Heat shock response of spirochetes

Stamm, Lola V.; Gherardini, Frank C.; Parrish, Eloise; Moomaw, Carolyn R.

doi:10.1128/iai.59.4.1572-1575.1991

Cited by 72 publications

(31 citation statements)

References 25 publications

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“…This differs from what is seen in other bacteria, e.g. in A. actinomycetemcomitans (15) and Leptospira interrogans (37), where the level of HSP60 was higher than HSP70. In E. coli , GroEL represents 1 to 2% of the total protein content under normal conditions, while under stress its concentration is increased four‐ to five‐fold (38).…”

Section: Discussioncontrasting

confidence: 88%

“…From the autoradiograms and the densitometric scans in our study, a significant increase in the synthesis of a 60‐kDa protein at elevated temperatures could be observed. From what has been observed in other bacteria (15, 37), one would have expected a higher synthesis, more like the 70‐kDa protein. We do have difficulties in explaining this.…”

Section: Discussionmentioning

confidence: 80%

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The heat shock response of Fusobacterium nucleatum

Skår

Bakken

2001

European J Oral Sciences

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The heat-shock response of the oral Gram-negative bacterium Fusobacterium nucleatum was examined. Different strains of F. nucleatum were grown at 37 C. 42 degrees C and 48 C in the presence of [35S]methionine. Cellular proteins synthesised after shifts to higher temperatures were analysed by SDS-PAGE and autoradiography. Strains ATCC 10953, F1, F3 and Fev1 exhibited heat-shock response, and major proteins were observed at 60, 70 and 90 kDa. but increased protein synthesis was also observed for other proteins. Immunoblot analysis, using a panel of antibodies directed to epitopes on different known heat-shock proteins revealed cross-reactive proteins, indicating homology between Escherichia coli, Mycobacterium leprae and F. nucleatum heat shock proteins.

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Section: Discussioncontrasting

confidence: 88%

Section: Discussionmentioning

confidence: 80%

The heat shock response of Fusobacterium nucleatum

Skår

Bakken

2001

European J Oral Sciences

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“…In a first step, the specificities and sensitivities of a series of immunodominant antigens in Ig WB were determined (Table 1). These included molecularly and immunologically well-characterized proteins like p83/100 (21,25,31,33), p66 (6), p60 (a homolog of GroEL of Escherichia coli) (16,26,36,37), p41 (flagellin) (14,38), p39 (BmpA) (32,34,35), OspA (4,43), and OspC (12,22,44,47). p75 in our WB is presumably identical to the heat shock protein, homologous to DnaK of E. coli, described by Luft et al (26) and Coleman and Benach (8).…”

Section: Discussionmentioning

confidence: 99%

Diagnostic Value of Proteins of ThreeBorreliaSpecies (Borrelia burgdorferiSensu Lato) and Implications for Development and Use of Recombinant Antigens for Serodiagnosis of Lyme Borreliosis in Europe

Hauser

Lehnert

Wilske

1998

Clin Diagn Lab Immunol

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More and more assays for the serodiagnosis of Lyme borreliosis (LB) are based on recombinant antigens. However, so far, there is no consensus as to which are the most specific and sensitive proteins and how they should be used in combination to obtain tests with the best discrimination abilities. The present study was preceded by a detailed analysis of Western blots (WB) using whole-cell lysates ofBorrelia burgdorferi sensu stricto strain PKa2, B. afzelii PKo, and B. garinii PBi (U. Hauser, G. Lehnert, R. Lobentanzer, and B. Wilske, J. Clin. Microbiol. 35:1433–1444, 1997). For the present work, the data bank from that study, containing information about the reactivities of 330 sera (from patients at different stages of LB [n = 189]; control group, n = 141), was reused. The specificities and sensitivities of various combinations of proteins from different strains were calculated for different interpretation criteria. For immunoglobulin G (IgG) WB, the recommended combination of antigens available to date as recombinant proteins included p83/100 of PKa2, p83/100 of PKo, p39 of PKo, p39 of PBi, and OspC of PBi (interpretation criterion, at least one reactive band required for a positive WB; specificity, 96.5%; sensitivity, 56.1%). The further addition of p58 of PKo, p17 of PKo, or p14 of PKo was most favorable in terms of both a considerable gain of sensitivity and little loss of specificity. IgG Western blotting with a whole-cell lysate of strain PKo might be improved by the addition of OspC of PBi. For IgG WB, the best combination, out of all bands, was p83/100, p58, p39, p30, and p21 of all three strains and OspC of PBi, p17b of PBi, p56 of PKa2, p43 of PKo, p17 of PKo, and p14 of PKo (interpretation criterion, at least two reactive bands required for a positive WB; specificity, 97.2%; sensitivity, 61.4%). An interpretation criterion of at least two reactive bands is more reliable than one of only one reactive band. For IgM WB, the best combination was OspC of PKo, OspC of PBi, p39 of all three strains, p17 of PKo, and strong reactions with p41 of all three strains (interpretation criterion, at least one reactive band required; specificity, 97.9%; sensitivity, 47.0%).

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“…The stress response in bacteria, its expression and regulation has mostly been studied in E. coli [12,13] but many hsp-like proteins have recently been identified in other Gram-negative species [14,15,16,17,18]. Except for one recent study [19] which indicated that a GroEL-like protein of Actinobacillus actinomycetemcomitans is an immunodominant antigen and a survey of the heat shock response of spirochetes including T. denticola [20], there has been no report on the heat shock response of other oral bacteria. In this study, we have shown that P. gingivalis as well as all other oral bacterial species tested exhibit a heat shock response.…”

Section: Resultsmentioning

confidence: 99%

“…3 shows some of these bands at different molecular mass for species other than P. gingiualis. This figure includes also the positive control which is stressed and unstressed E. cofi [20] who have identified a GroEL-like protein in T. denticolu. When the various heat-shocked bacterial species were tested with the anti-DnaK antibody (hsp70-like) only two isolates, Capnocytophugu sp.…”

Section: Resultsmentioning

confidence: 99%

Detection of stress proteins in Porphyromonas gingivalis and other oral bacteria by Western immunoblotting analysis

Vayssier

1994

FEMS Microbiology Letters

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Detection of stress proteins in Porphyromonas gingivalis was investigated by SDS-PAGE and Western immunoblotting procedure using a polyclonal antibody (anti hsp60) and a monoclonal antibody (anti-Dnak). Results indicate that P. gingivalis can elicit a hsp60-like stress protein when submitted to different environmental stresses such as a heat shift from 35 degrees C to 43 degrees C, a pH drop from 7.2 to 6.0 or an increase in oxygen concentration. Virulent and non-virulent strains of P. gingivalis responded the same way. The other bacterial species tested also showed an increased synthesis of a GroEL-like protein after heat shock, as detected by the anti hsp60 antibody. However, the monoclonal anti-Dnak recognized an hsp70-like protein only in two of the tested species.

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Heat shock response of spirochetes

Cited by 72 publications

References 25 publications

The heat shock response of Fusobacterium nucleatum

The heat shock response of Fusobacterium nucleatum

Diagnostic Value of Proteins of ThreeBorreliaSpecies (Borrelia burgdorferiSensu Lato) and Implications for Development and Use of Recombinant Antigens for Serodiagnosis of Lyme Borreliosis in Europe

Detection of stress proteins in Porphyromonas gingivalis and other oral bacteria by Western immunoblotting analysis

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