range of HPV types [1, 5]. This makes it a key target for the development of next-generation, broad-spectrum prophylactic vaccines, such as RG1-VLP, which aim to provide protection beyond the types covered by current L1-based vaccines [7, 8]. During infection, L2 interacts with host cellular machinery, including the retromer complex and dynein, to ensure the delivery of the viral DNA to the nucleus [2, 3]. Therapeutic strategies targeting L2 focus on preventing infection and the subsequent development of HPV-associated malignancies, including cervical and oropharyngeal cancers [5, 10].
Induction of cross-neutralizing antibodies that block viral entry or endosomal escape [1, 5].
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