Major capsid protein L1 of Human papillomavirus type 16 and Major capsid protein L1 of Human papillomavirus type 18 (L1 protein (HPV16); L1 protein (HPV18))

The Major capsid protein L1 of Human papillomavirus types 16 and 18 is a ~55 kDa structural protein that self-assembles into pentameric capsomers, forming 72 knobs on the virus surface and constituting about 90% of the viral protein mass[1][2][7]. L1 is responsible for encapsidating the viral DNA, mediating attachment to host cell receptors (including heparan sulfate proteoglycans), and undergoing conformational changes needed for viral entry and DNA release[1][4][7]. Recombinant L1 proteins are used to produce virus-like particles (VLPs) that are the immunogenic basis of current HPV vaccines, eliciting strong and highly type-specific neutralizing antibody responses that block infection[2][3][5][8]. L1 protein's surface loops harbor neutralizing epitopes and are targets for monoclonal antibody-based protection or detection[2][5][8]. HPV16 and HPV18 are high-risk types associated with most cervical and anogenital cancers; targeting their L1 protein prevents infection and associated malignancies[1][5].

Other names

HPV16 L1 proteinHPV18 L1 proteinHuman papillomavirus major capsid protein L1HPV L1 protein

Induction of neutralizing antibodies that block virus attachment and entry; Formation of virus-like particles (VLPs); these structurally mimic the natural virus and trigger immune protection