Heat shock proteins in immunopathology

C.M., Pieter; Thole, Jelle; Vries, RenéR.P. de

doi:10.1016/0960-9822(92)90203-m

Cited by 5 publications

(8 citation statements)

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“…An immune response to bacterial HSP60 is suggested to play a role in protection against infection by these microorganisms. However, inflammatory defense reactions might also be triggered and contribute to the local tissue damage [7]. It was shown in monkeys that purified chlamydial HSP60 is capable to elicit a delayed type hypersensitivity response in the eye whereas HSP70 was not able to provoke the reaction [22].…”

Section: Discussionmentioning

confidence: 99%

“…In addition, human HSP60 shares sequence homology with a wide range of known autoantigens [31]. T cells, activated by bacterial HSPs, might therefore cause autoimmunity by a cross-reaction with molecules (HSP or non-HSP) in autologous tissues [7]. It remains to be tested whether HSP molecules from oral bacteria might trigger off systemic diseases, but it has recently been proposed that 65 kDa HSP from Streptococcus sanguis might be implicated in the development of Behcet's syndrome [32].…”

Section: Discussionmentioning

confidence: 99%

“…HSPs may play important roles in antimicrobial defense and immunopathology (see reviews in [4][5][6][7]). The proteins show a remarkable degree of conservation among widely divergent organisms.…”

Section: Introductionmentioning

confidence: 99%

“…Furthermore, stressed autologous cells that bear endogenous or exogenous HSPs on their cell membrane surface may be eliminated [4]. However, due to extensive sequence homology between human and bacterial HSPs, an improperly regulated immune response to HSPs may turn against the host and result in immunopathology and in autoimmune disease (hypotheses reviewed in [7]).…”

Section: Introductionmentioning

confidence: 99%

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Heat shock response in Actinobacillus actinomycetemcomitans

Løkensgard¹

1994

FEMS Immunology and Medical Microbiology

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The heat shock response in Actinobacillus actinomycetemcomitans, a capnophilic Gram-negative bacterial species that is implicated in the development of certain forms of periodontitis, was characterized. Different strains of A. actinomycetemcomitans were grown at 37, 42 and 48 degrees C in the presence of 35S-methionine. The bacterial cells were lysed, run on SDS-PAGE and subsequently blotted on nitrocellulose paper. After autoradiography of the blots, several protein bands from the cultures at 42 degrees C showed an increased intensity; major bands were observed at 90, 70, and 60 kDa, but increased protein synthesis was also detected at 54, 28 and 17 kDa. Nitrocellulose blots were also incubated with a panel of monoclonal and polyclonal antibodies directed to epitopes on different heat shock proteins. Strong reactivity was found with several antibodies at the position corresponding to a molecular mass of 60 kDa. The protein is probably the GroEL homologue in A. actinomycetemcomitans, a member of the 'common bacterial antigen' family.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Heat shock response in Actinobacillus actinomycetemcomitans

Løkensgard¹

1994

FEMS Immunology and Medical Microbiology

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“…Heat Shock Proteins (HSP) are highly conserved proteins, synthesized in large amounts when cells are exposed to stressful stimuli [1]. Extensive sequence homology between microbial and human HSP [2] has led to the concept that HSP might be involved in the aetiology and pathogenesis of autoimmune disorders [3,4]. Immunization with heat-killed Mycobacterium tuberculosis induces adjuvant arthritis in rats, and the disease could be transferred to naive animals by HSP-primed T-cell clones reactive to T-cell epitope 180-188 of the 65 kDa HSP [5].…”

Section: Introductionmentioning

confidence: 99%

Recognition of B‐Cell Epitopes of the 65 kDa HSP in Behçet's Disease

et al. 1996

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B-cell epitopes of the mycobacterial 65 kDa heat shock protein (HSP) were mapped in sera from patients with Behçet's Disease (BD). A series of 47 overlapping synthetic peptides (15ers) derived from the sequence of the Mycobacterium tuberculosis 65 kDa HSP was used in ELISA. Significant increases in IgA and IgG antibody levels were observed with peptides 111-125, 154-172 and 311-326 in sera from BD, compared with those from controls. Homologous peptides derived from the sequence of the human mitochondrial 60 kDa HSP were then examined. Peptides 136-150 and 336-351 showed comparable results to the homologous mycobacterial peptides 111-125 and 311-326, respectively. The B-cell epitopes defined in this investigation overlap with the T-cell epitopes the authors have previously reported in BD. Inhibition studies are consistent with the view that antibodies to each of the three B-cell epitope peptides represent a small proportion of the total B-cell epitope repertoire elicited by the 65 or 60 kD HSP. Sequential antibody studies suggest that IgA and IgG antibody titres to one or all three peptides tested may increase during exacerbation of ocular disease. The functional role of these antibodies needs to be determined, but the peptides may be involved in the immunopathogenesis of BD as they can induce experimental uveitis in Lewis rats, which is a principal manifestation of BD.

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Oral Microbial Heat-shock Proteins and Their Potential Contributions to Infections

Goulhen

Grenier

Mayrand

2003

Critical Reviews in Oral Biology & Medicine

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ABSTRACT:The oral cavity is a complex ecosystem in which several hundred microbial species normally cohabit harmoniously. However, under certain special conditions, the growth of some micro-organisms with a pathogenic potential is promoted, leading to infections such as dental caries, periodontal disease, and stomatitis. The physiology and pathogenic properties of micro-organisms are influenced by modifications in environmental conditions that lead to the synthesis of specific proteins known as the heat-shock proteins (HSPs). HSPs are families of highly conserved proteins whose main role is to allow micro-organisms to survive under stress conditions. HSPs act as molecular chaperones in the assembly and folding of proteins, and as proteases when damaged or toxic proteins have to be degraded. Several pathological functions have been associated with these proteins. Many HSPs of oral micro-organisms, particularly periodontopathogens, have been identified, and some of their properties-including location, cytotoxicity, and amino acid sequence homology with other HSPs-have been reported. Since these proteins are immunodominant antigens in many human pathogens, studies have recently focused on the potential contributions of HSPs to oral diseases. The cytotoxicity of some bacterial HSPs may contribute to tissue destruction, whereas the presence of common epitopes in host proteins and microbial HSPs may lead to autoimmune responses. Here, we review the current knowledge regarding HSPs produced by oral micro-organisms and discuss their possible contributions to the pathogenesis of oral infections.

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Heat shock proteins in immunopathology

Cited by 5 publications

References 0 publications

Heat shock response in Actinobacillus actinomycetemcomitans

Heat shock response in Actinobacillus actinomycetemcomitans

Recognition of B‐Cell Epitopes of the 65 kDa HSP in Behçet's Disease

Oral Microbial Heat-shock Proteins and Their Potential Contributions to Infections

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