<i>Porphyromonas gingivalis</i> heat shock protein vaccine reduces the alveolar bone loss induced by multiple periodontopathogenic bacteria

Lee, Ju Youn; Yi, Ni-Na; Kim, Ueon-Suk; Choi, J.-S.; Kim, Sung-Jo; Choi, Jaeho

doi:10.1111/j.1600-0765.2005.00832.x

Cited by 48 publications

(44 citation statements)

References 22 publications

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“…Therefore, they are frequently used to produce subunit vaccines. Numerous studies have shown the efficiency of immunisation with HSP family proteins in the induction of a protective immune response against pathogens (Kaufman et al 1990;Mannicki 1995;Noll and Autenrieth 1996;Lee et al 2006;Bansal et al 2010). It has been demonstrated that H. somni rHsp60 induces an immune response in SPF mice .…”

Section: Discussionmentioning

confidence: 99%

Humoral and cellular immune response to Histophilus somni recombinant heat shock protein 60 kDa in farm animals

Jankowska¹,

Bajzert²,

Pisarek³

et al. 2015

Vet. Med.

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ABSTRACT:The aim of this study was to evaluate the effects of immunising farm animals with the Histophilus somni recombinant heat shock protein 60kDa (H. somni rHsp60) in field conditions. Fifty piglets, 10 calves and 30 hens were immunised twice, and the same number of each species was used as the control. The humoral immune response was evaluated using ELISA in piglets (IgG, IgA and IgM) and calves (IgG 1 , IgG 2 and IgM) sera and in hen egg yolks (IgY). Cell-mediated immune responses were evaluated using the skin test. Concentrations of serum haptoglobin in calves and piglets and plasma fibrinogen in calves, daily weight gain in piglets, as well as the inner body temperature and clinical signs in calves were measured to evaluate the clinical effects of vaccination. In animals immunised twice with H. somni rHsp60, a statistically significant increase in IgY antibodies in egg yolk as well as serum IgG 1 and IgG 2 antibodies in calves (P < 0.05) was found. In piglets, the antibody reaction against H. somni rHsp60 was higher in the experimental than in the control group, but the difference was significant only for the IgG class (P < 0.05). A moderate cell-mediated immune response to H. somni rHsp60 measured using the skin test was observed in piglets after 24 h (P < 0.05), but not in calves and hens. The daily weight gain was significantly higher in the experimental than in the control piglets (P < 0.05). The fibrinogen and haptoglobin levels in calves, as well as the inner body temperature, indicated a reduced risk of pathology in the experimental group of calves. The preliminary results confirmed the immunogenicity of H. somni rHsp60. A beneficial effect on piglet weight gain was observed. The obtained results warrant further studies of the protective effects of H. somni rHsp60 as an ingredient of subunit vaccines in farm animals.

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Section: Discussionmentioning

confidence: 99%

Humoral and cellular immune response to Histophilus somni recombinant heat shock protein 60 kDa in farm animals

Jankowska¹,

Bajzert²,

Pisarek³

et al. 2015

Vet. Med.

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“…They are potent inducers of the immune system, inducing both innate and adaptive immune responses. 27,28 Many microbial HSPs are reported to be dominant antigens that elicit host immune responses to a variety of pathogens [29][30][31][32][33][34] and act as effective adjuvants. 35 Previously, we developed recombinant (r) Hsp 60 (GroEL) and rHsp70 (DnaK) from Salmonella enterica serovar Typhi, and we reported that these candidate vaccine molecules stimulate both arms of immunity against S. Typhi and S. typhimurium infection in mice.…”

Section: Introductionmentioning

confidence: 99%

Co-administration of rIpaB domain of Shigella with rGroEL of S. Typhi enhances the immune responses and protective efficacy against Shigella infection

et al. 2015

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Shigella species cause severe bacillary dysentery in humans and are associated with high morbidity and mortality. The Invasion plasmid antigen (IpaB) protein, which is conserved across all Shigella spp., induces macrophage cell death and is required to invade host cells. The present study evaluates the immunogenicity and protective efficacy of the recombinant (r) domain region of IpaB (rIpaB) of S. flexneri. rIpaB was administered either alone or was co-administered with the rGroEL (heat shock protein 60) protein from S. Typhi as an adjuvant in a mouse model of intranasal immunization. The IpaB domain region (37 kDa) of S. flexneri was amplified from an invasion plasmid, cloned, expressed in BL21 Escherichia coli cells and purified. Immunization with the rIpaB domain alone stimulated both humoral and cell-mediated immune responses. Furthermore, robust antibody (IgG, IgA) and T-cell responses were induced when the rIpaB domain was co-administered with rGroEL. Antibody isotyping revealed higher IgG1 and IgG2a antibody titers and increased interferon-gamma (IFN-c) secretion in the co-administered group. Immunization of mice with the rIpaB domain alone protected 60%-70% of the mice from lethal infection by S. flexneri, S. boydii and S. sonnei, whereas co-administration with rGroEL increased the protective efficacy to 80%-85%. Organ burden and histopathological studies also revealed a significant reduction in lung infection in the co-immunized mice compared with mice immunized with the rIpaB domain alone. This study emphasizes that the co-administration of the rIpaB domain and rGroEL protein improves immune responses in mice and increases protective efficacy against Shigella infection. This is also the first report to evaluate the potential of the GroEL (Hsp 60) protein of S. Typhi as an adjuvant molecule, thereby overcoming the need for commercial adjuvants.

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“…Assays for a qualified target, such as the P18 subpeptides, would indicate/ justify aggressive adjunct periodontitis treatment and provide a simple method for monitoring that treatment. In the long term, these subpeptides might be found to be effective vaccine candidates (21). Since the P18 subpeptides appear to be unique antigens, they could be used as vaccines without fear of inducing inappropriate responses to human Hsp90.…”

Section: Discussionmentioning

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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Porphyromonas gingivalis heat shock protein vaccine reduces the alveolar bone loss induced by multiple periodontopathogenic bacteria

Abstract: We concluded that P. gingivalis HSP60 could potentially be developed as a vaccine to inhibit periodontal disease induced by multiple pathogenic bacteria.

Cited by 48 publications

References 22 publications

Humoral and cellular immune response to Histophilus somni recombinant heat shock protein 60 kDa in farm animals

Humoral and cellular immune response to Histophilus somni recombinant heat shock protein 60 kDa in farm animals

Co-administration of rIpaB domain of Shigella with rGroEL of S. Typhi enhances the immune responses and protective efficacy against Shigella infection

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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