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Jolene Sim

Bench E

31 August 2016 [1]


Higher order taxa

Bacteria – Bacteria – Bacteroidetes – Bacteroidia – Bacteroidales – Porphyromonadaceae – Porphyromonas [1]


Species name: Porphyromonas gingivalis

Type strain: W83, 381, 2526, ATCC 33277, BCRC 14417, CCRC 14417, CCUG 25893, CCUG 25928, CIP 103683, Coykendall 2561, DSM 20709, JCM 12257, KCTC 5121, KDI, NCTC 11834, Slots 2561, SU63, W50. [2]

Description and significance

Porphyromonas gingivalis (P. gingivalis) is a non-motile, asaccharolytic, rod-shaped gram negative bacteria. It is obligately anaerobic, requiring iron for growth and forms black-pigmented colonies on blood agar plates. P. gingivalis is significant in pathogenesis and progression of inflammations in periodontal diseases. It is detected in 85.7% of subgingival plaque samples from chronic periodontal patients. Disease initially occurs as acute inflammation of gingival tissue, untreated infections progressively cause formation of teeth pockets and loss of teeth. Habitat of P. gingivalis is subgingival sulcus of human oral cavity, serving as secondary colonizer of dental plaques by attaching onto primary colonizers such as Streptococcus gordonii and P. intermedia. [3] It functions to produce a variety of potential virulence factors as significant pathogen in progression of health to disease. [4] Besides gingival sulcular epithelial cells, P. gingivalis is able to attach onto human buccal epithelial cells in vitro. [5] Adding on, it causes non-oral infections such as endocarditis and abscesses in lung, head, neck and abdominal area. [6] P. gingivalis has also been cultured to study its significance in attachment and invasion of host cells [4], and internalization within host cells. [5]

Genome structure

P. gingivalis strain W38 has a genome structure of 2,343,479 bp consisting of an average GC content of 48.3%. It contains 4 ribosomal operons (5S-23S-tRNA Ala-tRNA Ile-tRNA 16S), 2 structural RNA genes, 53 tRNA genes coding for all 20 amino acids. P. gingivalis genes encode 3 restriction system proteins (PG0971, PG0968, PG1469), hemagglutinin proteins B and C (Hag B, PG1972, Hag C, PG1975), various capsular synthesis proteins, 20 transposase genes and 2 large mobile elements (PG1473 to PG1480). [7]

Cell structure and metabolism

Cell Wall

P. gingivalis uses its cell wall to attach and provide resistance to saliva flow, mediated by adhesins on surface of bacteria and receptors on oral surfaces. These adhesins are associated with cell structures such as capsules and fimbriae of P. gingivalis. Cell wall consists of distal polysaccharide (O-antigen), a non-repeating core oligosaccharide and a hydrophobic domain known as lipid A (endotoxin). Lipid A is the biological active site of lipopolysaccharide (LPS) that causes deregulation of mammalian innate immune system by interacting with both toll-like receptors 2 and 4. Lipid A has different acylation patterns that change according to microenvironmental conditions, affecting host immune signaling to facilitate bacterial survival in hosts. LPS of gram-negative bacteria is significant in maintaining cellular and structural integrity, as well as controlling entry of hydrophobic molecules and toxic chemicals. P. gingivalis LPS also inhibits osteoblastic differentitation and mineralization in periodontal ligament stem cells for periodontal tissue regeneration. [3]

Biofilm Formation

P. gingivalis utilizes biofilm to aid in the inflammatory responses of hosts in periodontal diseases. It was shown that P. gingivalis encodes a ppk gene for polyphosphate kinase activity for biofilm formation. [8] Adding on, studies have demonstrated that the bacteria uses luxS-based communication for biolfim formation, via quorum-sensing systems using autoinducer (AI) peptides. P. gingivalis and Streptococcus gordonii are involved in the mixed-species biofilm formation through LuxS-based communication, whereby Streptococcus gordonii consists of functional luxS gene as well. [9]


P. gingivalis is a non-motile bacterium. [3]

Metabolic Functions

P. gingivalis has a limited capacity to take up and metabolize organic nutrients. Glucose used by P. gingivalis is not demonstrated strongly, and carbohydrates so not aid in increased growth. To account for that, strain W83 has putative open reading frames (ORFs) for all enzymes necessary for glycolysis. 4 putative ORFs of pentose-phosphate pathway were recognized and it is very likely that P. gingivalis uses this pathway to generate metabolites for anaerobic growths. [10]


Major habitat of P. gingivalis is subgingival sulcus of human oral cavity. [3] It requires amino acid fermentation to produce energy needed for surviving in deep periodontal pocket, with low sugar availability. [3] P. gingivalis is usually found in periodontal pockets, but can be potentially found in supragingival plaque and oral mucosal surfaces, dorsum of tongue, and pharynx. P. gingivalis/host interaction is amphibiosis, where recent relationship between host and microbe can change, which in this case P. gingivalis increases along with dental plaques. Host physiological processes such as cell activation, proliferation, differentiation, metabolism and cellular motilities need cell-to-extracellular matrix (ECM) contacts. Cellular integrins function as ECM protein receptors for linkages between extracellular environment and intracellular cytoskeleton. ECM proteins in periodontal pocket fluid include vitronectin and fibronectin. Vitronectin protects gingival epithelium and connective tissues against periodontal damages. Fibronectin is significant in proliferation and chemotaxis of periodontal ligament cells. P. gingivalis binds ECM proteins through its fimbriae and outer membrane proteins, inhibiting ECM proteins from functioning, therefore slowing recovery processes caused by periodontal tissue destructions. P. gingivalis binds to β2 integrin on mouse peritoneal macrophages, leading to expressions of interleukin (IL)-1β and tumor necrosis factor (TNF)-α genes. Arginine-specific protease (Arg-gingipain) complex of P. gingivalis disrupts fibronectin and its receptor, blocking receptor-ligand interactions of human host fibroblasts. [11] This leads to inhibition of cellular signal transduction, enhancing tissue destruction. [3] P. gingivalis internalizes into host gingival epithelial and endothelial cells through membrane ruffles. These ruffles surround the bacteria, therefore internalizing it and exist as vacuoles to replicate and persist within these cells. Intracellular environment provides nutrients for P. gingivalis growth, and serves as protection against host immune system. P. gingivalis fimA genes have 5 variants (type I to V), classified based on nucleotide sequences. Polymerase chain reaction (PCR) is used to detect P. gingivalis variants in saliva and periodontal samples. It was shown that majority of samples collected contained type II fimA, and followed by type IV. On the contrary, type I was found in healthy individuals. Type III and V were less prevalent in the samples. These illustrate presence of disease and non-disease causations of P. gingivalis, where fimbriae variations are associated with bacterial infections, affecting disease development. Type II fimA was also observed to invade rapidly into host epithelial cells, promoting P. gingivalis invasion. [11]


The bacteria has also been identified as risk factor for coronary heart disease, pulmonary infections and pre-term, low birth weight deliveries. [11] P. gingivalis produces variety of virulence factors to penetrate gingivae and causes tissue destruction directly or indirectly, by inducing inflammation. These virulence factors are constituents or metabolites important in different stages of life cycle,causing damage in hosts. To survive and multiply in hosts, P. gingivalis has to overcome host external protective barrier before finding suitable environment for colonization, occuring only in presence of virulence factors such as fimbriae, capsules, lipopolysaccharide (LPS), lipoteichoic acids, haemagglutinins, gingipains, outer membrane proteins and outer membrane vesicles. Expression of viulence factors is regulated in response to external environment changes of peridontopathogen. [3]

Application to biotechnology


Periodontal tissue engineering involves repairing of alveolar bone, tooth-associated cementum and periodontal ligament (PDL). Regeneration of periodontal tissues depends on appropriate signals, cells, blood supply and scaffold necessary for targeting tissue defects. Appropriate signals such as growth factors, regulate cellular activities, providing signals for cell differentiation and produce matrix for developing tissues. Cells serve as machinery for new tissue growths and differentiation. Scaffolds serves as structural template for processes in periodontal tissue regeneration. Studies have shown that enamel matrix derivative (EMD), a bioactive molecule, can promote periodontal wound repairing by regenerating periodontal tissues. [12]

Biotechnologically relevant enzyme/compound production

Major arginine-specific cysteine proteinase of P. gingivalis, RGP-1 can be generated as polypeptides to function as erythrocyte-binding protein through various adhesion domains at the carboxyl terminus. [13]

Drug Targets

Nasal immunization with hemin-binding protein and cholera toxin exhibit immune response against P. gingivalis in young and aged mice, and preventing atherosclerosis. Nasal delivery of OM protein can be a potential vaccine strategy in providing protective immunity to human to prevent periodontitis. Plant-derived bioactive compunds as therapeutic roles to regulate interactions between microorganisms have been widely used and is non-toxic towards human cells. An anthraquinone from rhubarb roots, rhein, shows antibacterial synergistic effect when used together with other polyphenols. It downregulates rgpA and Kgp proteases genes associated with inactivation of host defense. Main polyphenols in black tea, theaflavins, inhibit P. gingivalis proteinase activities based on dosages. KYT-41, a synthetic dual protease inhibitor, inhibiting Rgp and Kgp of P. gingivalis. Also, it displays anti-inflammatory activity, which can be a potential treatment for gingivitis. [3]

Current research

Inhibitory effect of grape seed proanthocyanidin extracts can inhibit P. gingivalis LPS. Roles of α-tocopherol in countering damaging effect of LPS decreased inflammatory cytokines, increasing β-defensins, promoting gingival fibroblast growth and migration. Tormentic acid inhibits LPS-induced inflammatory response in human gingival fibroblasts. Differences in LPS profile of P.gingivalis affects colony morphology and polymyxin B resistance. Unlike healthy individuals, periodontal isolates were resistant to polymyxin b with low aggregation ability. This resistance highly relates to variation in LPS profiles as LPS from healthy individuals lack high molecular weight O-antigen moieties and anionic polysaccharide, whereas P. gingivalis isolates from periodontal subjects produce modified lipid-A molecules. [3]P. gingivalis fimbriae activate human gingival epithelial cells, spleen cells, and peripheral blood monocytes to release interleukins and TNF-α, and these molecular interactions between P. gingivalis and human hosts are currently being investigated. [10]


References examples

1. BacMap Genome Atlas


3. How, K.Y., Song, K.P., and Chan, K.G. (2016) Porphyromonas gingivalis: An overview of periodontal pathogen below the gum line. Front Microbiol 7: 1-14.

4. Dorn, B.R., Burks, J.N, Seifert, K.N., and Progulske-Fox, A. (2000) Invasion of endothelial and epithelial cells by strains of Porphyromonas gingivalis.FEMS Microbiology Letters 187: 139-144.

5. Lamont, R.J., Oda, D., Persson, R.E., and Persson, G.R. (1992) Interaction of Porphyromonas gingivalis with gingival epithelial cells maintained in culture. Oral Microbiol Immunol. 7: 364-367.

6. Asikainen, S., and Chen, C. (2000) Oral ecology and person-to-person transmission of Actinobacillus actinomycetemcomitans and Povphyromonas gingivalis. Periodontology 20: 65-81.

7. Nelson, K.E., Fleischmann, R.D., Deboy, R.T., Paulsen, I.T., Fouts, D.E., Eisen, J.A., et all. (2013) Complete Genome Sequence of the Oral Pathogenic Bacterium Porphyromonas gingivalis;; Strain W83. J Bacteriol 185: 5591-5601.

8. [ Kuramitsu, H., Chen, W., and Ikegami, A. (2005) Biofilm Formation by the Periodontopathic Bacteria Treponema denticola and Porphyromonas gingivalis. J Periodontol 76: 2047-2051.]

9. [ McNab, R., Ford, S.K., El-sabaeny, A., Barbieri, B., Cook, G.S., and Lamont, R.J. (2003) LuxS-Based Signaling in Streptococcus gordonii: Autoinducer 2 Controls Carbohydrate Metabolism and Biofilm Formation with Porphyromonas gingivalis 185: 274-284.]

10. Amano, A. (2003) Molecular Interaction of Porphyromonas gingivalis with Host Cells: Implication for the Microbial Pathogenesis of Peridontal Disease. J Periodontol 74: 90-96.

11. Yilmaz, O. (2008) The chronicles of Porphyromonas gingivalis: the microbium, the human oral epithelium and their interplay. 154: 2897-2903.

12. Taba, M.Jr., Jin, Q., Sugai, J.V., and Giannobile, W.V. (2005) Current concepts in periodontal bioengineering.8: 292-302.

13. Pavloff, N., Potempa, J., Pike, R.N., Prochazka, V., Kiefer, M.C., Travis, J., and Barr, P.J. (1995) Molecular cloning and structural characterisation of the Arg-gingipain proteinase of Porphyromonas gingivalis. 270: 1007-1010.

  1. MICR3004

This page is written by Jolene Sim for the MICR3004 course, Semester 2, 2016