Human papillomavirus type 18 major capsid protein L1[4] (HPV18 L1[1][4])

Human papillomavirus type 18 major capsid protein L1 is the principal structural protein that self-assembles into 72 pentameric capsomeres forming an icosahedral T=7 capsid of approximately 50 nm, stabilized by inter-capsomer disulfide bonds.[1][4] L1 VLPs are highly immunogenic and constitute the antigenic basis of current prophylactic HPV vaccines, eliciting neutralizing antibodies against conformational epitopes on assembled capsomeres.[1] Conserved features of L1 mediate initial cell attachment during infection, and a subset of L1 can remain associated with L2 and viral DNA during trafficking to the nucleus, likely as pentamers retaining conformation-dependent epitopes.[1][2] Structural compatibility between L1 and L2 is type dependent; specific N-terminal domains in HPV18 L1 influence cooperation with L2 to form infectious virions, highlighting interdependence of capsid proteins.[3] UniProt annotates HPV18 L1 as forming a T=7 icosahedral capsid composed of 72 disulfide-linked pentamers.[4]

Other names

L1 major capsid protein[1][4]HPV-18 L1[4]Major capsid protein L1 of HPV18[4]

Vaccine-induced neutralizing antibodies recognize conformational epitopes on assembled L1 capsomeres/VLPs, blocking virion attachment/entry and preventing infection.[1][2]