Lipoprotein modifications by gingipains of Porphyromonas gingivalis

Lönn, Johanna; Ljunggren, Stefan; Klarström-Engström, Kristin; Demirel, Isak; Bengtsson, Torbjörn; Karlsson, Helén

doi:10.1111/jre.12527

Cited by 45 publications

(35 citation statements)

References 49 publications

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“…Arginine residue dissolution from l-arginine occurs after hydrolysis participates in the formation of the arginine-specific cysteine proteinase (Arg-gingipain) of P. gingivalis [23]. Gingipain can activate the production of reactive oxygen species and induce peroxidation to induce the inflammation and destruction of periodontal tissues [24]. Thus, the aim of the present study was to establish the P. gingivalis biofilm and investigate the effects of d-arginine in inhibiting and disassembling the P. gingivalis biofilm.…”

Section: Introductionmentioning

confidence: 99%

Effects of D-arginine on Porphyromonas gingivalis biofilm

Liu

et al. 2020

J Oral Sci

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Porphyromonas gingivalis (P. gingivalis) is one of the major pathogenic bacteria of periodontitis or peri-implantitis. P. gingivalis tends to attach to the implant's neck with the formation of biofilm, leading to peri-implantitis. d-arginine has been shown to have a potential antimicrobial role. In this study, P. gingivalis was cultured in Brain Heart Infusion broth together with d-arginine. After 3 days (inhibition) or 6 days (dissociation), these were characterized using crystal violet (CV) staining for the biofilm, extracellular polysaccharide (EPS) production from the biofilm, and 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyl tetrazolium bromide (MTT) assay for biofilm activation. Furthermore, the P. gingivalis biofilm was observed by scanning electron microscopy (SEM). d-arginine effectively reduced biomass accumulation and promoted dissociation at concentrations of ≥50 mM and 100 mM, respectively. Through CV staining, d-arginine concentrations of EPS production from the biofilm for inhibition and dissociation effects was ≥50 mM and 100 mM, respectively. In addition, d-arginine affected biofilm activation for the corresponding concentrations: ≥60 mM for inhibition and ≥90 mM for dispersal. Under SEM observation, d-arginine changed the P. gingivalis biofilm structure in relatively high concentrations for inhibition or dissociation, respectively. The authors concluded that d-arginine could inhibit the formation of P. gingivalis biofilm and promote the dissociation of P. gingivalis biofilm.

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Section: Introductionmentioning

confidence: 99%

Effects of D-arginine on Porphyromonas gingivalis biofilm

Liu

et al. 2020

J Oral Sci

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“…LDL modification in vascular compartment may occur as a result of proteolytic effects of P. gingivalis and/or leukocyte proteases or by the oxidative burst response of phagocytes in the blood to P. gingivalis . LDL was reported to form aggregates with P. gingivalis and its outer membrane vesicles (OMV).…”

Section: Discussionmentioning

confidence: 99%

Porphyromonas gingivalis‐induced inflammatory responses in THP1 cells are altered by native and modified low‐density lipoproteins in a strain‐dependent manner

Jayaprakash

Demirel

Khalaf

et al. 2018

APMIS

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Strong epidemiological evidence supports an association between cardiovascular and periodontal disease and furthermore, the periodontopathogen Porphyromonas gingivalis has been identified in blood and from atheromatous plaques. Blood exposed to P. gingivalis shows an increased protein modification of low-density lipoprotein (LDL). In this study, we investigate the inflammatory responses of THP1 cells incubated with P. gingivalis and the effects of native or modified LDL on these responses. Reactive oxygen species (ROS) and IL-1β were observed in THP1 cells following infection with P. gingivalis ATCC33277 and W50. Caspase 1 activity was quantified in THP1 cells and correlated with IL-1β accumulation. Oxidized LDL (oxLDL) induced IL-1β release and CD36 expression on THP1 cells. Modified LDL co-stimulated with ATCC33277 exhibited regulatory effects on caspase 1 activity, IL-1β release and CD36 expression in THP1 cells, whereas W50 induced more modest responses in THP1 cells. In summary, we show that P. gingivalis is capable of inducing pro-inflammatory responses in THP1 cells, and native and modified LDL could alter these responses in a dose- and strain-dependent manner. Strain-dependent differences in THP1 cell responses could be due to the effect of P. gingivalis proteases, presence or absence of capsule and proteolytic transformation of native and modified LDL.

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“…161 The activity of P. gingivalis and its virulence factors may also contribute to the increased cardiovascular disease risk in RA and Parkinson's disease (PD) patients. 162,163 It has been demonstrated that Arginine-specific gingipains (RgpA, RgpB) are able to activate the coagulation cascade at multiple levels. Gingipains proteolytically stimulate coagulation factors IX, 164 X, 165 and II (prothrombin).…”

Section: Involvement Of Bacterial Components In Immunopathogenesis Anmentioning

confidence: 99%

“…167 The proteolytic activities of the virulence factors of P. gingivalis have been shown to degrade apolipoproteins essential for normal lipoprotein metabolism, producing proinflammatory and proarthritogenic events that could account for increased risk of atherosclerosis. 162 The proteolysis of human fibrinogen through the combined effect of PPAD and RgpB inhibits fibrin polymerization, which results in localized bleeding and a potentially dysregulated coagulation cascade. 168 Rgp is able to activate platelets via platelet activation receptors one (PAR-1) and four (PAR-4).…”

Section: Involvement Of Bacterial Components In Immunopathogenesis Anmentioning

confidence: 99%

The Central Role of Acute Phase Proteins in Rheumatoid Arthritis: Involvement in Disease Autoimmunity, Inflammatory Responses, and the Heightened Risk of Cardiovascular Disease

Bezuidenhout

Pretorius

2020

Semin Thromb Hemost

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Rheumatoid arthritis (RA) is an autoimmune disease of complex etiopathogenic origin and traditionally characterized by chronic synovitis and articular erosions. Furthermore, there is strong evidence that infectious agents, including those that become dormant within the host, play a major role in much of the etiology of RA and its hallmark of inflammation. A combination of genetic predisposition, environmental exposure, and presence of infectious agents may therefore lead to a loss of immune tolerance to citrullinated proteins, which present as self-antigens to the human immune system. This results in generation of highly RA-specific autoantibodies, known as anti-citrullinated protein antibodies (ACPAs). Protein citrullination occurs via posttranslational deamination of arginine residues by peptidylarginine deiminase enzymes, which have confirmed sources of both endogenous and infectious origins. A recognized plasma protein target of citrullination and RA autoantibody generation is fibrin and its soluble precursor fibrinogen, both key components of hemostasis and acute phase reaction. Increased titers of ACPAs that accompany rapid progression to clinical RA disease have been shown to drive a variety of proinflammatory processes, and therefore results in aberrant fibrin clot formation and increased cardiovascular risk. However, the full extent to which hemostasis is affected in RA remains controversial, owing to the differential impact that citrullinated fibrin(ogen) and concurrent systemic inflammation may have on resulting hemostatic outcome. This review highlights key events in initiation of autoimmune-driven inflammatory events, including the role of bacterial infectious agents, which subsequently result in clinical RA disease and associated secondary cardiovascular disease risk, with specific focus on plasma proteins that are heavily involved throughout the immunopathological progression process.

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Lipoprotein modifications by gingipains of Porphyromonas gingivalis

Cited by 45 publications

References 49 publications

Effects of D-arginine on <i>Porphyromonas gingivalis</i> biofilm

Effects of D-arginine on <i>Porphyromonas gingivalis</i> biofilm

Porphyromonas gingivalis‐induced inflammatory responses in THP1 cells are altered by native and modified low‐density lipoproteins in a strain‐dependent manner

The Central Role of Acute Phase Proteins in Rheumatoid Arthritis: Involvement in Disease Autoimmunity, Inflammatory Responses, and the Heightened Risk of Cardiovascular Disease

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