Identification of lipopolysaccharide binding site on high molecular weight kininogen

Perkins, Ryan; Ngo, My-Linh; Mahdi, Fakhri; Shariat‐Madar, Zia

doi:10.1016/j.bbrc.2007.12.042

Cited by 12 publications

(11 citation statements)

References 22 publications

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“…Tight binding of HK to E. coli LPS has been reported recently (60). In this study, however, we have found that LPS isolated from P. gingivalis did not show any remarkable affinity to HK or FXII (Fig.…”

Section: Discussionsupporting

confidence: 40%

Adsorption of Components of the Plasma Kinin-Forming System on the Surface ofPorphyromonas gingivalisInvolves Gingipains as the Major Docking Platforms

et al. 2011

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Enhanced production of proinflammatory bradykinin-related peptides, the kinins, has been suggested to contribute to the pathogenesis of periodontitis, a common inflammatory disease of human gingival tissues. In this report, we describe a plausible mechanism of activation of the kinin-generating system, also known as the contact system or kininogen-kallikrein-kinin system, by the adsorption of its plasma-derived components such as high-molecular-mass kininogen (HK), prekallikrein (PK), and Hageman factor (FXII) to the cell surface of periodontal pathogen Porphyromonas gingivalis. The adsorption characteristics of mutant strains deficient in selected proteins of the cell envelope suggested that the surface-associated cysteine proteinases, gingipains, bearing hemagglutinin/adhesin domains (RgpA and Kgp) serve as the major platforms for HK and FXII adhesion. These interactions were confirmed by direct binding tests using microplate-immobilized gingipains and biotinylated contact factors. Other bacterial cell surface components such as fimbriae and lipopolysaccharide were also found to contribute to the binding of contact factors, particularly PK. Analysis of kinin release in plasma upon contact with P. gingivalis showed that the bacterial surface-dependent mechanism is complementary to the previously described kinin generation system dependent on HK and PK proteolytic activation by the gingipains. We also found that several P. gingivalis clinical isolates differed in the relative significance of these two mechanisms of kinin production. Taken together, these data show the importance of this specific type of bacterial surface-host homeostatic system interaction in periodontal infections.

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Section: Discussionsupporting

confidence: 40%

Adsorption of Components of the Plasma Kinin-Forming System on the Surface ofPorphyromonas gingivalisInvolves Gingipains as the Major Docking Platforms

et al. 2011

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“…Thus, the role of the contact system could be to promote a developing thrombus, which may provide a surface for assembly of the contact factors (32). Different surface molecules interact with HK, such as curli, fibrous proteins of Escherichia coli and Salmonella enterica serovar Typhimurium, the M protein of Streptococcus pyogenes (2,3), gingipains of Porphyromonas gingivalis (29), and lipopolysaccharide (26). Different regions of the HK molecule have been shown to bind to various cellular surfaces; domains D3, D4, and D5 of HK bind to platelets or endothelial cells (10)(11)(12)32), and D5 mediates binding and subsequent contact activation at bacterial surfaces (3,20).…”

mentioning

confidence: 99%

Activation of the Contact System at the Surface of Fusobacterium necrophorum Represents a Possible Virulence Mechanism in Lemièrre's Syndrome

et al. 2011

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Fusobacterium necrophorum causes Lemièrre's syndrome, a serious disease with septic thrombophlebitis of the internal jugular vein, pulmonary involvement, and systemic inflammation. The contact system is a link between inflammation and coagulation, and contact activation by the bacteria could therefore contribute to the abnormal coagulation and inflammation seen in patients with Lemièrre's syndrome. In this study, F. necrophorum was found to bind radiolabeled high-molecular-weight kininogen (HK), a central component of the contact system. Binding was inhibited by the addition of unlabeled HK and domain D5 of HK but not other components of the contact system, indicating a specific interaction mediated through the D5 region. Binding of HK was significantly reduced after pretreatment of the bacteria with trypsin, suggesting that surface proteins are involved in HK binding. Incubation of the bacteria with human plasma resulted in an HK breakdown pattern suggestive of bradykinin release, and bradykinin was also detected in the supernatant. In addition, we show that factor XI (FXI), another component of the contact system, binds to F. necrophorum and that the bound FXI reconstitutes the activated partial thromboplastin time of FXI-deficient plasma. Thrombin activity was detected at the surface of the bacteria following incubation with plasma, indicating that the intrinsic pathway of coagulation is activated at the surface. This activity was completely blocked by inhibitors of the contact system. The combined results show that the contact system is activated at the surface of F. necrophorum, suggesting a pathogenic role for this system in Lemièrre's syndrome.

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“…All contact factors were assembled on these fibrous structures and mutant strains lacking either curli or fimbriae did not activate the cascade (Ben Nasr et al, 1996;Herwald et al, 1998). Also LPS was described to provide a surface for contact activation by binding to domain 5 in HK, which is responsible for binding to negatively charged surfaces (Perkins et al, 2008). For S. aureus it was proposed that negatively charged teichoic acids induce contact activation (Kalter et al, 1983;Mattsson et al, 2001).…”

Section: Contact Activation On Bacteriamentioning

confidence: 99%

Bacteria under stress by complement and coagulation

Berends¹,

Kuipers²,

Ravesloot³

et al. 2014

FEMS Microbiol Rev

103

108

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The complement and coagulation systems are two related protein cascades in plasma that serve important roles in host defense and hemostasis, respectively. Complement activation on bacteria supports cellular immune responses and leads to direct killing of bacteria via assembly of the Membrane Attack Complex (MAC). Recent studies have indicated that the coagulation system also contributes to mammalian innate defense since coagulation factors can entrap bacteria inside clots and generate small antibacterial peptides. In this review, we will provide detailed insights into the molecular interplay between these protein cascades and bacteria. We take a closer look at how these pathways are activated on bacterial surfaces and discuss the mechanisms by which they directly cause stress to bacterial cells. The poorly understood mechanism for bacterial killing by the MAC will be reevaluated in light of recent structural insights. Finally, we highlight the strategies used by pathogenic bacteria to modulate these protein networks. Overall, these insights will contribute to a better understanding of the host defense roles of complement and coagulation against bacteria.

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Identification of lipopolysaccharide binding site on high molecular weight kininogen

Cited by 12 publications

References 22 publications

Adsorption of Components of the Plasma Kinin-Forming System on the Surface ofPorphyromonas gingivalisInvolves Gingipains as the Major Docking Platforms

Adsorption of Components of the Plasma Kinin-Forming System on the Surface ofPorphyromonas gingivalisInvolves Gingipains as the Major Docking Platforms

Activation of the Contact System at the Surface of Fusobacterium necrophorum Represents a Possible Virulence Mechanism in Lemièrre's Syndrome

Bacteria under stress by complement and coagulation

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