The papillomavirus major capsid protein L1

Virology. 2013 Oct;445(1-2):169-74. doi: 10.1016/j.virol.2013.05.038. Epub 2013 Jun 22.


The elegant icosahedral surface of the papillomavirus virion is formed by a single protein called L1. Recombinant L1 proteins can spontaneously self-assemble into a highly immunogenic structure that closely mimics the natural surface of native papillomavirus virions. This has served as the basis for two highly successful vaccines against cancer-causing human papillomaviruses (HPVs). During the viral life cycle, the capsid must undergo a variety of conformational changes, allowing key functions including the encapsidation of the ~8 kb viral genomic DNA, maturation into a more stable state to survive transit between hosts, mediating attachment to new host cells, and finally releasing the viral DNA into the newly infected host cell. This brief review focuses on conserved sequence and structural features that underlie the functions of this remarkable protein.

Keywords: HPV; HPV16; L2; Maturation; Papillomaviridae; Virion.

Publication types

  • Research Support, N.I.H., Intramural
  • Review

MeSH terms

  • Amino Acid Sequence
  • Capsid Proteins / genetics
  • Capsid Proteins / metabolism*
  • Conserved Sequence
  • Genes, Viral*
  • Heparan Sulfate Proteoglycans / metabolism
  • Human papillomavirus 16 / genetics
  • Human papillomavirus 16 / metabolism*
  • Human papillomavirus 16 / physiology
  • Humans
  • Oncogene Proteins, Viral / genetics
  • Oncogene Proteins, Viral / metabolism*
  • Protein Folding
  • Protein Interaction Mapping
  • Virus Assembly
  • Virus Internalization


  • Capsid Proteins
  • Heparan Sulfate Proteoglycans
  • L2 protein, Human papillomavirus type 16
  • Oncogene Proteins, Viral
  • L1 protein, Human papillomavirus type 16