Cellular localization of a Hsp90 homologue in Porphyromonas gingivalis

Lopatin, Dennis E.

doi:10.1016/s0378-1097(99)00506-6

Cited by 10 publications

(16 citation statements)

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“…This association appears to be protective only in individuals with P. gingivalis in their subgingival dental plaque (22). Subsequently, we reported that P. gingivalis expressed a 68-kDa protein reactive with antibodies directed against human Hsp90 (21). The antibody reactivity and the presence of a 68-kDa polypeptide are consistent with the existence of a member of the HtpG family, the Hsp90 homologue found in prokaryotes.…”

mentioning

confidence: 59%

“…This antibody was raised against a conserved epitope of A. ambisexualis shown to react with multiple species (33). Two additional antibodies subsequently became available for use in the analysis of P. gingivalis Western blots: rabbit anti-E. coli HtpG, a generous gift of James Bardwell, and rabbit anti-human Hsp90 prepared in our laboratory (21). Reactivity with P. gingivalis ATCC 33277 whole cells at mid-log phase (A 600 ϭ 0.32) stressed at 45°C or held at a control temperature of 37°C is shown in Fig.…”

Section: Resultsmentioning

confidence: 99%

“…The antibody reactivity and the presence of a 68-kDa polypeptide are consistent with the existence of a member of the HtpG family, the Hsp90 homologue found in prokaryotes. In addition, we showed by immunoelectron microscopy that the P. gingivalis antiHsp90-reactive epitope is associated with the cell membrane fraction and extracellular vesicles (21).…”

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confidence: 88%

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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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confidence: 59%

Section: Resultsmentioning

confidence: 99%

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

et al. 2000

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“…Lopatin et al (1999a) found a 68-kDa HSP90 protein in P. gingivalis that cross-reacts with antibodies to human HSP90. They also reported the presence of antibodies in the sera of periodontitis patients that cross-react with P. gingivalis HSP90 (Lopatin et al, 1999b).…”

Section: (33) Hsp90 Proteinsmentioning

confidence: 97%

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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“…These molecules seem to provide protection from only a very high level of heat shock (ϳ45°C) and are involved in tetrapyrrole biosynthesis (51). HtpG of P. gingivalis is minimally expressed on the bacterial surface, and an HtpG disruption mutation in P. gingivalis did not affect growth or adherence to mammalian cells (26,47). The N-terminal 600 amino acids of HtpG contain some regions common to all molecules of the HSP90 group; however, P18 was found to be exclusive to Bacteroides spp.…”

mentioning

confidence: 99%

Immunoglobulin G (IgG) Class, but Not IgA or IgM, Antibodies to Peptides of thePorphyromonas gingivalisChaperone HtpG Predict Health in Subjects with Periodontitis by a Fluorescence Enzyme-Linked Immunosorbent Assay

Sweier¹,

Shelburne²,

Giannobile³

et al. 2009

Clin Vaccine Immunol

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Chaperones are molecules found in all cells and are critical in stabilization of synthesized proteins, in repair/removal of defective proteins, and as immunodominant antigens in innate and adaptive immunity. Subjects with gingivitis colonized by the oral pathogen Porphyromonas gingivalis previously demonstrated levels of anti-human chaperone Hsp90 that were highest in individuals with the best oral health. We hypothesized that similar antibodies to pathogen chaperones might be protective in periodontitis. This study examined the relationship between antibodies to P. gingivalis HtpG and clinical statuses of healthy and periodontitissusceptible subjects. We measured the humoral responses (immunoglobulin G [IgG], IgA, and IgM) to peptides of a unique insert (P18) found in Bacteroidaceae HtpG by using a high-throughput, quantitative fluorescence enzyme-linked immunosorbent assay. Indeed, higher levels of IgG class anti-P. gingivalis HtpG P18 peptide (P < 0.05) and P18␣, consisting of the N-terminal 16 amino acids of P18 (P < 0.05), were associated with better oral health; these results were opposite of those found with anti-P. gingivalis whole-cell antibodies and levels of the bacterium in the subgingival biofilm. When we examined the same sera for IgA and IgM class antibodies, we found no significant relationship to subject clinical status. The relationship between anti-P18 levels and clinical populations and individual subjects was found to be improved when we normalized the anti-P18␣ values to those for anti-P18␥ (the central 16 amino acids of P18). That same ratio correlated with the improvement in tissue attachment gain after treatment (P < 0.05). We suggest that anti-P. gingivalis HtpG P18␣ antibodies are protective in periodontal disease and may have prognostic value for guidance of individual patient treatment.

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Cellular localization of a Hsp90 homologue in Porphyromonas gingivalis

Cited by 10 publications

References 16 publications

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

Immunoglobulin G (IgG) Class, but Not IgA or IgM, Antibodies to Peptides of thePorphyromonas gingivalisChaperone HtpG Predict Health in Subjects with Periodontitis by a Fluorescence Enzyme-Linked Immunosorbent Assay

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