Adhesins encoded by the gingipain genes of Porphyromonas gingivalis are responsible for co-aggregation with Prevotella intermedia

Kamaguchi, Arihide; Ohyama, Tohru; Sakai, Eiko; Nakamura, Reiko; Watanabe, Toshihiro; Baba, Hisae; Nakayama, Koji

doi:10.1099/mic.0.25997-0

Cited by 55 publications

(52 citation statements)

References 44 publications

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“…Rabbit antiserum against a peptide derived from the amino acid sequence F 387 GLYDMAGNVAEWT 400 of PGN_1676 (PorK) in which a cysteine residue was synthesized at the N terminus of the peptide and conjugated to keyhole limpet hemocyanin was purchased from Sigma Genosys. Preparation of anti-Kgp and anti-Hgp44 antisera has been described previously (12,26). c-Myc antibody was obtained from Sigma.…”

Section: Methodsmentioning

confidence: 99%

A protein secretion system linked to bacteroidete gliding motility and pathogenesis

Satô

Naito²,

Yukitake³

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

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316

648

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Porphyromonas gingivalis secretes strong proteases called gingipains that are implicated in periodontal pathogenesis. Protein secretion systems common to other Gram-negative bacteria are lacking in P. gingivalis, but several proteins, including PorT, have been linked to gingipain secretion. Comparative genome analysis and genetic experiments revealed 11 additional proteins involved in gingipain secretion. Six of these (PorK, PorL, PorM, PorN, PorW, and Sov) were similar in sequence to Flavobacterium johnsoniae gliding motility proteins, and two others (PorX and PorY) were putative two-component system regulatory proteins. Real-time RT-PCR analysis revealed that porK, porL, porM, porN, porP, porT, and sov were down-regulated in P. gingivalis porX and porY mutants. Disruption of the F. johnsoniae porT ortholog resulted in defects in motility, chitinase secretion, and translocation of a gliding motility protein, SprB adhesin, to the cell surface, providing a link between a unique protein translocation system and a motility apparatus in members of the Bacteroidetes phylum.gingipain | Porphyromonas gingivalis | Flavobacterium | chitinase

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Section: Methodsmentioning

confidence: 99%

A protein secretion system linked to bacteroidete gliding motility and pathogenesis

Satô

Naito²,

Yukitake³

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

316

648

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“…Preparation of Anti-Hgp44, Anti-HbR, and Anti-PorT AntiseraRecombinant Hgp44 protein was obtained as described previously (36). A peptide derived from the amino acid sequence (Thr 221 to Leu 233 ) of PorT with an N-terminal cysteine residue, CTHERPDLLDDYKL, which was conjugated to keyhole limpet hemocyanin was purchased from Sigma Genosys.…”

Section: Methodsmentioning

confidence: 99%

Identification of a New Membrane-associated Protein That Influences Transport/Maturation of Gingipains and Adhesins of Porphyromonas gingivalis

Satô

Sakai

Veith

et al. 2005

Journal of Biological Chemistry

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132

175

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The dual membrane envelopes of Gram-negative bacteria provide two barriers of unlike nature that regulate the transport of molecules into and out of organisms. Organisms have developed several systems for transport across the inner and outer membranes. The Gramnegative periodontopathogenic bacterium Porphyromonas gingivalis produces proteinase and adhesin complexes, gingipains/adhesins, on the cell surface and in the extracellular milieu as one of the major virulence factors. Gingipains and/or adhesins are encoded by kgp, rgpA, rgpB, and hagA on the chromosome. In this study, we isolated a P. gingivalis mutant (porT), which showed very weak activities of gingipains in the cell lysates and culture supernatants. Subcellular fractionation and immunoblot analysis demonstrated that precursor forms of gingipains and adhesins were accumulated in the periplasmic space of the porT mutant cells. Peptide mass fingerprinting and N-terminal amino acid sequencing of the precursor proteins and the kgp-rgpB chimera gene product in the porT mutant indicated that these proteins lacked the signal peptide regions, consistent with their accumulation in the periplasm. The PorT protein seemed to be membrane-associated and exposed to the periplasmic space, as revealed by subcellular fractionation and immunoblot analysis using antiPorT antiserum. These results suggest that the membrane-associated protein PorT is essential for transport of the kgp, rgpA, rgpB, and hagA gene products across the outer membrane from the periplasm to the cell surface, where they are processed and matured.

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“…Vesicles are abundant in natural biofilms, and OM vesicle surface-bound DNA appears to be an electrostatic, bridging component that is central to membrane vesicle-bacterium-biofilm matrix interactions (120,121). Porphyromonas gingivalis vesicles mediate the coaggregation of the periodontopathogen Tannerella forsythia, and vesicles mediate the interaction/aggregation of staphylococci and Prevotella intermedia (65,71,72). By participating in quorum sensing, OM vesicles can also aid survival by contributing to communication within mixed populations of pathogens.…”

Section: Roles Of Om Vesicles In Interbacterial Interactionsmentioning

confidence: 99%

“…Vesicles from oral bacteria, in particular, promote biofilm formation and colonization (48,71,72,94). Vesicles are abundant in natural biofilms, and OM vesicle surface-bound DNA appears to be an electrostatic, bridging component that is central to membrane vesicle-bacterium-biofilm matrix interactions (120,121).…”

Section: Roles Of Om Vesicles In Interbacterial Interactionsmentioning

confidence: 99%

Virulence and Immunomodulatory Roles of Bacterial Outer Membrane Vesicles

Ellis

Kuehn

2010

Microbiol Mol Biol Rev

807

736

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SUMMARY Outer membrane (OM) vesicles are ubiquitously produced by Gram-negative bacteria during all stages of bacterial growth. OM vesicles are naturally secreted by both pathogenic and nonpathogenic bacteria. Strong experimental evidence exists to categorize OM vesicle production as a type of Gram-negative bacterial virulence factor. A growing body of data demonstrates an association of active virulence factors and toxins with vesicles, suggesting that they play a role in pathogenesis. One of the most popular and best-studied pathogenic functions for membrane vesicles is to serve as natural vehicles for the intercellular transport of virulence factors and other materials directly into host cells. The production of OM vesicles has been identified as an independent bacterial stress response pathway that is activated when bacteria encounter environmental stress, such as what might be experienced during the colonization of host tissues. Their detection in infected human tissues reinforces this theory. Various other virulence factors are also associated with OM vesicles, including adhesins and degradative enzymes. As a result, OM vesicles are heavily laden with pathogen-associated molecular patterns (PAMPs), virulence factors, and other OM components that can impact the course of infection by having toxigenic effects or by the activation of the innate immune response. However, infected hosts can also benefit from OM vesicle production by stimulating their ability to mount an effective defense. Vesicles display antigens and can elicit potent inflammatory and immune responses. In sum, OM vesicles are likely to play a significant role in the virulence of Gram-negative bacterial pathogens.

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Adhesins encoded by the gingipain genes of Porphyromonas gingivalis are responsible for co-aggregation with Prevotella intermedia

Cited by 55 publications

References 44 publications

A protein secretion system linked to bacteroidete gliding motility and pathogenesis

A protein secretion system linked to bacteroidete gliding motility and pathogenesis

Identification of a New Membrane-associated Protein That Influences Transport/Maturation of Gingipains and Adhesins of Porphyromonas gingivalis

Virulence and Immunomodulatory Roles of Bacterial Outer Membrane Vesicles

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