Experientia

, Volume 48, Issue 7, pp 635–639

Heat shock proteins and infection: Interactions of pathogen and host

  • T. R. Garbe
Multi-Author Reviews Heat Shock Proteins

DOI: 10.1007/BF02118308

Cite this article as:
Garbe, T.R. Experientia (1992) 48: 635. doi:10.1007/BF02118308

Abstract

Invasive microorganisms encounter defensive attempts of the host to starve, destroy and eliminate the infection. In experimental model systems aiming to imitate defensive actions of the host, microorganisms respond by the rapid acceleration in the rate of expression of heat shock and other stress proteins. Heat shock proteins (hsp) of most if not all pathogens are major immune targets for both B- and T-cells. Host cells involved in the defensive action cannot avoid exposure to their own reactive compounds, such as oxygen radicals, resulting in premature cell death and tissue damage. Long-term consequences to the host may include cancer. In cells in tissue culture, induction of host-specific hsps occurs upon exposure to oxidants and in viral infections. Drugs that bind to members of the hsp70 family induce peroxisome proliferation and hepatocarcinoma, but may open the way for the development of novel drugs in support of antimetabolite treatment of infections and cancer.

Key words

Nutrient withholdingphagocytesoxidantscancerperoxisome proliferators

Copyright information

© Birkhäuser Verlag 1992

Authors and Affiliations

  • T. R. Garbe
    • 1
  1. 1.Medical Research Council Tuberculosis and Related Infections UnitHammersmith HospitalLondonEngland