L2, the minor capsid protein of papillomavirus

Joshua W. Wang, Richard B.S. Roden

Research output: Contribution to journalArticlepeer-review

116 Scopus citations


The capsid protein L2 plays major roles in both papillomavirus assembly and the infectious process. While L1 forms the majority of the capsid and can self-assemble into empty virus-like particles (VLPs), L2 is a minor capsid component and lacks the capacity to form VLPs. However, L2 co-assembles with L1 into VLPs, enhancing their assembly. L2 also facilitates encapsidation of the ~8. kbp circular and nucleosome-bound viral genome during assembly of the non-enveloped T=7. d virions in the nucleus of terminally differentiated epithelial cells, although, like L1, L2 is not detectably expressed in infected basal cells. With respect to infection, L2 is not required for particles to bind to and enter cells. However L2 must be cleaved by furin for endosome escape. L2 then travels with the viral genome to the nucleus, wherein it accumulates at ND-10 domains. Here, we provide an overview of the biology of L2.

Original languageEnglish (US)
Pages (from-to)175-186
Number of pages12
Issue number1-2
StatePublished - Oct 2013


  • Daxx
  • E2
  • Encapsidation
  • Furin
  • HPV
  • Infection
  • L1
  • L2
  • Minor capsid protein
  • ND-10
  • Papillomavirus
  • SP100

ASJC Scopus subject areas

  • Virology


Dive into the research topics of 'L2, the minor capsid protein of papillomavirus'. Together they form a unique fingerprint.

Cite this