Effect of <i>Porphyromonas gingivalis</i> ATCC 33277 Vesicle on Adherence of <i>Streptococcus mutans</i> OMZ 70 to the Experimental Pellicle

Kamaguchi, Arihide; Baba, Hisae; Hoshi, Masaaki; Inomata, Koshiro

doi:10.1111/j.1348-0421.1995.tb02237.x

Cited by 7 publications

(8 citation statements)

References 26 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Since the BspA protein belongs to the LRR domain family as well as the Big_2 domain family, involved in receptor-ligand recognition via protein-protein interactions, it is possible that BspA interacts with a specific epithelial cell surface receptor for adherence and invasion. Previous studies have shown that P. gingivalis OMVs are potent activators of adhesion and aggregation (15,16) for other gram-positive bacteria. Our investigations of the interactions between P. gingivalis and T. forsythia have shown that the attachment abilities of T. forsythia ATCC 43037 and its BspA mutant were increased in the presence of P. gingivalis vesicles, supporting the notion that synergy exists between these two species with respect to adherence and colonization.…”

Section: Discussionmentioning

confidence: 99%

“…The P. gingivalis OMVs released into the environment are thought to play important roles in periodontal disease by serving as vehicles for toxin and enzyme spreading as well as being involved in the adherence and aggregation of bacteria (1,6,20). P. gingivalis OMVs have also been shown to be potent activators of adhesion (16) and aggregation for other oral bacteria (15). P. gingivalis OMVs have been shown to aggregate host platelets (33) as well as to invade epithelial cells in vitro (13,41).…”

mentioning

confidence: 99%

See 1 more Smart Citation

Porphyromonas gingivalis Vesicles Enhance Attachment, and the Leucine-Rich Repeat BspA Protein Is Required for Invasion of Epithelial Cells by “ Tannerella forsythia ”

et al. 2006

View full text Add to dashboard Cite

The human oral cavity harbors more than 500 species of bacteria. Periodontitis, a bacterially induced inflammatory disease that leads to tooth loss, is believed to result from infection by a select group of gram-negative periodontopathogens that includes Porphyromonas gingivalis, Treponema denticola, and "Tannerella forsythia" (opinion on name change from Tannerella forsythensis pending; formerly Bacteroides forsythus). Epithelial cell invasion by periodontopathogens is considered to be an important virulence mechanism for evasion of the host defense responses. Further, the epithelial cells with invading bacteria also serve as reservoirs important in recurrent infections. The present study was therefore undertaken to address the epithelial cell adherence and invasion properties of T. forsythia and the role of the cell surface-associated protein BspA in these processes. Further, we were interested in determining if P. gingivalis, one of the pathogens frequently found associated in disease, or its outer membrane vesicles (OMVs) could modulate the epithelial cell adherence and invasion abilities of T. forsythia. Here we show that epithelial cell attachment and invasion by T. forsythia are dependent on the BspA protein. In addition, P. gingivalis or its OMVs enhance the attachment and invasion of T. forsythia to epithelial cells. Thus, interactions between these two bacteria may play important roles in virulence by promoting host cell attachment and invasion.

show abstract

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Porphyromonas gingivalis Vesicles Enhance Attachment, and the Leucine-Rich Repeat BspA Protein Is Required for Invasion of Epithelial Cells by “ Tannerella forsythia ”

et al. 2006

View full text Add to dashboard Cite

show abstract

“…Its fimbriae have been shown to interact with epithelial cells (15), cultured human fibroblasts (20), and saliva-coated hydroxyapatite beads (2,32), while its vesicles have been shown to interact with collagen-coated hydroxyapatite beads (32). Further, in studies to determine which of the surface components of P. gingivalis interact with grampositive bacteria, its fimbriae have been reported to interact with A. viscosus (12) and S. gordonii (24); its vesicles have been reported to interact with A. naeslundii (8), A. viscosus (13), and S. mutans (17); and its hemagglutinin has been reported to interact with A. viscosus (34).…”

mentioning

confidence: 99%

“…In order to cause infection, it is necessary for P. gingivalis to attach to tooth surfaces, subgingival epithelium, or early colonizing gram-positive bacteria; this step constitutes the initial stage of colonization in periodontal pockets (38). In addition, the bacterium has been reported to interact with a variety of other oral gram-positive bacteria (19), including Actinomyces naeslundii (36,43), Actinomyces viscosus (9,12,26,27,36), Streptococcus gordonii (23), Streptococcus mutans (17), Streptococcus oralis (29), and Streptococcus sanguis (39); these interactions are considered to play a vital role in the colonization of P. gingivalis in the oral cavity.…”

mentioning

confidence: 99%

Glyceraldehyde-3-Phosphate Dehydrogenase of Streptococcus oralis Functions as a Coadhesin for Porphyromonas gingivalis Major Fimbriae

et al. 2004

View full text Add to dashboard Cite

Cohesive interactions between Porphyromonas gingivalis and plaque-forming bacteria, such as Streptococcus oralis, are considered to play an important role in the colonization of P. gingivalis in periodontal sites. Although P. gingivalis fimbriae have been reported to mediate coaggregation with S. oralis, the S. oralis molecule involved has not been identified. We identified the coadhesin of S. oralis ATCC 9811 and purified it by affinity column chromatography. We found that the molecular mass of the purified protein was approximately 40 kDa. Dot blot and Western blot assays showed binding of the 40-kDa protein to P. gingivalis fimbriae. Further, turbidimetric assays showed that the coadhesin inhibited coaggregation between P. gingivalis and S. oralis in a dose-dependent manner. Analyses of the amino-terminal sequences of the protein and its lysyl endopeptidase-cleaved fragments revealed that the coadhesin was identical to glyceraldehyde-3-phosphate dehydrogenase (GAPDH). Next, we cloned the gene that encodes S. oralis GAPDH and found that the sequence had a high degree of homology with the sequences of GAPDHs of various bacteria, including Streptococcus gordonii and Fusobacterium nucleatum. To confirm the contribution of S. oralis GAPDH to the interaction with P. gingivalis, a recombinant GAPDH protein was generated in Escherichia coli; this protein bound to P. gingivalis fimbriae and had an inhibitory effect on coaggregation. These results suggest that S. oralis GAPDH functions as a coadhesin for P. gingivalis fimbriae. In addition, considering the high degree of homology of the GAPDHs of various bacteria, those of other plaque-forming bacteria also may contribute to the colonization of P. gingivalis.Porphyromonas gingivalis is considered to be a prominent periodontopathogen, as it possesses a variety of virulence factors, such as proteinases, hemagglutinin, and lipopolysaccharide (28,37,41). In order to cause infection, it is necessary for P. gingivalis to attach to tooth surfaces, subgingival epithelium, or early colonizing gram-positive bacteria; this step constitutes the initial stage of colonization in periodontal pockets (38). In addition, the bacterium has been reported to interact with a variety of other oral gram-positive bacteria (19), including Actinomyces naeslundii (36, 43), Actinomyces viscosus (9, 12, 26, 27, 36), Streptococcus gordonii (23), Streptococcus mutans (17), Streptococcus oralis (29), and Streptococcus sanguis (39); these interactions are considered to play a vital role in the colonization of P. gingivalis in the oral cavity.P. gingivalis possesses several cell surface components that are important for its attachment. Its fimbriae have been shown to interact with epithelial cells (15), cultured human fibroblasts (20), and saliva-coated hydroxyapatite beads (2, 32), while its vesicles have been shown to interact with collagen-coated hydroxyapatite beads (32). Further, in studies to determine which of the surface components of P. gingivalis interact with grampositive bacteria, its fimbri...

show abstract

“…P. gingivalis possesses several components as adhesins on the cell surface, such as FimA fimbriae and Mfa1 fimbriae (2,6,12,14,17,23,25), vesicles (10,15,19,31), hemagglutinin (24), and Arg-and Lys-specific cysteine proteinases (1). Interactions between the following P. gingivalis cell surface components and oral grampositive bacteria have been documented: (i) FimA fimbriae and Actinomyces viscosus (12), (ii) FimA and Mfa1 fimbriae and Streptococcus gordonii (6,23), (iii) Arg-and Lys-specific cysteine proteinases and A. viscosus (1), and (iv) vesicles and Actinomyces naeslundii (10), A. viscosus (15,31), and Streptococcus mutans (19). Additionally, P. gingivalis FimA fimbriae have been shown to interact with epithelial cells (17), cultured human fibroblasts (14), and salivary proteins (2), which indicates that P. gingivalis FimA fimbriae play an important role as a main adhesive component in bacterial colonization.…”

mentioning

confidence: 99%

Identification of the Binding Domain of Streptococcus oralis Glyceraldehyde-3-Phosphate Dehydrogenase for Porphyromonas gingivalis Major Fimbriae

et al. 2009

View full text Add to dashboard Cite

Porphyromonas gingivalis forms communities with antecedent oral biofilm constituent streptococci. P. gingivalis major fimbriae bind to glyceraldehyde-3-phosphate dehydrogenase (GAPDH) present on the streptococcal surface, and this interaction plays an important role in P. gingivalis colonization. This study identified the binding domain of Streptococcus oralis GAPDH for P. gingivalis fimbriae. S. oralis recombinant GAPDH (rGAPDH) was digested with lysyl endopeptidase. Cleaved fragments of rGAPDH were applied to a reversephase high-pressure liquid chromatograph equipped with a C 18 column. Each peak was collected; the binding activity toward P. gingivalis recombinant fimbrillin (rFimA) was analyzed with a biomolecular interaction analysis system. The fragment displaying the strongest binding activity was further digested with various proteinases, after which the binding activity of each fragment was measured. The amino acid sequence of each fragment was determined by direct sequencing, mass spectrometric analysis, and amino acid analysis. Amino acid residues 166 to 183 of S. oralis GAPDH exhibited the strongest binding activity toward rFimA; confocal laser scanning microscopy revealed that the synthetic peptide corresponding to amino acid residues 166 to 183 of S. oralis GAPDH (pep166-183, DNFGVVEGLMTTIHAYTG) inhibits S. oralis-P. gingivalis biofilm formation in a dose-dependent manner. Moreover, pep166-183 inhibited interbacterial biofilm formation by several oral streptococci and P. gingivalis strains with different types of FimA. These results indicate that the binding domain of S. oralis GAPDH for P. gingivalis fimbriae exists within the region encompassing amino acid residues 166 to 183 of GAPDH and that pep166-183 may be a potent inhibitor of P. gingivalis colonization in the oral cavity.

show abstract

Effect of Porphyromonas gingivalis ATCC 33277 Vesicle on Adherence of Streptococcus mutans OMZ 70 to the Experimental Pellicle

Cited by 7 publications

References 26 publications

Porphyromonas gingivalis Vesicles Enhance Attachment, and the Leucine-Rich Repeat BspA Protein Is Required for Invasion of Epithelial Cells by “ Tannerella forsythia ”

Porphyromonas gingivalis Vesicles Enhance Attachment, and the Leucine-Rich Repeat BspA Protein Is Required for Invasion of Epithelial Cells by “ Tannerella forsythia ”

Glyceraldehyde-3-Phosphate Dehydrogenase of Streptococcus oralis Functions as a Coadhesin for Porphyromonas gingivalis Major Fimbriae

Identification of the Binding Domain of Streptococcus oralis Glyceraldehyde-3-Phosphate Dehydrogenase for Porphyromonas gingivalis Major Fimbriae

Contact Info

Product

Resources

About