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Year : 2015  |  Volume : 7  |  Issue : 1  |  Page : 51-58

Porphyromonas gingivalis : Its virulence and vaccine

1 Department of Periodontology and Oral Implantology, Dayanand Anglo Vedic Centenary Dental College (D.A.V. ©Dental College), Yamuna Nagar, Haryana, India
2 Department of Periodontology and Oral Implantology, Government Dental College and Hospital, Jamnagar, Gujarat, India

Date of Web Publication18-Mar-2015

Correspondence Address:
Dr. Priyanka Tikoo
H.No. 2001, Sector 17, Huda, Jagadhri - 135 003, Haryana
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Source of Support: None, Conflict of Interest: None

DOI: 10.4103/2231-0754.153496

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Background: The microbial florae in adult periodontitis lesions are comprised of anaerobic rods with Porphyromonas gingivalis as one of the major components (Slots 1976; Slots 1979; and Tanner et al., 1979). P. gingivalis is a black-pigmented gram-negative anaerobic rod and a secondary colonizer of dental plaque requiring antecedent organisms. The presence of this organism either alone or as a mixed infection with other bacteria and with the absence of beneficial species appears to be essential for disease activity. It is a predominant member of the subgingival microbiota in disease. It possesses and "excretes" numerous potentially toxic virulence factors. Aim of this study is to perform a systematic review of studies on P. gingivalis and its virulence factors with a special focus on its vaccine. Materials and Methods: An electronic and manual search based on agreed search phrases between the primary investigator and a secondary investigator was performed for the literature review till January 2014. The articles that were identified by this systematic review (total of 190) were analyzed in detail, which included the study of inference and conclusion. Conclusions: Within the limits of this systematic review, it can be concluded that P. gingivalis induce immune inflammatory response in periodontitis subjects. Therapeutic vaccines need to be developed and studied for their efficacy in controlling periodontitis.

Keywords: Gingipains, host cells, P. gingivalis, virulence factors

How to cite this article:
Pandit N, Changela R, Bali D, Tikoo P, Gugnani S. Porphyromonas gingivalis : Its virulence and vaccine. J Int Clin Dent Res Organ 2015;7:51-8

How to cite this URL:
Pandit N, Changela R, Bali D, Tikoo P, Gugnani S. Porphyromonas gingivalis : Its virulence and vaccine. J Int Clin Dent Res Organ [serial online] 2015 [cited 2023 Mar 27];7:51-8. Available from: https://www.jicdro.org/text.asp?2015/7/1/51/153496

   Introduction Top

Porphyromonas gingivalis , a black-pigmented gram-negative anaerobic rod, has been implicated as a major pathogen of chronic periodontitis. Recent studies using deoxyribonucleic acid (DNA) hybridization also indicated the increased prevalence of P. gingivalis as well as other 'red complex species' (P. gingivalis, Treponema denticola, and Tannerella forsythia) in the subjects with chronic periodontitis. [1] It is also evident that the colonization of the putative pathogenic bacteria in subgingival plaque is not sufficient for the initiation/onset of periodontitis as most periodontopathic bacteria including P. gingivalis may also be present at healthy sites (around 11.2 times less in healthy sites than periodontitis). [2] Thus, the onset and progress of chronic periodontitis is based on the balance between the pathogenesis of the periodontopathic microorganisms and the host-defense against them [Figure 1].
Figure 1: Petridish showing colonies of Porphyromonas gingivalis

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The complex interaction to the host response fundamentally responsible for chronic periodontitis cannot be reproduced in vitro. The studies with animal models that P. gingivalis can induce experimental periodontitis with alveolar bone losses clearly indicate that  P.gingivalis Scientific Name Search  is a major causative pathogen of chronic periodontitis. [3] Its pathogenic factors could be potentially involved solely or cooperatively in every step of the onset and progression of the disease. The virulence factors of P. gingivalis including fimbriae, hemagglutinin, capsule, lipopolysaccharide (LPS), outer membrane vesicles, organic metabolites such as butyric acid, and various enzymes such as Arg- and Lys-gingipains, collagenase, gelatinase, and hyaluronidase, could contribute to the induction of chronic periodontitis in diverse ways. [3]

Virulence factors

Virulence factors are described as molecules that result in the establishment and maintenance of a species associated with or within the confines of a host. [4] Virulence factors are classically believed to harm the host, but they can also function in the establishment of a symbiotic or parasitic relationship between the bacterial species and the host.

Virulence factors of P. gingivalis

  • Involved in colonization and attachment:

    • Fimbriae
    • Hemagglutinins
    • Outer membrane proteins and vesicles
    • Gingipains
  • Involved in evading (modulating) host responses:

    • Capsule
    • LPS
    • Ig and complement proteases, otherantiphagocytic products
    • Fimbriae
  • Involved in damaging host tissues and spreading:

    • Proteinases (Arg- and Lys-gingipains)
    • Collagenase
    • Fibrinolytic, keratinolytic, and other hydrolytic enzymes.

   Involved in Colonization and Attachment Top

Bacterial fimbriae

Structure and situation: Fimbriae or pili are proteinaceous, filamentous appendages that protrude outwards from the bacterial cell surface. [5] With only one or two exceptions, all of the P. gingivalis strains so far examined contain fimbriae arranged in a peritrichous fashion over the surface of the cell. Ultrastructural examination has revealed the presence of peritrichious fimbriae, 0.3-3.0 μm long and 5 nm wide, on most strains of P. gingivalis. [6]

Types: The first fimbriae are called major, long, or FimA fimbriae, and the second ones are referred to as minor, short, or Mfa1 fimbriae. [7] The presence of more than one type of fimbriae on P. gingivalis has recently become apparent depending upon the genotype (I-V and Ib).

Fimbriae play a crucial role in virulence by stimulating bacterial attachment to host cells or tissues. Fimbriae appear to be a major adherence-mediating determinant of P. gingivalis. Immunization with purified fimbriae confers protection against periodontal destruction in a gnotobiotic rat model [8] [Figure 2].
Figure 2: Numerous thin fibrils or fimbriae (F) emerge from the surface of the cells

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The initial step of P. gingivalis attachment to the oral tissue is fimbriae-mediated. Ogawa et al., recently investigated the contribution of various regions of the fimbriae to binding to the human gingival fibroblast cell line. [9] Purified, intact, and radiolabeled fimbriae bound firmly to the surface of the fibroblasts. The synthetic peptides, when either added first to the fibroblast cells or concomitantly with the intact fimbriae, inhibited binding in a dose-dependent fashion.

In addition to mediating adherence, fimbriae have a variety of other properties (such as chemotactic properties and cytokine induction). The fimbriae werealso highly immunogenic, eliciting both an antibodyand cell-mediated response in serum and saliva. [10]


Structure and situation: Hemagglutinin proteins are important virulence factors for a number of bacterial species. These enzymes are either exposed at the surface (in the outer membrane) of the bacterium where they are able to come into contact with host cells and tissues or within the periplasmic space from where they are capable of being transported to the cell surface. [10]

Types: P. gingivalis produces at least five hemagglutinating molecules. Three hag genes encoding hemagglutinins have been cloned.

When expressed on the bacterial cell surface, hemagglutinins may promote colonization by mediating the binding of bacteria to receptors (usually oligosaccharides) on human cells. P. gingivalis binding to erythrocytes with the help of hemagglutinin may also serve a nutritional function as it utilizes heme for growth.

It is clear that basically all hemagglutinin activity is related to hemagglutinin-adhesin domains of RgpA, Kgp, and HagA. [11] Arecent study by Lepine et al., revealed 9-10 different restriction polymorphism profiles using hagC and hagA as probes. [12] These results suggest that several copies of this hemagglutinin gene are located on the chromosome of P. gingivalis.

Duncan et al., have demonstrated that the P. gingivalis hemagglutinins may also participate inthe binding of the bacterium to host cells otherthan red blood cells. [13]

Outer membrane proteins/vesicles

Structure and situation: They are released from the outer membrane proper during growth and are referred to as outer membrane vesicles. Trapped within these closed sacs are numerous enzymes that occur in the periplasmic region of the intact cell. These include phospholipase C, proesterases, alkaline phosphatase, hemolysins, and autolysins. [10] The majority of the cells' Arg-gingipain cysteine protease was localized in the outer membrane vesicles.

Vesicles are able to fuse with the outer membrane of other bacterial species, into which virulence factors are released, resulting in an impairment of target cells. Outermembrane vesicles from P. gingivalis enhance interleukin-12 induced interferon-c production by T cells, which may augment immunopathology noted in periodontitis. [14] This activity was also noted with the outer membrane from the microorganism, as well as with LPS.

   Involved in Evading Host Response Top


Structure and situation: Bacterial capsules have been considered major virulence factors on the bacterial cell surface. [10] It is formed by a polysaccharide heteropolymer on the outer membrane of the bacterial cell (Woo et al., 1979). [15] Mansheim and Kasperdetermined that the capsule of P. gingivalis 381 contained galactose, glucose, and glucosamine; [16] whereas, Okuda et al., confirmed the presence of these sugars along with rhamnose, glucose, galactose, mannose, and methylpentose. [17]

Types: Six serotypes (K1-K6) and K negative isolates have been identified based on capsular K-antigens. [18]

The presence of a capsule in P. gingivalis has been considered an important antiphagocytic virulence factor. The highly encapsulated P. gingivalis strains exhibit decreased autoagglutination, lower buoyant densities, and are more hydrophilic than the less encapsulated strains. [19],[20] Increased encapsulation is also correlated with increased resistance to phagocytosis, serum resistance, and decreased induction of polymorphonuclear leukocyte chemiluminescence. The decreased tendency for the highly encapsulated strains to be phagocytized has been proposed to be due to the increased hydrophilicity of the strains and their decreased ability to activate the alternative complement pathway.

LPS and lipid A component

Structure and situation: LPS is the major macromolecule found on the outer surface of gram-negative bacteria. LPS is typically composed of three domains: Lipid A, a short core oligosaccharide, and an O-antigen that may be a long polysaccharide. Lipid A is the innermost component of LPS. It is conserved in structure and forms the outer leaflet of the outer membrane [Figure 3].
Figure 3: Lipopolysaccharide (LPS).a = O antigen, b = core oligosaccharide, c = lipid A

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LPS is critical to the bacterium for maintaining its structural integrity, and for establishing a selective permeability barrier that limits entry of hydrophobic molecules and toxic chemicals such as detergents and antibiotics. [21] LPS is also required for the proper folding and insertion of many outer membrane proteins [Figure 4].
Figure 4: Function of LPS

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Lipid A, also known as endotoxin, is the bioactive region of LPS that is recognized by the innate immune system. P. gingivalis agonist lipid A structures induced the expression of human β-defensin-1, -2, and -3, while P. gingivalis antagonist lipid A species downregulated their expression. [22]

   Involved in Damaging Host Tissues and Spreading Top

Proteinases (gingipains)

Structure and situation: The Arg- and Lys-proteinases are cysteine proteinases and have been given the common name, gingipains. These enzymes are either exposed at the surface (in the outer membrane) of the bacterium where they are able to come into contact with host cells and tissues or within the periplasmic space capable of being transported to the cell surface, and in outer membrane vesicles, which are sloughed from the outer membrane during growth. [10]

Types: Gingipains, including arginine-specific gingipains (Arg-gingipain-A, RgpA, and Arg gingipain-B, RgpB) and lysine-specific gingipain (Lys-gingipain, Kgp), are encoded by three different genes referred to as rgpA, rgpB, and kgp [Figure 5]. [23]
Figure 5: Effects of P. gingivalisproteinases

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Function of gingipains

  • Adherence and colonization: The gingipains are themselves, potent non-fimbrial adhesins avidly binding several extracellular matrix proteins such as fibrinogen, fibronectin, laminin, and collagen type V. [24] They also apparently mediate a tight adherence to epithelial cells and gingival fibroblasts with Kgp being implicated as providing most of the binding.
  • Gingipains in hemoglobin binding and heme acquisition: Gingipains exert a sequential action on which Rgps converts oxyhemoglobin to methemoglobin, which render the hemoglobin more susceptible to degradation by Kgp. [25] The occurrence of gingipains in large complexes is a very cleaver design to facilitate hemoglobin degradation and the capture of the released heme is accomplished with high affinity by hemagglutinin-adhesin-2. Gingipains may function as hemophore-like proteins; shuttling captured heme to a hemoglobin receptor (HmuR) in the outer membrane.
  • Production of nutritious peptides: Gingipains as the most "aggressive" endopeptidases degrade serum and tissue-derived proteins. The gingipain generated protein fragments are finally subjected to the action of di- and tripeptidyl peptidases to release di- and tripeptides to be transported into the cell and used in P.gingivalis carbon and energy metabolism. [26]
  • Degradation of antibacterial peptides: In densely populated biofilm, gingipains as well as proteases released by other periodontopathogens can proteolytically inactivate cationic antimicrobial peptides to enable the survival of other bacterial species which are highly sensitive to them. [27] Degradation of cationic antimicrobial peptides also inactivates cationic antimicrobial peptides' ability to neutralize LPSs, which may lead to exacerbated, sustained production of proinflammatory cytokines.
  • Exploiting complement: P. gingivalis is resistant to killing by the human complement system. In a large part, this resistance is dependent on proteolytic activity of gingipains degrading different components of complement. [28] In addition, gingipains also contribute to proteolysis independent protection of P. gingivalis against complement-mediated lysis. This is achieved through the capture of the human complement inhibitor C4b-binding protein, thus, hindering deposition of the membrane attack complex on the P. gingivalis surface. [26]
  • Direct degradation of extracellular matrix proteins: Gingipains efficiently degrade several extracellular matrix proteins in vitro gingipains can accomplish a lot more harm indirectly by disturbing the protease-protease inhibitor balance. In the case of human gingival fibroblasts, it was shown that matrix metalloprotease-1 expression was stimulated by Rgp activity. [29] Latent matrix metalloproteases can be directly activated by gingipains.


Structure and situation: Collagenase is perhaps the most important of the P. gingivalis proteolytic enzymes. These enzymes are either exposed at the surface (in the outer membrane) of the bacterium where they are able to come into contact with host cells and tissues, within the periplasmic space capable of being transported to the cell surface or in outer membrane vesicles. [10]

If expressed in vivo, it is a major destructive enzyme (virulence factor) associated with the soft tissue destruction characteristic of human periodontitis. [30] Mayrand and Grenier were able to dissect the collagenolytic activity into at least two activities: A specific collagenase activity and nonspecific proteinase activity. [31] These thiol-dependent collagenolytic enzymes had a molecular weight of 70 kDa and were purified from the spent culture supernatant, and their inhibition with serum components was studied.

In a study, Hoover and Felton [32] and Li et al., [33] used specific P. gingivalis collagenase-deficient mutants generated by nitrosoguanidine mutagenesis and showed that the mutants possessed significantly decreased interaction (that is, adherence) to A. viscosus compared with its wild type parent. Takahashi et al., were able to isolate a prtCgene from P. gingivalis strain 53977, which expressed collagenase activity. [34]


Structure and situation: These enzymes are either exposed at the surface (in the outer membrane) of the bacterium where they are able to come into contact with host cells and tissues or within the periplasmic space capable of being transported to the cell surface, and in outer membrane vesicles.

P. gingivalis is the only member of periodontopathic microbiota that exhibits strong dipeptidyl arylaminopeptidase activity. [35] Abiko et al., purified dipeptidylaminopeptidase from the spent growth supernatant of P. gingivalis and exposed it to type 1 collagen, cleaving a glycylpropyl dipeptide from the collagen protein. [36] Grenier and McBride were successful in localizing their aminopeptidase activity to the surface of P. gingivalis. Immunoelectron microscopy localized the enzyme in the periplasmic space. [37],[66]

Vaccine against P. gingivalis

Vaccination is a process that induces specific immune resistance to a bacterial or viral infection. A common finding in patients with periodontitis is the presence of P. gingivalis-specific antibodies in serum and gingival crevicular fluid. Immunization with several P. gingivalis-specific antigens has been shown to enhance the immune response against P. gingivalis, as demonstrated by the induction of specific antibodies and reduction of P. gingivalis-induced alveolar bone loss in animal models. The production of antibodies generally indicates the activation of our major host defense mechanism; these antibodies are insufficient to clear P. gingivalis infection. Although complete protection through immunization has not yet been achieved, new knowledge about specific P. gingivalis antigens holds promising possibilities for the future [Table 1].
Table 1: Studies on immunization with Porphyromonas gingivalis-specific antigens

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   Conclusion Top

In general, the major antigens of P. gingivalis induce an overall inflammatory immune response, as demonstrated in vitro for a wide variety of cell types and also in vivo; in experimental animal models. These data correlate with findings from studies with periodontitis patients. New research has highlighted earlier apparent contradictions in the literature demonstrating cytokine stimulation and degradation as well as cellular activation and apoptosis. These apparent contradictions can be explained by P. gingivalis antigen concentration effects, and when this is taken into account, the localized dysregulation of the immune response, that is, commonly reported can also be explained. Finally, despite the strong and active inflammatory immune response generated by P. gingivalis antigens, more research is needed to study the use of these same antigens as vaccine candidates, which, if used appropriately, may have utility as an adjunctive therapy in ameliorating chronic periodontitis.

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  [Figure 1], [Figure 2], [Figure 3], [Figure 4], [Figure 5]

  [Table 1]

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