Major capsid protein L1 of Human papillomavirus (L1)

The major capsid protein L1 of Human papillomavirus is a ~55 kDa structural protein that forms the outer shell (capsid) of the virion by assembling into 72 pentameric capsomers with icosahedral symmetry[1][2][4][6][7]. L1 can self-assemble into virus-like particles (VLPs), which are highly immunogenic and serve as the basis for current HPV vaccines[1][4][2]. The surface loops of L1 contain type-specific epitopes that are the primary target for neutralizing antibodies, while highly conserved regions are involved in capsid assembly and genome packaging[2][4]. L1 is expressed late in the viral life cycle, mediates attachment to host cells, and is critical for encapsidating the viral genome before transmission[4][6]. While not an active enzyme or receptor, it is a primary therapeutic target because it elicits strong protective immunity and is the antigenic basis for successful prophylactic vaccines against HPV-related diseases[1][4]. Note: The phrase "L1 protein of Human Papillomavirus types 6, 11, 16, 18, 31, 33, 45, 52, 58" appropriately refers to the L1 proteins of specific HPV types included in current vaccine formulations; each type's L1 is very similar in structure and function but immunologically distinct enough to warrant inclusion in multi-type vaccines. No spelling or conceptual errors are present in the target designation.

Other names

L1 proteinHPV major capsid protein L1

Induction of neutralizing antibodies that prevent viral entry by binding to conformational epitopes on L1; Immune-mediated clearance through vaccine-induced immunity