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The human papillomavirus type 31 major capsid protein L1 is a structural protein that constitutes the majority of the viral capsid. It forms 72 pentameric capsomeres, making up the icosahedral shell that encapsulates the viral genome[4][5]. L1 is essential for viral infectivity: it mediates attachment to host cells by binding to heparan sulfate proteoglycans or integrins on the cell surface[2][5]. During infection, these interactions enable viral entry and genetic material delivery to the nucleus. L1 is highly immunogenic and serves as the target for neutralizing antibodies; consequently, it is the basis for the virus-like particle (VLP) vaccines used in HPV immunization[1][3][5]. Variability in L1 can affect, but generally does not compromise, the efficacy of neutralizing antibodies and vaccines across HPV31 strains[1]. The main biological functions of L1 include capsid assembly, facilitating viral entry, and triggering immune responses. In diagnostic and vaccine contexts, L1 detection or antibodies to L1 serve as biomarkers of infection or immunization status. As a critical structural component in HPV infection and immune targeting, L1 is both a marker and a therapeutic target for infection prevention.
Induction of neutralizing antibodies (for vaccines, VLPs trigger the immune system to produce antibodies that prevent viral infection by blocking attachment and entry into host cells)[1][3][5].
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