Is chlamydial heat shock protein 60 a risk factor for oncogenesis?

Cell Mol Life Sci. 2005 Jan;62(1):4-9. doi: 10.1007/s00018-004-4367-6.


Heat shock protein 60 (HSP60) plays an important role in the protein folding of prokaryotic and eukaryotic cells. Most of the papers published on chlamydial HSP60 concern its role in immune response during infection. In the last decade, exposure to Chlamydia trachomatis has been consistently associated with the development of cervical and ovarian cancer. Moreover, it has been suggested that chlamydial HSP60 may have an anti-apoptotic effect during persistent infection. We hypothesize that the accumulation of exogenous chlamydial HSP60 in the cytoplasm of actively replicating eukaryotic cells may interfere with the regulation of the apoptotic pathway. The concomitant expression of viral oncoproteins and/or the presence of mutations may lead to the ability to survive apoptotic stimuli, loss of replicative senescence, uncontrolled proliferation and, finally neoplastic transformation.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Apoptosis
  • Bacterial Proteins / metabolism*
  • Cell Transformation, Neoplastic
  • Chaperonin 60 / metabolism*
  • Chlamydia Infections / complications*
  • Chlamydia trachomatis / metabolism*
  • Female
  • Genital Neoplasms, Female / microbiology*
  • Humans
  • Risk Factors


  • Bacterial Proteins
  • Chaperonin 60