Major capsid protein L1 (Human papillomavirus 33) (HPV 33 L1)

The HPV type 33 L1 major capsid protein is the primary structural component of the Human Papillomavirus type 33 virion, a high-risk genotype associated with cervical, vulvar, and oropharyngeal cancers (Sino Biological; NIH). This protein has the unique ability to self-assemble into icosahedral virus-like particles (VLPs) composed of 72 pentamers, which are immunologically indistinguishable from the native virus (ResearchGate; NIH). Biologically, the L1 protein mediates the initial attachment of the virus to heparan sulfate proteoglycans on the surface of host keratinocytes, triggering conformational changes that facilitate viral entry via endocytosis (UniProt P06416). During the infection process, L1 also plays a role in encapsidating the viral DNA and stabilizing the virion for transmission between hosts (Journal of Virology; UniProt P06416). Because it contains the major neutralizing epitopes, the L1 protein is the central component of prophylactic vaccines like Gardasil 9 (NIH). These vaccines work by inducing high titers of type-specific neutralizing antibodies that block the virus from infecting host cells (Sino Biological; NIH). Targeting the L1 protein is a highly effective strategy for preventing persistent HPV 33 infection and its progression to malignancy (NIH).

Other names

L1 proteinMajor capsid protein L1HPV33 L1Late protein L1

Prophylactic immunization through the induction of neutralizing antibodies that prevent viral attachment and entry