Human papillomavirus type 52 L1 major capsid protein (HPV52 L1)

The **Human papillomavirus type 52 L1 major capsid protein** (HPV52 L1) is the principal structural protein forming the icosahedral shell (capsid) of HPV52 virions. This protein, ~55 kDa, is highly conserved among papillomaviruses and can self-assemble into pentameric capsomers, ultimately organizing into a T=7 icosahedral capsid approximately 50-55 nm in diameter[1][6]. L1 mediates initial viral attachment to host cells by recognizing heparan sulfate proteoglycans and related receptors, enabling viral entry[4]. During viral assembly, L1 encapsulates the ~8 kb viral genome and undergoes conformational maturation steps essential for virion stability and infectivity[2][1]. In immunization, recombinant L1 forms virus-like particles (VLPs), which are the immunogenic basis for current prophylactic HPV vaccines that prevent persistent infection and reduce HPV-related cancer risk by inducing neutralizing antibodies[2][5]. L1 is highly immunogenic but is not an enzyme or receptor in the classic sense, rather functioning as a key structural and antigenic element of the viral particle[2][6]. There are no small-molecule drugs targeting L1, but L1-based VLP vaccines are a major breakthrough in HPV disease prevention.

Other names

Major capsid protein L1 (HPV-52)L1 protein (HPV 52)HPV52 L1

Elicits production of neutralizing antibodies that block viral entry (for VLP vaccines based on L1) Inhibits infection by immunogenic mimicry of natural viral particles