Human papillomavirus type 16 L1 capsid protein – host cell surface receptor interface (HPV-16 L1-receptor interface) (HPV-16 L1-receptor interface)

The Human papillomavirus type 16 (HPV-16) L1 capsid protein – host cell surface receptor interface is the critical site for the initiation of viral infection in basal epithelial cells. The L1 protein, the major structural component of the HPV capsid, mediates initial attachment by binding to heparan sulfate proteoglycans (HSPGs) on the basement membrane or cell surface (Day et al., 2003, PMID: 11448163). This interaction induces conformational changes in the capsid, allowing the virus to engage secondary receptors such as alpha-6 integrin or the tetraspanin CD151 for internalization (Schelhaas et al., 2012, PMID: 22511868). This interface is the primary target for prophylactic vaccines like Gardasil 9 and Cervarix, which elicit neutralizing antibodies that bind to L1 and sterically block its interaction with host receptors (Schiller & Lowy, 2012, PMID: 22941505). By preventing this initial binding event, the vaccines effectively neutralize the virus before it can enter the host cell. Beyond vaccines, this interface is also a target for experimental entry inhibitors like carrageenan, which mimic HSPGs to competitively inhibit viral attachment (Buck et al., 2006, PMID: 16835347). Understanding the structural dynamics of this interface is essential for developing next-generation therapeutics against HPV-16, a leading cause of cervical and oropharyngeal cancers.

Other names

HPV16 L1-HSPG interfaceHPV16 L1-heparan sulfate proteoglycan interfaceHPV16 L1-alpha-6 integrin interfaceHPV16 L1-CD151 interfaceHPV16 L1-receptor complex

Neutralization of viral particles by antibodies to prevent binding to host cell receptors (Schiller & Lowy, 2012, PMID: 22941505); competitive inhibition of viral attachment to heparan sulfate proteoglycans (HSPGs) (Buck et al., 2006, PMID: 16835347).