Book contents
- Frontmatter
- Contents
- Contributors
- Preface
- SECTION 1 MOLECULAR CHAPERONES AND THE CELL STRESS RESPONSE
- SECTION 2 CHANGING PARADIGMS OF PROTEIN TRAFFICKING AND PROTEIN FUNCTION
- SECTION 3 EXTRACELLULAR BIOLOGY OF MOLECULAR CHAPERONES: MOLECULAR CHAPERONES AS CELL REGULATORS
- SECTION 4 EXTRACELLULAR BIOLOGY OF MOLECULAR CHAPERONES: PHYSIOLOGICAL AND PATHOPHYSIOLOGICAL SIGNALS
- SECTION 5 EXTRACELLULAR BIOLOGY OF MOLECULAR CHAPERONES: MOLECULAR CHAPERONES AS THERAPEUTICS
- 15 Neuroendocrine Aspects of the Molecular Chaperones ADNF and ADNP
- 16 Heat Shock Proteins Regulate Inflammation by Both Molecular and Network Cross-Reactivity
- 17 Heat Shock Protein Fusions: A Platform for the Induction of Antigen-Specific Immunity
- 18 Molecular Chaperones as Inducers of Tumour Immunity
- SECTION 6 EXTRACELLULAR BIOLOGY OF MOLECULAR CHAPERONES: WHAT DOES THE FUTURE HOLD?
- Index
- References
17 - Heat Shock Protein Fusions: A Platform for the Induction of Antigen-Specific Immunity
Published online by Cambridge University Press: 10 August 2009
- Frontmatter
- Contents
- Contributors
- Preface
- SECTION 1 MOLECULAR CHAPERONES AND THE CELL STRESS RESPONSE
- SECTION 2 CHANGING PARADIGMS OF PROTEIN TRAFFICKING AND PROTEIN FUNCTION
- SECTION 3 EXTRACELLULAR BIOLOGY OF MOLECULAR CHAPERONES: MOLECULAR CHAPERONES AS CELL REGULATORS
- SECTION 4 EXTRACELLULAR BIOLOGY OF MOLECULAR CHAPERONES: PHYSIOLOGICAL AND PATHOPHYSIOLOGICAL SIGNALS
- SECTION 5 EXTRACELLULAR BIOLOGY OF MOLECULAR CHAPERONES: MOLECULAR CHAPERONES AS THERAPEUTICS
- 15 Neuroendocrine Aspects of the Molecular Chaperones ADNF and ADNP
- 16 Heat Shock Proteins Regulate Inflammation by Both Molecular and Network Cross-Reactivity
- 17 Heat Shock Protein Fusions: A Platform for the Induction of Antigen-Specific Immunity
- 18 Molecular Chaperones as Inducers of Tumour Immunity
- SECTION 6 EXTRACELLULAR BIOLOGY OF MOLECULAR CHAPERONES: WHAT DOES THE FUTURE HOLD?
- Index
- References
Summary
Introduction
The unusual immunogenicity of heat shock proteins (also known as stress proteins) was discovered in studies of the immune response to microbial infection, in which a large proportion of the humoral and cellular immune response to diverse microbial pathogens was found to be specific for pathogen-derived heat shock protein [1]. These studies demonstrated that immune recognition of pathogen-derived heat shock proteins occurs in natural and experimental settings in animals and man. This is discussed in detail in Chapter 16. Immune responses elicited to mycobacterial heat shock proteins have been particularly well studied. In man, recognition of mycobacterial heat shock protein by CD4+ T cells occurs in the context of numerous human leukocyte antigen (HLA) alleles, and epitopes have been identified that are presented by multiple HLA molecules [2]. The promiscuous recognition of mycobacterial heat shock proteins supports their utility as ‘universal’ immunogens for the genetically diverse human population. The immunogenic properties of microbial heat shock proteins have accordingly led to their application in a variety of immunisation formats as prophylactic and therapeutic agents in models of infectious disease and cancer [3]. In these studies, heat shock proteins have been delivered as subunit vaccines, carrier proteins in chemical conjugates, recombinant fusion proteins and DNA expression vectors for induction of humoral and cellular immunity.
To explain the disproportionate focus of the immune response on a small subset of pathogen antigens, heat shock proteins were proposed to act as ‘red flags’ – alerting the immune system to the presence of a foreign invader [4].
- Type
- Chapter
- Information
- Molecular Chaperones and Cell Signalling , pp. 288 - 299Publisher: Cambridge University PressPrint publication year: 2005
References
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