Stress proteins may provide a link between the immune response to infection and autoimmunity

Lamb, Jonathan R.; Bal, Vineeta; Méndez-Samperio, Patricia; Mehiert, A.; So, Alex; Rothbard, Jonathan; Jindal, Shalini; Young, Richard A.; Young, Deborah

doi:10.1093/intimm/1.2.191

Cited by 253 publications

(142 citation statements)

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“…A substantial sequence homology exists between equivalent Hsp family members derived either from prokaryotes or eukaryotes [14,28]. Hence it was assumed that these Hsps would have a high degree of functional conservation, also with respect to their protective capacity in a Vibrio challenge test.…”

Section: Discussionmentioning

confidence: 99%

Efficacy of heterologous and homologous heat shock protein 70s as protective agents to Artemia franciscana challenged with Vibrio campbellii

Baruah

Ranjan

Sorgeloos

et al. 2010

Fish & Shellfish Immunology

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a b s t r a c tThe Hsp70 class of heat shock proteins (Hsps) has been implicated at multiple points in the immune response of both vertebrates and invertebrates. This class of chaperones is highly conserved in both sequence and structure, from prokaryotes to higher eukaryotes. In view of their high degree of homology, it was assumed that these Hsp70 proteins derived either from the prokaryotes or eukaryotes would have similar functions, especially in relation to their protective ability in a challenge assay. To verify this, we compared two evolutionary diverse Hsp70s, Artemia Hsp70 and Escherichia coli Hsp70 equivalent DnaK (each overproduced in E.coli), for their ability to protect Artemia against Vibrio challenge. Results showed that Artemia fed with E. coli producing Artemia Hsp70 or DnaK proteins, as assessed by immune-probing in western blots, survived better in a Vibrio challenge assay. The observed effects could be due to enhancement of the Artemia immune system as phenoloxidase activity was found to be increased by these proteins. These two Hsp70 proteins exhibit a high degree of homology, particularly in the peptidebinding domain (the putative innate immunity-activating portion) with 59.6% identity, indicating that the observed protective capacity of homologous or heterologous Hsp70 proteins might reside within this peptide-binding domain.

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Section: Discussionmentioning

confidence: 99%

Efficacy of heterologous and homologous heat shock protein 70s as protective agents to Artemia franciscana challenged with Vibrio campbellii

Baruah

Ranjan

Sorgeloos

et al. 2010

Fish & Shellfish Immunology

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“…Several studies have implicated stress proteins from different bacteria in the induction of autoimmune disease (Lamb et al, 1989;Oldstone, 1987;Young, 1990). Heatshock proteins of many pathogenic bacteria (e.g.…”

Section: Discussionmentioning

confidence: 99%

Microbial pathogenesis in cystic fibrosis: co‐ordinate regulation of heat‐shock response and conversion to mucoidy in Pseudomonas aeruginosa

Schurr

Deretić

1997

Molecular Microbiology

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SummaryConversion of Pseudomonas aeruginosa to the mucoid phenotype plays a major role in the pathogenesis of respiratory infections in cystic fibrosis (CF). One mechanism responsible for mucoidy is based on mutations that inactivate the anti-factor, MucA, which normally inhibits the alternative sigma factor, AlgU. The loss of MucA allows AlgU to freely direct transcription of the genes responsible for the production of the exopolysaccharide alginate resulting in mucoid colony morphology. In Escherichia coli, a close homologue of AlgU, E , directs transcription of several genes under conditions of extreme heat shock. Here we examined whether AlgU, besides its role in controlling alginate production, affects the heat-shock response in P. aeruginosa. The P. aeruginosa rpoH gene encoding a homologue of the major heat-shock sigma factor, 32 , was found to be transcribed by AlgU containing RNA polymerase from one of its promoters (P 3 ) identified in this study. Transcription of rpoH from P 3 was elevated upon exposure to extreme heat shock in an algU-dependent manner. Importantly, the AlgU-dependent promoter of rpoH was found to be activated in mucoid mucA mutants. In keeping with this observation, introduction of a wild-type mucA gene abrogated AlgU-dependent rpoH transcription in mucoid P. aeruginosa laboratory isolates and CF isolates. These results suggest that conversion to mucoidy and the heat-shock response are co-ordinately regulated in P. aeruginosa. The simultaneous activation of both systems in mucA mutants, selected in the lungs of CF patients, may have significance for the inflammatory processes characteristic of the establishment of chronic infection and ensuing clinical deterioration in CF.

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“…Based on the strong sequence homologies in HSP families from pro-and eukaryotes (Jindal et al, 1989;Lamb et al, 1989) it seems possible that HSP, particularly the 65-kD HSP, are the common denominator of all the causes discussed in the past for RA (Holoshitz era/., 1986;Rook, 1988). In addition, the postulated antigenic mimicry as a basis for the induction of RA (van Eden, Holoshitz & Cohen, 1987;Gaston et al, 1989) would be more acceptable.…”

Section: Discussionmentioning

confidence: 99%

Prevention of adjuvant arthritis in rats by a nonapeptide from the 65-kD mycobacterial heat-shock protein

Yang

Gasser

Feige

1990

Clinical and Experimental Immunology

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SUMMARYAdjuvant arthritis in Lewis rats is a model of T cell-mediated autoimmune arthritis resembling human rheumatoid arthritis, A nonapeptide from the 65-kD heat-shock protein of Mycobacterium bovis BCG, amino acid sequence 180-188, has been described to carry the dominant immunogenic epitope(s) for both arthritis-protective and arthritogenie T cell clones. Here we demonstrate that immunizations with the synthetic nonapeptide completely protected rats against adjuvant arthritis induced by M. tuberculosis. Interestingly, deletion of the N-teminal threonine of the nonapeptide resulted in loss ofthe protective activity, Pretreatments with the nonapeptide resulted in an immune response to the nonapeptide and to M. tuberculosis. After immunizations with the synthetic nonapeptide, only low titres of nonapeptide-specific antibodies were produced, whereas a significant cellular immune response to the nonapeptide was observed. In addition, the protection was transferable to naive rats by spleen T cells. These findings document the requirement of a T cellspecific immune response to the dominant epitope ofthe 65-kD mycobacterial heat-shock protein for the protection against adjuvant arthritis and suggest the feasibility of immune intervention in autoimmune arthritis through the use of synthetic peptides.

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Stress proteins may provide a link between the immune response to infection and autoimmunity

Cited by 253 publications

References 0 publications

Efficacy of heterologous and homologous heat shock protein 70s as protective agents to Artemia franciscana challenged with Vibrio campbellii

Efficacy of heterologous and homologous heat shock protein 70s as protective agents to Artemia franciscana challenged with Vibrio campbellii

Microbial pathogenesis in cystic fibrosis: co‐ordinate regulation of heat‐shock response and conversion to mucoidy in Pseudomonas aeruginosa

Prevention of adjuvant arthritis in rats by a nonapeptide from the 65-kD mycobacterial heat-shock protein

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