Lipopolysaccharide biosynthesis-related genes are required for colony pigmentation of Porphyromonas gingivalis

Satô, Keiko; Kido, Nobuo; Murakami, Yukitaka; Hoover, Charles I.; Nakayama, Koji; Yoshimura, Fuminobu

doi:10.1099/mic.0.025163-0

Cited by 27 publications

(45 citation statements)

References 47 publications

(73 reference statements)

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“…Several genes, including porR, gftB, rfa, ugdA, vimE, and vimF, have shown the importance of the O side chain polysaccharide (O-LPS) and anionic polysaccharide (A-LPS) in these processes (50,53,(61)(62)(63)66). A defect in some of these genes resulted in a complete loss of surface-associated gingipain proteinases, strong autoaggregation, and a marked increase in biofilm formation.…”

Section: Discussionmentioning

confidence: 99%

VimA-Dependent Modulation of Acetyl Coenzyme A Levels and Lipid A Biosynthesis Can Alter Virulence in Porphyromonas gingivalis

et al. 2012

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The Porphyromonas gingivalis VimA protein has multifunctional properties that can modulate several of its major virulence factors. To further characterize VimA, P. gingivalis FLL406 carrying an additional vimA gene and a vimA-defective mutant in a different P. gingivalis genetic background were evaluated. The vimA-defective mutant (FLL451) in the P. gingivalis ATCC 33277 genetic background showed a phenotype similar to that of the vimA-defective mutant (FLL92) in the P. gingivalis W83 genetic background. In contrast to the wild type, gingipain activity was increased in P. gingivalis FLL406, a vimA chimeric strain. P. gingivalis FLL451 had a five times higher biofilm-forming capacity than the parent strain. HeLa cells incubated with P. gingivalis FLL92 showed a decrease in invasion, in contrast to P. gingivalis FLL451 and FLL406, which showed increases of 30 and 40%, respectively. VimA mediated coenzyme A (CoA) transfer to isoleucine and reduced branched-chain amino acid metabolism. The lipid A content and associated proteins were altered in the vimA-defective mutants. The VimA chimera interacted with several proteins which were found to have an LXXTG motif, similar to the sorting motif of Gram-positive organisms. All the proteins had an N-terminal signal sequence with a putative sorting signal of L(P/T/S)X(T/N/D)G and two unique signatures of EXGXTX and HISXXGXG, in addition to a polar tail. Taken together, these observations further confirm the multifunctional role of VimA in modulating virulence possibly through its involvement in acetyl-CoA transfer and lipid A synthesis and possibly by protein sorting. Porphyromonas gingivalis, a Gram-negative anaerobic bacterium, is one of the main etiological agents of adult periodontitis. While several virulence factors, including fimbriae (28), hemagglutinin (17), capsule (4), and lipopolysaccharide (68), have been implicated in the pathogenicity of P. gingivalis, the strong proteolytic abilities of this organism are considered to be important for its survival and thus play a significant role in virulence (12, 63). The major proteases, called gingipains, consist of arginine-specific (Arg-gingipain [Rgp]) and lysine-specific (Lysgingipain [Kgp]) proteases that are both extracellular and cell membrane associated (32). The activation of these gingipains is associated with several genes, including vimA, vimE, and vimF, that modulate the posttranslational glycosylation of those proteins (44,(62)(63)(64). These genes are part of the 6. locus which has previously been shown to be important to the pathogenic potential of P. gingivalis (1,26,44,(62)(63)(64).We have demonstrated that the bcp and recA genes play the expected role in oxidative stress resistance and DNA repair, respectively (26). The association of these genes with the vim genes on the same transcriptional unit could be considered an important strategy for P. gingivalis to coordinate its oxidative stress and proteolytic activities. A response to oxidative stress will involve binding of oxygen and its toxic derivativ...

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Section: Discussionmentioning

confidence: 99%

VimA-Dependent Modulation of Acetyl Coenzyme A Levels and Lipid A Biosynthesis Can Alter Virulence in Porphyromonas gingivalis

et al. 2012

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“…These gingipain adhesin complexes are anchored by cell surface polysaccharides. The porR related to the biosynthesis of APS 12 , vimA 13 , vimE, vimF putative glycosyltransferase 14 , rfa related to the biosynthesis of lipopolysaccharides LPS and APS 15 , gtfB glycosyltransferase 16 , and PG1051 putative O antigen ligase 17 genes were identified as being associated with the biosynthesis of LPS and or cell surface polysaccharides that can function as anchorage points for gingipain adhesin complexes. Gingipain activity was detected in the supernatant but not in intact cells.…”

Section: P Gingivalis Genes Involved In Colonial Blackmentioning

confidence: 99%

Por Secretion System of Porphyromonas gingivalis

Satô

2011

Journal of Oral Biosciences

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“…The porR, vimA, vimE, vimF, rfa, and ugdA genes, mutants of which lose colonial pigmentation, appear to be involved in the formation of extracellular polysaccharides and glycan additions of gingipain-adhesin complexes, resulting from a lack of immunoreactivity to MAb 1B5, which reacts with anionic surface polysaccharide (APS) (51,56,(62)(63)(64). Also, Chen et al (5) isolated a nonpigmented mutant having a transposon insertion at a gene homologous to a glycosyl (rhamnosyl) transferaseencoding gene that showed reduced levels of Rgp activity and hemagglutination.…”

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“…Colonial pigmentation is caused by accumulation of -oxo heme dimer on the cell surface (58). Nonpigmented mutants of P. gingivalis have been isolated and characterized by a number of researchers (5,17,51,56,(62)(63)(64). Colonial pigmentation on blood agar plates has been shown to be linked with hemagglutination and activities of major proteinases, Arggingipain (Rgp) and Lys-gingipain (Kgp), and other virulence factors, suggesting that colonial pigmentation is associated with the presence of gingipain-adhesin complexes on the cell surface (3,11,60).…”

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APorphyromonas gingivalisMutant Defective in a Putative Glycosyltransferase Exhibits Defective Biosynthesis of the Polysaccharide Portions of Lipopolysaccharide, Decreased Gingipain Activities, Strong Autoaggregation, and Increased Biofilm Formation

et al. 2010

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The Gram-negative anaerobic bacterium Porphyromonas gingivalis is a major pathogen in periodontal disease, one of the biofilm-caused infectious diseases. The bacterium possesses potential virulence factors, including fimbriae, proteinases, hemagglutinin, lipopolysaccharide (LPS), and outer membrane vesicles, and some of these factors are associated with biofilm formation; however, the precise mechanism of biofilm formation is still unknown. Colonial pigmentation of the bacterium on blood agar plates is related to its virulence. In this study, we isolated a nonpigmented mutant that had an insertion mutation within the new gene Porphyromonas gingivalis is a major pathogen in severe forms of periodontal disease and refractory periapical perodontitis (28,39). This Gram-negative anaerobic bacterium possesses several virulence factors, including fimbriae, proteinases, hemagglutinin, lipopolysaccharide (LPS), and outer membrane vesicles (7,13,16,27). P. gingivalis forms black-pigmented colonies on blood agar plates. Colonial pigmentation is caused by accumulation of -oxo heme dimer on the cell surface (58). Nonpigmented mutants of P. gingivalis have been isolated and characterized by a number of researchers (5,17,51,56,(62)(63)(64). Colonial pigmentation on blood agar plates has been shown to be linked with hemagglutination and activities of major proteinases, Arggingipain (Rgp) and Lys-gingipain (Kgp), and other virulence factors, suggesting that colonial pigmentation is associated with the presence of gingipain-adhesin complexes on the cell surface (3,11,60).Pigmentation-related genes that have been characterized are classified into three categories: gene expression, membrane translocation, and surface attachment of gingipain-adhesin complexes (51). Gingipain-adhesin complexes comprise Rgp and Kgp proteinases encoded by rgpA, rgpB, and kgp and adhesins encoded by rgpA, kgp, and hagA. kgp single and rgpA rgpB kgp triple mutants form less-and nonpigmented colonies, respectively, whereas an rgpA rgpB double mutant forms pigmented colonies (42, 55). Smalley et al. (59) found that Rgp activity is crucial for converting oxyhemoglobin into the methemoglobin form, which is rendered more susceptible to Kgp degradation for the eventual release of iron(III) protoporphyrin IX and production of -oxo heme dimer. A defect in membrane translocation of gingipain-adhesin complexes causes nonpigmentation. The three genes porT, sov, and PG0027, mutants of which exhibit nonpigmentation, have been reported to be involved in membrane translocation of gingipain-adhesin complexes (18,49,53). High-molecularweight forms of Rgp, Kgp, and adhesins accumulate in the periplasmic space of those mutants (49,53). Very recently, we found a novel protein secretion system, the Por secretion system (PorSS), mediating secretion for gingipain-adhesin complexes, and the porK, porL, porM, porN, porP, porQ, porU, porW, porX, and porY genes have been added to this category (52).

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Lipopolysaccharide biosynthesis-related genes are required for colony pigmentation of Porphyromonas gingivalis

Cited by 27 publications

References 47 publications

VimA-Dependent Modulation of Acetyl Coenzyme A Levels and Lipid A Biosynthesis Can Alter Virulence in Porphyromonas gingivalis

VimA-Dependent Modulation of Acetyl Coenzyme A Levels and Lipid A Biosynthesis Can Alter Virulence in Porphyromonas gingivalis

Por Secretion System of Porphyromonas gingivalis

APorphyromonas gingivalisMutant Defective in a Putative Glycosyltransferase Exhibits Defective Biosynthesis of the Polysaccharide Portions of Lipopolysaccharide, Decreased Gingipain Activities, Strong Autoaggregation, and Increased Biofilm Formation

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