IL12, IL10, IFNγ and TNFα Expression in Human Primary Monocytes Stimulated with Bacterial Heat Shock GroEL (Hsp64) Protein

Nalbant, Ayten; Saygılı, Tahsin

doi:10.1371/journal.pone.0154085

Cited by 8 publications

(8 citation statements)

References 24 publications

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“…Despite this structural conservation, previous reports have shown additional functions of chaperonins besides those to assist protein folding and to protect proteins from denaturation [ 21 – 31 ]. The divergent sequences observed in the substrate-binding domains of chaperonins from group I in comparison of sequences from group II chaperonin subunits might be related with the multiple unexpected biological activities of bacterial HSPs that have been identified, such as induction of proinflammatory molecules [ 24 – 28 ] and adheshion of the host components [ 23 , 58 – 62 ], as described here. In conclusion, leptospiral GroEL protein may contribute to the adhesion of leptospires to host tissues, stimulate the production of cytokines during infection and be involved in the pathogenesis of leptospirosis.…”

Section: Discussionmentioning

confidence: 89%

“…Since several bacterial HSPs have been identified as potent proinflammatory agents [ 24 – 28 ], we investigated the cytokine expression profiles of murine macrophage cell line J774.1 stimulated with different concentrations of GroEL protein. As shown in the Fig.…”

Section: Resultsmentioning

confidence: 99%

“…Besides these functions, these proteins can present multiple unexpected biological activities [ 21 – 23 ]. Some are potent immunomodulatory proteins, being able to stimulate the production of nitric oxide and several cytokines, such as tumor necrosis factor-α (TNF-α), interferon-γ (IFNγ), and interleukins (IL) IL-1β, IL-6, IL10, and IL-12 in monocytes, macrophages, and dendritic cells [ 24 – 28 ]. In addition, previous studies showed that the bacterial HSPs are capable of binding to host components, inducing the aggregation and promoting the biofilm formation [ 29 – 31 ].…”

Section: Introductionmentioning

confidence: 99%

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GroEL protein of the Leptospira spp. interacts with host proteins and induces cytokines secretion on macrophages

Takara

Monaris

et al. 2021

BMC Microbiol

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Background Leptospirosis is a zoonotic disease caused by infection with spirochetes from Leptospira genus. It has been classified into at least 17 pathogenic species, with more than 250 serologic variants. This wide distribution may be a result of leptospiral ability to colonize the renal tubules of mammalian hosts, including humans, wildlife, and many domesticated animals. Previous studies showed that the expression of proteins belonging to the microbial heat shock protein (HSP) family is upregulated during infection and also during various stress stimuli. Several proteins of this family are known to have important roles in the infectious processes in other bacteria, but the role of HSPs in Leptospira spp. is poorly understood. In this study, we have evaluated the capacity of the protein GroEL, a member of HSP family, of interacting with host proteins and of stimulating the production of cytokines by macrophages. Results The binding experiments demonstrated that the recombinant GroEL protein showed interaction with several host components in a dose-dependent manner. It was also observed that GroEL is a surface protein, and it is secreted extracellularly. Moreover, two cytokines (tumor necrosis factor-α and interleukin-6) were produced when macrophages cells were stimulated with this protein. Conclusions Our findings showed that GroEL protein may contribute to the adhesion of leptospires to host tissues and stimulate the production of proinflammatory cytokines during infection. These features might indicate an important role of GroEL in the pathogen-host interaction in the leptospirosis.

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Section: Discussionmentioning

confidence: 89%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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GroEL protein of the Leptospira spp. interacts with host proteins and induces cytokines secretion on macrophages

Takara

Monaris

et al. 2021

BMC Microbiol

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“…Literature data indicate that bacterial heat shock protein (GroEL, Cpn60), originating from different bacteria, induces the expression of cytokines in cells of the host's immune system 30,31 . It is known that chaperonin Cpn60 from Mycobacterium tuberculosis induce production of TNF-α in human monocyte cell line, THP-1 32,33 .…”

Section: Discussionmentioning

confidence: 99%

Correlation of the expression of tumor necrosis factor-alpha in chronic periapical lesions with the expression of bacterial chaperonin 60

Stanisic-Zindovic¹,

Mihailovic²,

Djordjevic³

et al. 2022

VOJNOSANIT PREGL

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Background/Aim: The aim of this study is to determine the quantitative expression of the bacterial heat shock protein, Chaperonin-60 (Cpn60) and pro-inflammatory and anti-inflammatory cytokine in periapical tissue, obtained from individuals with chronic periapical lesions and to determine the correlation between the expression of the bacterial heat shock protein and the expression of these cytokines. Methods. The study was performed on 18 periapical lesions and 6 control samples of healthy periapical tissue, taken at the Clinic of Dental Medicine, Faculty of Medical 4 Sciences University of Pristina, Kosovska Mitrovica. The levels of mRNA expression of pro- and anti- inflammatory cytokines and bacterial heat shock protein were determined by real time quantitative RT-PCR. Results. Analysis revealed significantly higher mRNA levels of TNF-? and Cpn60 in the tissue of periapical lesions compared with normal periapical tissue (P <0.05). Contrary to these results, the mRNA expression of anti-inflammatory IL-10 was significantly higher in the samples of normal periapical tissue compared with the mRNA levels of this cytokine in the tissue of periapical lesions (P <0.001). Expression of Cpn60 is in strong correlation with TNF-? expression in periapical lesions. Conclusion. Cpn60 released from bacteria in periapical tissue could be a strong stimulator of inflammatory response and one of the important players in the pathogenesis of periapical lesions.

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“…In addition, since P.gingivalis GroEL increased the secretion of IL -6 and IL -8, it may be possible that P. gingivalis has take part in osteoclastogenesis via the activation of receptor activator of nuclear factor κ-B ligand mRNA and the inhibition of alkaline phosphatase mRNA in periodontal ligament cells(28) . Furthermore, GroEL has been reported to induce the expression of TNFα and IFNγ in human monocytes(29) . Therefore, nasal immunization using P. gingivalisGroEL as an immunogen may suppress the pathogenic activity of GroEL that leads to the destruction of periodontal tissue and bone.…”

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confidence: 99%

Nasal Vaccination with GroEL plus CpG ODN Inhibits <i>P. gingivalis</i>-induced Inflammation and Alveolar Bone Loss

et al. 2020

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The oral cavity is structurally considered to be an organ that provide double layers of protection simultaneously through secretory immunoglobulin A (S-IgA) from mucosal immunity and immunoglobulin (Ig) G antibodies (Abs) from gingival crevicular fluid (1-3). Although immunization via injection can induce an effective immune responses in the systemic immune systems, but not an antigen (Ag)specific mucosal immune responses. Therefore, in order to prevent oral infection, it is ideal to induce mucosal immunity and systemic immunity simultaneously. Chronic periodontitis reduces oral function by causing periodontal tissue destruction and bone resorption. Recently, chronic periodontitis has been reported to cause systemic diseases such as diabetes, aspiration pneumonia, and atherosclerosis, and their relationship has been investigated (4-9). Therefore, prevention of periodontitis is important for oral health and systemic health derived from the oral cavity. Currently 7 to 10 bacterial candidates have been claimed to be putative periodontal pathogens (10, 11). Among them, P. gingivalis is a keystone pathogen that is strongly associated with disease progression of chronic periodontitis. The reason for using GroEL as a vaccine antigen is that is can be found in most putative periodontopathic pathogens, including P.gingivalis, and it was reported to crossreact among bacterial antigens. Thus far, a positive relationship has been observed between levels of saliva IgA directed against GroEL and

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IL12, IL10, IFNγ and TNFα Expression in Human Primary Monocytes Stimulated with Bacterial Heat Shock GroEL (Hsp64) Protein

Cited by 8 publications

References 24 publications

GroEL protein of the Leptospira spp. interacts with host proteins and induces cytokines secretion on macrophages

GroEL protein of the Leptospira spp. interacts with host proteins and induces cytokines secretion on macrophages

Correlation of the expression of tumor necrosis factor-alpha in chronic periapical lesions with the expression of bacterial chaperonin 60

Nasal Vaccination with GroEL plus CpG ODN Inhibits <i>P. gingivalis</i>-induced Inflammation and Alveolar Bone Loss

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