Interaction of Porphyromonas gingivalis with transferrin

Tazaki, Katsuko; Inoshita, Eiji; Amano, Atsuo; Hanioka, Takashi; Tamagawa, Hiroo; Shizukuishi, Satoshi

doi:10.1016/0378-1097(95)00253-2

Cited by 12 publications

(13 citation statements)

References 29 publications

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“…In addition to hemin-and hemecontaining proteins, P. gingivalis can utilize nonhemin iron source transferrin for growth (5,7,24,54,59). However, specific receptors for transferrin in this organism have not been described.…”

Section: Resultsmentioning

confidence: 99%

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Degradation of Host Heme Proteins by Lysine- and Arginine-Specific Cysteine Proteinases (Gingipains) of Porphyromonas gingivalis

et al. 2001

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Porphyromonas gingivalis can use hemoglobin bound to haptoglobin and heme complexed to hemopexin as heme sources; however, the mechanism by which hemin is released from these proteins has not been defined. In the present study, using a variety of analytical methods, we demonstrate that lysine-specific cysteine proteinase of P. gingivalis (gingipain K, Kgp) can efficiently cleave hemoglobin, hemopexin, haptoglobin, and transferrin. Degradation of hemopexin and transferrin in human serum by Kgp was also detected; however, we did not observe extensive degradation of hemoglobin in serum by Kgp. Likewise the ␤-chain of haptoglobin was partially protected from degradation by Kgp in a haptoglobin-hemoglobin complex. Arginine-specific gingipains (gingipains R) were also found to degrade hemopexin and transferrin in serum; however, this was observed only at relatively high concentrations of these enzymes. Growth of P. gingivalis strain A7436 in a minimal media with normal human serum as a source of heme correlated not only with the ability of the organism to degrade hemoglobin, haptoglobin, hemopexin, and transferrin but also with an increase in gingipain K and gingipain R activity. The ability of gingipain K to cleave hemoglobin, haptoglobin, and hemopexin may provide P. gingivalis with a useable source of heme for growth and may contribute to the proliferation of P. gingivalis within periodontal pockets in which erythrocytes are abundant.

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Section: Resultsmentioning

confidence: 99%

“…gingivalis can utilize several different iron sources for bacterial growth including hemin, hemoglobin, and transferrin (5,7,18,24,54,59). Hemoglobin has been reported to be more effective in supporting the growth of P. gingivalis than hemin or transferrin (53,54).…”

Section: Discussionmentioning

confidence: 99%

Degradation of Host Heme Proteins by Lysine- and Arginine-Specific Cysteine Proteinases (Gingipains) of Porphyromonas gingivalis

et al. 2001

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“…Kesavalu et al (8) demonstrated that P. gingivalis cells grown under iron-depleted conditions for multiple passages showed significantly decreased lesion size in mice, in contrast to cells grown under iron-normal and iron-elevated conditions. Conversely, other reports have shown increases in virulence under hemin limitation (11)(12)(13)(14). The binding (12) and transferring (13) of hemoglobin increased considerably when the organisms were grown under hemin-limited conditions, and collagenolytic activity was generally higher in heminlimited cultures (11).…”

Section: Introductionmentioning

confidence: 82%

Gene expression profiling and characterization under hemin limitation in Porphyromonas gingivalis

2005

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Hemin is an important nutrient forPorphyromonas gingivalis growth and pathogenicity. We examined the gene expression profile of P. gingivalis, including genes involved in its pathogenicity, at various growth stages under hemin-standard and limited conditions by using a custom-made microarray. The transcription of many genes decreased after late-log and mid-log phases under hemin-standard and limited conditions, respectively. We focused on two groups of genes while comparing gene expression profiles under hemin-standard and limited conditions by gene tree analysis. Genes belonging to group A maintained high transcriptional levels, whereas genes in group B were expressed at low levels under standard hemin conditions. However, group B genes increased remarkably under hemin-limited conditions. Groups A and B contained genes involved in regulatory functions and protein fate, respectively. Genes related to energy metabolism, transport, and protein binding were present in both groups. Our results suggest that P. gingivalis experienced severe stress under hemin-limited conditions, and growth phase-dependent changes in transcription levels were observed for many genes. Moreover, increased expression of genes involved in energy metabolism suggests that hemin is related not only to pathogenicity, but also energy metabolism. (J. Oral Sci. 47,[191][192][193][194][195][196][197] 2005)

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“…This indicates that the iron and the porphyrin ring (i.e., the entire heme moiety) are taken into the P. gingivalis cell [43]. Iron-saturated transferrin was found to support the long-term growth of P. gingivalis [78,83,84]. This protein is found in large amounts in gingival crevicular fluid from patients with destructive periodontitis [80,81].…”

Section: Iron/heme Requirements For P Gingivalis Growthmentioning

confidence: 99%

“…In addition to heme, transferrin may represent one of the most important sources of iron for P. gingivalis. Tazaki et al [84] found that the binding of human transferrin to P. gingivalis cells occurred rapidly, reversibly and specifically (K d = 1.4 · 10 À6 M). Iron-saturated transferrin was found to support the long-term growth of P. gingivalis [78,83,84].…”

Section: Iron/heme Requirements For P Gingivalis Growthmentioning

confidence: 99%

Iron and heme utilization inPorphyromonas gingivalis

et al. 2005

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Porphyromonas gingivalis is a Gram-negative anaerobic bacterium associated with the initiation and progression of adult periodontal disease. Iron is utilized by this pathogen in the form of heme and has been shown to play an essential role in its growth and virulence. Recently, considerable attention has been given to the characterization of various secreted and surface-associated proteins of P. gingivalis and their contribution to virulence. In particular, the properties of proteins involved in the uptake of iron and heme have been extensively studied. Unlike other Gram-negative bacteria, P. gingivalis does not produce siderophores. Instead it employs specific outer membrane receptors, proteases (particularly gingipains), and lipoproteins to acquire iron/heme. In this review, we will focus on the diverse mechanisms of iron and heme acquisition in P. gingivalis. Specific proteins involved in iron and heme capture will be described. In addition, we will discuss new genes for iron/heme utilization identified by nucleotide sequencing of the P. gingivalis W83 genome. Putative iron- and heme-responsive gene regulation in P. gingivalis will be discussed. We will also examine the significance of heme/hemoglobin acquisition for the virulence of this pathogen.

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Interaction of Porphyromonas gingivalis with transferrin

Cited by 12 publications

References 29 publications

Degradation of Host Heme Proteins by Lysine- and Arginine-Specific Cysteine Proteinases (Gingipains) of Porphyromonas gingivalis

Degradation of Host Heme Proteins by Lysine- and Arginine-Specific Cysteine Proteinases (Gingipains) of Porphyromonas gingivalis

Gene expression profiling and characterization under hemin limitation in Porphyromonas gingivalis

Iron and heme utilization inPorphyromonas gingivalis

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