Heat shock proteins and infection: interactions of pathogen and host.
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.
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Medical Research Council Tuberculosis and Related Infections Unit, Hammersmith Hospital, London, England.
D000818:Animals; D006360:Heat-Shock Proteins / Q000096:biosynthesis*; D006801:Humans; D007239:Infections / Q000378:metabolism*; D010587:Phagocytosis; D016897:Respiratory Burst
D006360:Heat-Shock Proteins