Stress response of <i>Porphyromonas gingivalis</i>

Lu, Biqing; McBride, B C

doi:10.1111/j.1399-302x.1994.tb00054.x

Cited by 48 publications

(51 citation statements)

References 42 publications

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“…Previous studies have shown that expression of dnaK and groEL was increased when P. gingivalis was stressed at 42°C, but expression of these genes did not change in response to oxidative stress or pH (32). These data suggest that dnaK and groEL are related to temperature stress, but not oxidative or pH stress.…”

Section: Discussionsupporting

confidence: 52%

Microarray Analysis of Quorum-Sensing-Regulated Genes inPorphyromonas gingivalis

2005

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Quorum sensing is a phenomenon defined as gene regulation in response to cell density that regulates various functions in bacteria. The periodontopathogen Porphyromonas gingivalis possesses a luxS gene homologue that may encode a quorum-sensing system. In order to identify genes of P. gingivalis that are regulated by luxS, gene expression analysis was done using microarrays and RNA samples from the W83 wild-type strain and an isogenic luxS mutant, LY2001. The results indicated that 17 open reading frames (ORFs) in LY2001 are upregulated and two are downregulated. Real-time PCR was done to confirm the microarray results. Among the upregulated ORFs is a group of stress-related genes, including htrA, clpB, groEL, dnaK, and the F subunit of alkyl hydroperoxide reductase. This suggested that luxS is involved in stress gene regulation in P. gingivalis. Stress response experiments, including high-temperature survival, resistance to hydrogen peroxide (H 2 O 2 ), and survival during exposure to low and high pH, were performed on the P. gingivalis wild-type and LY2001 strains. LY2001 had a significantly higher survival rate than did W83 when stressed at 50°C. No difference was found at pH 5, but LY2001 had increased survival compared to W83 at pH 9. LY2001 also survived better than W83 when stressed with 0.35 mM H 2 O 2 . These results suggest that luxS might be involved in promoting survival of P. gingivalis in the host by regulating its response to host-induced stresses such as temperature, H 2 O 2 , and pH.

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Section: Discussionsupporting

confidence: 52%

Microarray Analysis of Quorum-Sensing-Regulated Genes inPorphyromonas gingivalis

2005

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“…There have been studies which reported (i) detection of common stress proteins in oral microorganisms (7)(8)(9), (ii) cloning of these stress proteins (10,24,43), (iii) demonstration of potent induction of bone resorption (16,30), or (iv) purification of specific heat shock proteins from various Hsp families (4,10,14,20,23,39,40,44). There have been several studies that reported an association between periodontal disease and titers of antibody to Hsp65 and Hsp90 in serum (17,22,24,31).…”

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confidence: 99%

Characterization of Heat-Inducible Expression and Cloning of HtpG (Hsp90 Homologue) of Porphyromonas gingivalis

et al. 2000

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Porphyromonas gingivalis is implicated in the etiology of periodontal disease. Associations between microbial virulence and stress protein expression have been identified in other infections. For example, Hsp90 homologues in several microbial species have been shown to contribute to virulence. We previously reported that P. gingivalis possessed an Hsp90 homologue (HtpG) which cross-reacts with human Hsp90. In addition, we found that elevated levels of serum antibody to Hsp90 stress protein in individuals colonized with this microorganism were associated with periodontal health. However, the role of HtpG in P. gingivalis has not been explored. Therefore, we cloned the htpG gene and investigated the characteristics of HtpG localization and expression in P. gingivalis. htpG exists as a single gene of 2,052 bp from which a single message encoding a mature protein of approximately 68 kDa is transcribed. Western blot analysis revealed that the 68-kDa polypeptide was stress inducible and that a major band at 44 kDa and a minor band at 40 kDa were present at constitutive levels. Cellular localization studies revealed that the 44-and 40-kDa species were associated with membrane and vesicle fractions, while the 68-kDa polypeptide was localized to the cytosolic fractions.

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“…Polyclonal antibodies raised against A. actinomycetemcomitans GroEL react strongly with E. coli GroEL and, to a lesser extent, with P. gingivalis and B. forsythus GroELs (Hinode et al, 1998a). The heat-shock response of P. gingivalis was first examined by Lu and McBride (1994) using one-and two-dimensional SDS-PAGE after labeling the cells with 14 Camino acids. Four proteins were up-regulated (62, 74, 80, and 92 kDa), and one (50 kDa) was down-regulated following a heat stress (Lu and McBride, 1994).…”

Section: (31) Groes and Groel Proteinsmentioning

confidence: 99%

“…The heat-shock response of P. gingivalis was first examined by Lu and McBride (1994) using one-and two-dimensional SDS-PAGE after labeling the cells with 14 Camino acids. Four proteins were up-regulated (62, 74, 80, and 92 kDa), and one (50 kDa) was down-regulated following a heat stress (Lu and McBride, 1994). Western immunoblotting analysis was used to confirm that P. gingivalis can increase production of GroEL and DnaK when subjected to a temperature shift from 35°C to 43°C (Vayssier et al, 1994).…”

Section: (31) Groes and Groel Proteinsmentioning

confidence: 99%

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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Stress response of Porphyromonas gingivalis

Cited by 48 publications

References 42 publications

Microarray Analysis of Quorum-Sensing-Regulated Genes inPorphyromonas gingivalis

Microarray Analysis of Quorum-Sensing-Regulated Genes inPorphyromonas gingivalis

Characterization of Heat-Inducible Expression and Cloning of HtpG (Hsp90 Homologue) of Porphyromonas gingivalis

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

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