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Related Experiment Videos

DNA-induced structural changes in the papillomavirus capsid.

C Fligge1, F Schäfer, H C Selinka

  • 1Institute for Medical Microbiology and Hygiene, University of Mainz, D-55101 Mainz, Germany.

Journal of Virology
|July 20, 2001
PubMed
Summary

Human papillomavirus (HPV) capsid assembly involves disulfide bonds in the major capsid protein L1. Encapsidating DNA into virus-like particles (VLPs) increases L1 cross-linking, similar to natural virions.

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Area of Science:

  • Virology
  • Structural Biology
  • Molecular Biology

Background:

  • Human papillomavirus (HPV) capsid assembly relies on disulfide bonds between major capsid protein L1 molecules.
  • Naturally occurring HPV virions exhibit greater L1 cross-linking than laboratory-generated virus-like particles (VLPs).

Purpose of the Study:

  • To investigate the structural changes in HPV virus-like particles (VLPs) upon DNA encapsidation.
  • To compare the cross-linking of L1 protein in VLPs with and without DNA to that of natural virions.

Main Methods:

  • Generation of HPV virus-like particles (VLPs) in eukaryotic expression systems.
  • Analysis of intercapsomeric disulfide bond formation in L1 protein.
  • Assessment of trypsin resistance as an indicator of capsid stability.

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Main Results:

  • DNA encapsidation into VLPs significantly increased cross-linking of the L1 protein.
  • The degree of L1 cross-linking in DNA-containing VLPs was comparable to that observed in natural HPV virions.
  • VLPs containing DNA showed enhanced trypsin resistance, suggesting tighter capsomere association.

Conclusions:

  • DNA encapsidation is a critical factor in stabilizing the human papillomavirus capsid structure.
  • The presence of DNA induces conformational changes in L1 protein, leading to increased cross-linking and stability.
  • Understanding these structural changes can inform the development of more effective HPV vaccines and antiviral strategies.