Human papillomavirus type 6 capsid protein (HPV6 L1 (major), HPV6 L2 (minor); capsid protein collectively ("HPV6 L1/L2"))

The Human papillomavirus type 6 capsid protein encompasses two main viral proteins, L1 (major) and L2 (minor), which together form the icosahedral shell of HPV6 virions. L1 can self-assemble into virus-like particles and serves as the principal target for neutralizing antibodies generated by prophylactic HPV vaccines. These proteins mediate attachment and entry into host epithelial cells by binding to cell surface receptors such as heparan sulfate proteoglycans and potentially α6 integrins. Detection of the L1 and L2 proteins in epithelial cells is indicative of an ongoing productive infection, and their controlled expression by the virus allows immune evasion. Therapeutically, the capsid proteins—primarily L1—are exploited in licensed HPV vaccines for their ability to elicit robust, protective antibody responses, markedly reducing the incidence of HPV6-associated diseases such as genital warts. While rarely associated with cancer, HPV6 infection can cause significant benign disease, making its capsid proteins clinically relevant antiviral and diagnostic targets[1][2][3][5][6][7].

Other names

HPV6 L1 protein (major capsid protein)HPV6 L2 protein (minor capsid protein)HPV6 capsid proteinHPV type 6 L1HPV type 6 L2

Vaccines: Induction of neutralizing antibodies against L1 protein, blocking viral entry[3][5] - Experimental: Antibody-based neutralization