Oral microbiology and immunology最新文献

{"title":"Human cytomegalovirus and Epstein-Barr virus inhibit oral bacteria-induced macrophage activation and phagocytosis.","authors":"Y-L Lin,&nbsp;M Li","doi":"10.1111/j.1399-302X.2009.00504.x","DOIUrl":"https://doi.org/10.1111/j.1399-302X.2009.00504.x","url":null,"abstract":"<p><strong>Introduction: </strong>Periodontal disease is an inflammatory condition caused by periodontal microorganisms. Viruses such as human cytomegalovirus (HCMV) and Epstein-Barr virus (EBV) are associated with certain types of periodontal disease, but their roles in promoting the disease are unclear. Because both viruses infect human macrophages, cells which play key roles in the clearance of pathogenic bacteria, it is likely that the viruses alter the functional capacity of macrophages by inhibiting their defense mechanisms against invading pathogens.</p><p><strong>Methods: </strong>Macrophages preinfected with HCMV or EBV were evaluated following stimulation by selected oral bacteria. Bacteria-induced macrophage activation was assayed by measuring the levels of tumor necrosis factor-alpha (TNF-alpha) produced in the media, and phagocytic activity was analysed by a phagocytosis assay with fluorescein isothiocyanate-labeled bacteria. The virus-infected macrophages were also subjected to semi-quantitative polymerase chain reaction to measure the expression of toll-like receptor 9, which is involved in the activation of phagocytosis-related pathways.</p><p><strong>Results: </strong>Both HCMV and EBV significantly diminished the TNF-alpha production typically induced by oral bacteria, inhibited the phagocytic activity of macrophages, and downregulated the expression of toll-like receptor 9.</p><p><strong>Conclusion: </strong>Infection by HCMV or EBV inhibits the functional ability of macrophages to respond to bacterial challenge, thereby suggesting their pathogenic role in the development of periodontal disease.</p>","PeriodicalId":19630,"journal":{"name":"Oral microbiology and immunology","volume":"24 3","pages":"243-8"},"PeriodicalIF":0.0,"publicationDate":"2009-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1111/j.1399-302X.2009.00504.x","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"28225416","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Expression of receptor activator of nuclear factor-kappaB ligand by B cells in response to oral bacteria.","authors":"X Han,&nbsp;X Lin,&nbsp;A R Seliger,&nbsp;J Eastcott,&nbsp;T Kawai,&nbsp;M A Taubman","doi":"10.1111/j.1399-302X.2008.00494.x","DOIUrl":"https://doi.org/10.1111/j.1399-302X.2008.00494.x","url":null,"abstract":"<p><strong>Introduction: </strong>We investigated receptor activator of nuclear factor-kappaB ligand (RANKL) expression by B lymphocytes during early and late aspects of the immune response to Aggregatibacter actinomycetemcomitans, a gram-negative, anaerobic bacterium associated with aggressive periodontal disease.</p><p><strong>Methods: </strong>Expression of messenger RNA transcripts (tumor necrosis factor-alpha, Toll-like receptors 4 and 9, interleukins 4 and 10, and RANKL) involved in early (1-day) and late (10-day) responses in cultured rat splenocytes was examined by reverse transcription-polymerase chain reaction (RT-PCR). The immune cell distribution (T, B, and natural killer cells and macrophages) in cultured rat splenocytes and RANKL expression in B cells were determined by flow cytometric analyses. B-cell capacity for induction of osteoclast differentiation was evaluated by coculture with RAW 264.7 cells followed by a tartrate-resistant acid phosphatase (TRAP) activity assay.</p><p><strong>Results: </strong>The expression levels of interleukins 4 and 10 in cultured cells were not changed in the presence of A. actinomycetemcomitans until cultured for 3 days, and peaked after 7 days. After culture for 10 days, the percentages of B and T cells, the overall RANKL messenger RNA transcripts, and the percentage of RANKL-expressing immunoglobulin G-positive cells were significantly increased in the presence of A. actinomycetemcomitans. These increases were considerably greater in cells isolated from A. actinomycetemcomitans-immunized animals than from non-immunized animals. RAW 264.7 cells demonstrated significantly increased TRAP activity when cocultured with B cells from A. actinomycetemcomitans-immunized animals. The addition of human osteoprotegerin-Fc to the culture significantly diminished such increases.</p><p><strong>Conclusion: </strong>This study suggests that B-lymphocyte involvement in the immune response to A. actinomycetemcomitans through upregulation of RANKL expression potentially contribute to bone resorption in periodontal disease.</p>","PeriodicalId":19630,"journal":{"name":"Oral microbiology and immunology","volume":"24 3","pages":"190-6"},"PeriodicalIF":0.0,"publicationDate":"2009-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1111/j.1399-302X.2008.00494.x","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"28152388","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Homotypic biofilm structure of Porphyromonas gingivalis is affected by FimA type variations.","authors":"M Kuboniwa,&nbsp;A Amano,&nbsp;H Inaba,&nbsp;E Hashino,&nbsp;S Shizukuishi","doi":"10.1111/j.1399-302X.2009.00511.x","DOIUrl":"https://doi.org/10.1111/j.1399-302X.2009.00511.x","url":null,"abstract":"<p><strong>Introduction: </strong>Porphyromonas gingivalis is a periodontal pathogen whose long fimbriae (FimA) are classified into six genotypes (types I-V and Ib) based on the diversity of the fimA genes. FimA variations were previously shown to be related to the onset and development of adult periodontitis in a general population, while FimA were recently found to be critical mediators of initial biofilm formation. However, it is unclear if FimA variations have effects on biofilm features. Here, we compare the characteristic structures of homotypic biofilms developed by P. gingivalis strains with different FimA types.</p><p><strong>Methods: </strong>Biofilms were formed on saliva-coated glass bottom wells in phosphate-buffered saline and their structures were analysed using confocal laser scanning microscopy. Furthermore, the biovolumes of the biofilms were quantified with a three-dimensional fluorophotometric method.</p><p><strong>Results: </strong>Biofilm structures formed by the six representative FimA-type strains apparently differed. Type I and Ib P. gingivalis formed biofilms with a dense basal monolayer and dispersed microcolonies, whereas those formed by types II, III and IV strains had markedly luxuriant biofilms filled with widely clumped and tall colonies, and their biovolumes were significantly greater than those of types I and Ib. These characteristic features were confirmed to be closely related to FimA type in assays that utilized fimA-substituted mutants from type I to II and those from type II to I.</p><p><strong>Conclusion: </strong>Our results suggest that FimA variations have effects on the structures of biofilms formed by P. gingivalis, which may be an important factor in the pathogenesis of periodontitis.</p>","PeriodicalId":19630,"journal":{"name":"Oral microbiology and immunology","volume":"24 3","pages":"260-3"},"PeriodicalIF":0.0,"publicationDate":"2009-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1111/j.1399-302X.2009.00511.x","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"28227567","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Oral cavity is not a reservoir for Helicobacter pylori in infected patients with functional dyspepsia.","authors":"V P Silva Rossi-Aguiar,&nbsp;T Navarro-Rodriguez,&nbsp;R Mattar,&nbsp;M P Siqueira de Melo Peres,&nbsp;R Correa Barbuti,&nbsp;F M Silva,&nbsp;F J Carrilho,&nbsp;J N Eisig","doi":"10.1111/j.1399-302X.2008.00491.x","DOIUrl":"https://doi.org/10.1111/j.1399-302X.2008.00491.x","url":null,"abstract":"<p><strong>Introduction: </strong>Helicobacter pylori infection is very prevalent in Brazil, infecting almost 65% of the population. The aim of this study was to evaluate the presence of this bacterium in the oral cavity of patients with functional dyspepsia (epigastric pain syndrome), establish the main sites of infection in the mouth, and assess the frequency of cagA and vacA genotypes of oral H. pylori.</p><p><strong>Methods: </strong>All 43 outpatients with epigastric pain syndrome, who entered the study, were submitted to upper gastrointestinal endoscopy to rule out organic diseases. Helicobacter pylori infection in the stomach was confirmed by a rapid urease test and urea breath tests. Samples of saliva, the tongue dorsum and supragingival dental plaque were collected from the oral cavity of each subject and subgingival dental plaque samples were collected from the patients with periodontitis; H. pylori infection was verified by polymerase chain reaction using primers that amplify the DNA sequence of a species-specific antigen present in all H. pylori strains; primers that amplify a region of urease gene, and primers for cagA and vacA (m1, m2, s1a, s1b, s2) genotyping.</p><p><strong>Results: </strong>Thirty patients harbored H. pylori in the stomach, but it was not possible to detect H. pylori in any oral samples using P1/P2 and Urease A/B. The genotype cagA was also negative in all samples and vacA genotype could not be characterized (s-m-).</p><p><strong>Conclusion: </strong>The oral cavity may not be a reservoir for H. pylori in patients with epigastric pain syndrome, the bacterium being detected exclusively in the stomach.</p>","PeriodicalId":19630,"journal":{"name":"Oral microbiology and immunology","volume":"24 3","pages":"255-9"},"PeriodicalIF":0.0,"publicationDate":"2009-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1111/j.1399-302X.2008.00491.x","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"28227566","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Oral Candida infection and colonization in solid organ transplant recipients.","authors":"A Dongari-Bagtzoglou,&nbsp;P Dwivedi,&nbsp;E Ioannidou,&nbsp;M Shaqman,&nbsp;D Hull,&nbsp;J Burleson","doi":"10.1111/j.1399-302X.2009.00505.x","DOIUrl":"https://doi.org/10.1111/j.1399-302X.2009.00505.x","url":null,"abstract":"<p><strong>Introduction: </strong>Oral Candida carriage and infection have been reported to be associated with a greater risk for systemic infection in transplant recipients; however, a systematic analysis of the oral Candida titers and species has not been previously conducted. The objectives of this study were to determine the prevalence of oropharyngeal candidiasis, the oral carrier status, Candida titers and species in this population.</p><p><strong>Methods: </strong>Ninety kidney and heart transplant subjects and 72 age-matched healthy controls were included. Swabs from the oral mucosa and a standardized amount of unstimulated saliva were plated on Chromagar Candida, and colony-forming units per millilitre were calculated. Initial speciation was based on colony color and was confirmed by standard germ tube, biotyping, or polymerase chain reaction assays.</p><p><strong>Results: </strong>Infection with C. albicans was detected in seven transplant subjects and none of the controls. The transplant group had significantly higher oral Candida titers than the control group. There were no statistically significant relationships between the dose or type of immunosuppressants and oral Candida titers or infection. A significantly higher percentage of transplant subjects were colonized by more than one species, compared with control subjects. The most frequent species combination in transplant subjects was C. albicans and C. glabrata. C. glabrata was isolated from 13.5% of transplant carriers and none of the controls.</p><p><strong>Conclusions: </strong>Increased oral Candida infection and carriage titers were found in the transplant population. Although the majority of transplant patients were colonized by C. albicans, C. glabrata appears to emerge as the second most prevalent species.</p>","PeriodicalId":19630,"journal":{"name":"Oral microbiology and immunology","volume":"24 3","pages":"249-54"},"PeriodicalIF":0.0,"publicationDate":"2009-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1111/j.1399-302X.2009.00505.x","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"28225417","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Porphyromonas gingivalis stimulates TACE production by T cells.","authors":"N Bostanci,&nbsp;D Reddi,&nbsp;M Rangarajan,&nbsp;M A Curtis,&nbsp;G N Belibasakis","doi":"10.1111/j.1399-302X.2008.00488.x","DOIUrl":"https://doi.org/10.1111/j.1399-302X.2008.00488.x","url":null,"abstract":"<p><strong>Introduction: </strong>Tumour necrosis factor-alpha converting enzyme (TACE), also known as ADAM17, is a membrane-bound metalloprotease and disintegrin. It is produced by a number of host cells and is known to shed and release cell-bound cytokines, particularly members of the tumour necrosis factor family. The aim of this study was to investigate the effect of Porphyromonas gingivalis on TACE production by a human T-cell line, to identify putative virulence factors involved in this process, and to investigate the effect of doxycycline.</p><p><strong>Methods: </strong>P. gingivalis 6-day culture supernatants were used to challenge Jurkat T cells for 6 h. Secreted and cell-associated TACE levels were measured by enzyme-linked immunosorbent assay, whereas messenger RNA expression was investigated by quantitative real-time polymerase chain reaction. To investigate the involvement of cysteine proteases or proteinaceous components in general, P. gingivalis culture supernatants were treated with the specific chemical inhibitor TLCK or heat-inactivated, respectively. The effect of doxycycline on the regulation of TACE secretion by P. gingivalis was also investigated.</p><p><strong>Results: </strong>P. gingivalis challenge resulted in a concentration-dependent enhancement of TACE messenger RNA expression and protein release by Jurkat cells. TLCK treatment or heat treatment of P. gingivalis culture supernatants decreased TACE release to control levels. Doxycycline inhibited TACE secretion dose dependently.</p><p><strong>Conclusion: </strong>The induction of TACE by T cells in response to P. gingivalis may in turn favour the shedding of host cell-bound cytokines into the local microenvironment, potentially amplifying the inflammatory response. In the present experimental system, P. gingivalis cysteine proteases are involved in TACE release by T cells.</p>","PeriodicalId":19630,"journal":{"name":"Oral microbiology and immunology","volume":"24 2","pages":"146-51"},"PeriodicalIF":0.0,"publicationDate":"2009-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1111/j.1399-302X.2008.00488.x","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"28004612","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Inhibiting effects of Streptococcus salivarius on competence-stimulating peptide-dependent biofilm formation by Streptococcus mutans.","authors":"S Tamura,&nbsp;H Yonezawa,&nbsp;M Motegi,&nbsp;R Nakao,&nbsp;S Yoneda,&nbsp;H Watanabe,&nbsp;T Yamazaki,&nbsp;H Senpuku","doi":"10.1111/j.1399-302X.2008.00489.x","DOIUrl":"https://doi.org/10.1111/j.1399-302X.2008.00489.x","url":null,"abstract":"<p><strong>Introduction: </strong>The effects of Streptococcus salivarius on the competence-stimulating peptide (CSP)-dependent biofilm formation by Streptococcus mutans were investigated.</p><p><strong>Methods: </strong>Biofilms were grown on 96-well microtiter plates coated with salivary components in tryptic soy broth without dextrose supplemented with 0.25% sucrose. Biofilm formations were stained using safranin and quantification of stained biofilms was performed by measuring absorbance at 492 nm.</p><p><strong>Results: </strong>S. mutans formed substantial biofilms, whereas biofilms of S. salivarius were formed poorly in the medium conditions used. Furthermore, in combination cultures, S. salivarius strongly inhibited biofilm formation when cultured with S. mutans. This inhibition occurred in the early phase of biofilm formation and was dependent on inactivation of the CSP of S. mutans, which is associated with competence, biofilm formation, and antimicrobial activity of the bacterium, and is induced by expression of the comC gene. Comparisons between the S. mutans clinical strains FSC-3 and FSC-3DeltaglrA in separate dual-species cultures with S. salivarius indicated that the presence of the bacitracin transport ATP-binding protein gene glrA caused susceptibility to inhibition of S. mutans biofilm formation by S. salivarius, and was also associated with the regulation of CSP production by com gene-dependent quorum sensing systems.</p><p><strong>Conclusion: </strong>It is considered that regulation of CSP by glrA in S. mutans and CSP inactivation by S. salivarius are important functions for cell-to-cell communication between biofilm bacteria and oral streptococci such as S. salivarius. Our results provide useful information for understanding the ecosystem of oral streptococcal biofilms, as well as the competition between and coexistence of multiple species in the oral cavity.</p>","PeriodicalId":19630,"journal":{"name":"Oral microbiology and immunology","volume":"24 2","pages":"152-61"},"PeriodicalIF":0.0,"publicationDate":"2009-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1111/j.1399-302X.2008.00489.x","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"28004613","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Role of lysine in interaction between surface protein peptides of Streptococcus gordonii and agglutinin peptide.","authors":"H Koba,&nbsp;K Okuda,&nbsp;H Watanabe,&nbsp;J Tagami,&nbsp;H Senpuku","doi":"10.1111/j.1399-302X.2008.00490.x","DOIUrl":"https://doi.org/10.1111/j.1399-302X.2008.00490.x","url":null,"abstract":"<p><strong>Introduction: </strong>Streptococcus gordonii interacts with the salivary pellicle on the tooth surface and plays an important role in dental biofilm formation. Reports show that the analog Ssp peptide (A11K; alanine to lysine at position 11 in the arranged sequence, (1)DYQAKLAAYQAEL(13)) of SspA and SspB of S. gordonii increased binding to the salivary agglutinin (gp-340/DMBT1) peptide (scavenger receptor cysteine-rich domain 2: SRCRP2). To determine the role of lysine in the binding of the Ssp(A11K) peptide to SRCRP2, we investigated whether an additional substitution by lysine influenced the binding of Ssp(A11K) peptide to SRCRP2 using a BIAcore biosensor assay.</p><p><strong>Methods: </strong>Six analogs of the Ssp peptide with positive charges in surface positions on the structure were synthesized using substitution at various positions.</p><p><strong>Results: </strong>The binding activity of analog Ssp(A4K-A11K) peptide was significantly higher than the other Ssp analogs. The binding activity rose under low ionic strength conditions. The distance between positively charged amino acids in the Ssp(A4K-A11K) peptide between 4K and 11K was 1.24 +/- 0.02 nm and was close to the distance (1.19 +/- 0.00 nm) between Q and E, presenting a negative charged area, on SRCRP2 using chemical computing graphic analysis. The molecular angle connecting 1D-11K-4K in the Ssp(A4K-A11K) peptide secondary structure was smaller than the other peptide angles (1D-11K-XK). The Ssp(A4K-A11K) peptide showed higher inhibiting activity for Streptococcus mutans binding to saliva-coated hydroxyapatite than the (A11K) peptide.</p><p><strong>Conclusion: </strong>The positioning of lysine is important for binding between Ssp peptide and SRCRP2, and the inhibiting effect on S. mutans binding to the tooth surface.</p>","PeriodicalId":19630,"journal":{"name":"Oral microbiology and immunology","volume":"24 2","pages":"162-9"},"PeriodicalIF":0.0,"publicationDate":"2009-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1111/j.1399-302X.2008.00490.x","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"28003469","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Correlations of oral bacterial arginine and urea catabolism with caries experience.","authors":"M M Nascimento,&nbsp;V V Gordan,&nbsp;C W Garvan,&nbsp;C M Browngardt,&nbsp;R A Burne","doi":"10.1111/j.1399-302X.2008.00477.x","DOIUrl":"https://doi.org/10.1111/j.1399-302X.2008.00477.x","url":null,"abstract":"<p><strong>Background/aim: </strong>Alkali generation by oral bacteria plays a key role in plaque pH homeostasis and may be a major impediment to the development of dental caries. To determine if the capacity of oral samples to produce ammonia from arginine or urea was related to caries experience, the arginine deiminase system (ADS) and urease activity in saliva and dental plaque samples were measured in 45 adult subjects.</p><p><strong>Methods: </strong>The subjects were divided into three groups according to caries status; 13 caries-free (CF) individuals (decayed, missing, and filled teeth = 0); 21 caries-active (CA) individuals (decayed teeth >or= 4); and 11 caries-experienced (CE) individuals (decayed teeth = 0; missing and filled teeth > 0). Real-time polymerase chain reaction was used to quantify the proportion of certain acid- or alkali-producing organisms in the samples.</p><p><strong>Results: </strong>The amount of ammonia generated from the test substrates by plaque samples was generally higher than that produced by salivary samples in all groups. Significantly higher levels of salivary ADS activity and plaque urease activity were observed in CF subjects compared to CA subjects (P = 0.0004 and P = 0.014, respectively). The proportions of Streptococcus mutans from saliva and dental plaque of CA subjects were significantly higher than those from the CF group (P = 0.0153 and P = 0.0009, respectively). In the CA group, there was an inverse relationship between urease activity and the levels of S. mutans (P < 0.0001).</p><p><strong>Conclusion: </strong>This study supports the theory that increased caries risk is associated with reduced alkali-generating capacity of the bacteria colonizing the oral cavity; providing compelling evidence to further our understanding of oral alkali-generation in health and disease.</p>","PeriodicalId":19630,"journal":{"name":"Oral microbiology and immunology","volume":"24 2","pages":"89-95"},"PeriodicalIF":0.0,"publicationDate":"2009-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1111/j.1399-302X.2008.00477.x","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"28004111","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Ceragenin CSA-13 exhibits antimicrobial activity against cariogenic and periodontopathic bacteria.","authors":"E Isogai,&nbsp;H Isogai,&nbsp;K Takahashi,&nbsp;K Okumura,&nbsp;P B Savage","doi":"10.1111/j.1399-302X.2008.00464.x","DOIUrl":"https://doi.org/10.1111/j.1399-302X.2008.00464.x","url":null,"abstract":"<p><strong>Introduction: </strong>Ceragenin CSA-13 is a bile-acid-based mimic of endogenous antimicrobial peptides and shares a mechanism of action with many of these antimicrobial agents. Because CSA-13 is not peptide based, it is not a substrate for the proteases that are found in the oral cavity, which are capable of degrading antimicrobial peptides. Furthermore, the simplicity of the ceragenins makes them easier to prepare and purify than antimicrobial peptides. In this study, we examined the antimicrobial activities of CSA-13 against oral pathogens and found that this compound was bactericidal against all of the strains tested.</p><p><strong>Methods: </strong>The strains used were isolates of Streptococcus mutans and Porphyromonas species. Minimum inhibitory concentrations (MIC) were determined using agar dilution methods. In susceptibility testing, viable counts were determined after incubation with CSA-13.</p><p><strong>Results: </strong>CSA-13 was potent against all 23 strains tested with MICs of 1-8 microg/ml for S. mutans and 1-16 microg/ml for 24 strains of the genus Porphyromonas. The MIC(50) was 2 and the MIC(90) was 8 mug/ml for S. mutans. MIC ranges for protease-positive P. gingivalis and P. cangingivalis were 2-16 microg/ml, and 1-2 microg/ml for protease-negative P. circumdentaria. CSA-13 interacted with lipopolysaccharide-sensitized erythrocytes at a concentration of 5.0-20.0 microg/ml.</p><p><strong>Conclusion: </strong>CSA-13 displays broad-spectrum activity against cariogenic and periodontopathic bacteria. CSA-13 was effective against protease-positive Porphyromonas. It was shown to bind to erythrocytes coated with lipopolysaccharide and lipoteichoic acid from diverse bacterial strains. These results suggest that CSA-13 may be useful for the prevention and treatment of oral microbial diseases.</p>","PeriodicalId":19630,"journal":{"name":"Oral microbiology and immunology","volume":"24 2","pages":"170-2"},"PeriodicalIF":0.0,"publicationDate":"2009-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1111/j.1399-302X.2008.00464.x","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"28003470","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}