Structure of small virus-like particles assembled from the L1 protein of human papillomavirus 16

Mol Cell. 2000 Mar;5(3):557-67. doi: 10.1016/s1097-2765(00)80449-9.

Abstract

The papillomavirus major late protein, L1, forms the pentameric assembly unit of the viral shell. Recombinant HPV16 L1 pentamers assemble in vitro into capsid-like structures, and truncation of ten N-terminal residues leads to a homogeneous preparation of 12-pentamer, icosahedral particles. X-ray crystallographic analysis of these particles at 3.5 A resolution shows that L1 closely resembles VP1 from polyomaviruses. Surface loops contain the sites of sequence variation among HPV types and the locations of dominant neutralizing epitopes. The ease with which small virus-like particles may be obtained from L1 expressed in E. coli makes them attractive candidate components of a papillomavirus vaccine. Their crystal structure also provides a starting point for future vaccine design.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Capsid / chemistry
  • Capsid Proteins*
  • Crystallization
  • Crystallography, X-Ray
  • Drug Design
  • Epitopes
  • Models, Molecular
  • Molecular Sequence Data
  • Neutralization Tests
  • Oncogene Proteins, Viral / chemistry*
  • Oncogene Proteins, Viral / immunology
  • Oncogene Proteins, Viral / ultrastructure
  • Papillomaviridae / chemistry*
  • Papillomaviridae / immunology
  • Papillomaviridae / ultrastructure
  • Protein Binding
  • Receptors, Virus
  • Sequence Homology, Amino Acid
  • Viral Vaccines

Substances

  • Capsid Proteins
  • Epitopes
  • Oncogene Proteins, Viral
  • Receptors, Virus
  • VP1 protein, polyomavirus
  • Viral Vaccines
  • L1 protein, Human papillomavirus type 16

Associated data

  • PDB/1DAL