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Heat shock proteins, or stress proteins have been identified as part of a highly conserved cellular defence mechanism mediated by multiple, distinct gene familes and corresponding gene products. As intracellular chaperones, stress proteins participate in many essential biochemical pathways of protein maturation and function active during times of stress and during normal cellular homeostasis. In addition to their well-characterized role as protein chaperones, stress proteins are now realized to possess another important biological property: immunogenicity. Stress proteins are now understood to play a fundamental role in immune surveillance of infection and malignancy and this body of basic research has provided a framework for their clinical application. As key targets of both humoral and cellular immunity during infection, stress proteins have accordingly received considerable research interest as prophylactic vaccines for infectious disease applications. The unique and potent immunostimulatory properties of stress proteins have similarly been applied to the development of new approaches to cancer therapy, including both protein and gene-based modalities. [ABSTRACT FROM AUTHOR]