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1.
Clin Oral Investig ; 28(1): 108, 2024 Jan 22.
Artículo en Inglés | MEDLINE | ID: mdl-38246944

RESUMEN

OBJECTIVES: Crohn's disease patients, who are prone to develop periodontal diseases, may carry genetic defects in their Th17 cytokine, human beta-defensin (hBD) 1-3, and salivary and scavenger agglutinin (SALSA) expressions. Biochemical composition of saliva reflects the oral consequences of systemic immune response modifications. Our aim was to evaluate the salivary Th17 cytokine, epithelial hBD 1-3, and SALSA levels in relation to Crohn's disease. MATERIALS AND METHODS: This cross-sectional study included 42 Crohn's disease patients and 34 systemically healthy controls. Periodontal and dental indexes were measured, and stimulated saliva samples were collected. Salivary Th17 cytokine levels were analyzed by multiplex technique, and hBD 1-3 and SALSA levels by enzyme-linked immunosorbent assay. RESULTS: There were 19 gingivitis and 11 initial periodontitis patients in the Crohn's disease group, and 15 gingivitis and 4 initial periodontitis in the control group. In comparison to controls, higher salivary Th17 cytokine levels were observed in Crohn's disease patients. No statistical difference was observed between Crohn's disease and control groups in terms of their salivary hBD 1-3 and SALSA levels. Based on the regression analysis, there is no independent association between Crohn's disease and salivary Th17 cytokine levels. CONCLUSIONS: Crohn's disease does not relate to salivary antimicrobial hBD 1-3 or SALSA levels. While Crohn's disease patients have higher salivary Th17 cytokine levels in comparison to systemically healthy controls, an independent association between Crohn's disease and Th17 cytokine profile is still missing. CLINICAL RELEVANCE: Diminished Th17 cytokine response in Crohn's disease, which might be related to genetic susceptibility, can be also visualized in saliva.


Asunto(s)
Enfermedad de Crohn , Gingivitis , Periodontitis , beta-Defensinas , Humanos , Aglutininas , Estudios Transversales , Citocinas
2.
J Periodontal Res ; 58(3): 646-654, 2023 Jun.
Artículo en Inglés | MEDLINE | ID: mdl-37021333

RESUMEN

OBJECTIVE: To monitor salivary B-cell activating factor (BAFF), tumor necrosis factor-like weak inducer of apoptosis (TWEAK), and soluble (s)CD163 levels and arginase activity in periodontitis patients following nonsurgical periodontal treatment. BACKGROUND: BAFF, TWEAK, and sCD163 and arginase are associated with activities of B cells and macrophages, which are important regulators of periodontal immune-inflammatory response and healing following treatment. Increased salivary BAFF and sCD163 levels and arginase activity in periodontitis have been demonstrated, but their changes following treatment have not been evaluated before. MATERIALS AND METHODS: Forty-four Stage III/IV periodontitis patients and 35 periodontally healthy controls were included in the study. Full-mouth periodontal measurements were recorded and unstimulated saliva was obtained from all participants at baseline. Sample collection and measurements were repeated in periodontitis patients at 2, 6, 12, and 24 weeks following full-mouth scaling and root debridement, whereas controls were only seen at baseline. BAFF, TWEAK, and sCD163 levels were analyzed with bead-based multiplexed immunoassay. Arginase activity was measured with Chinard's method. RESULTS: BAFF (p < .001) and sCD163 (p = .003) levels and arginase activity (p < .015) were higher in periodontitis patients compared to healthy controls. BAFF levels (p < .001) and arginase activity (p < .001) of periodontitis patients were reduced at 2 weeks posttreatment and continued to decrease up to 6 (p = .038) and 12 weeks (p = .024), respectively. The reduction of sCD163 levels became significant (p = .003) at 24 weeks posttreatment. CONCLUSIONS: The decrease in salivary BAFF levels 2 weeks after periodontal treatment indicates a change in cell signaling toward limited B-cell activation. Decreasing arginase activity similarly reflects a significant reduction in inflammatory response. The reduction in sCD163 levels that are observed at 24 weeks may reflect a longstanding anti-inflammatory macrophage activation, given their multiple functions in immune response, inflammation, and healing.


Asunto(s)
Arginasa , Periodontitis , Humanos , Factor Activador de Células B , Antígenos CD , Periodontitis/terapia , Saliva
3.
Acta Odontol Scand ; 81(4): 267-277, 2023 May.
Artículo en Inglés | MEDLINE | ID: mdl-36436210

RESUMEN

OBJECTIVE: To comprehensively assess recent data on the effects of orthodontic forces on the dental pulp and to critically evaluate, whether any of the changes are permanent. MATERIALS AND METHODS: Articles published between 2/2009 and 2/2022 were searched electronically on the PubMed, EMBASE and SCOPUS databases. The initial search retrieved 780 publications and, applying the Preferred Reporting Items for Systematic Reviews and Meta-Analyses (PRISMA) guidelines, 33 relevant articles were identified. Twenty articles fulfilled the requirements for high (n = 1) or moderate (n = 19) methodological quality and were included. All assessments were made independently by three researchers. RESULTS: Orthodontic forces appeared to cause a reduction in pulpal blood flow and a reduction in tooth sensibility, as indicated by increased response thresholds and increased amounts of negative responses to tooth sensibility tests. In addition, there were increases in the expression or activity levels of enzymes and neuropeptides associated with hypoxia and inflammation. Fibrotic tissue formation in the pulp was also reported. CONCLUSIONS: Except for some histological and morphological alterations, the observed pulpal changes were in most cases only temporary, appearing within days of initiating the treatment and usually lasting for weeks. There were no clear signs of permanent damage.


Asunto(s)
Fuerza de la Mordida , Pulpa Dental , Humanos
4.
Acta Odontol Scand ; 81(6): 491-498, 2023 Aug.
Artículo en Inglés | MEDLINE | ID: mdl-37192014

RESUMEN

OBJECTIVES: Kombuchas and other tea-based beverages are often perceived as healthy products despite the lack of knowledge on their effects on oral health. This in vitro study determined the erosive potential of commercial kombuchas, and ice teas compared to cola drinks. MATERIALS AND METHODS: The pH and fluoride content of 7 kombuchas and 18 tea drinks were measured with ion-selective electrodes. Calcium dissolution from hydroxyapatite grains was quantified by atomic absorption spectroscopy after beverage exposure. The effect of beverages on the enamel surface was visualized by scanning electron microscopy (SEM). Distilled water, and cola drinks were used as negative and positive controls. RESULTS: The kombuchas exhibited lower pH values (2.82-3.66) than the ice teas (2.94-4.86), but still higher than the cola drinks (2.48-2.54). The fluoride concentration varied between 0.05 and 0.46 ppm and for 7 beverages the concentration was below the detection limit. The calcium release for kombuchas was 198-746 mg/l, for ice teas 16.1-507 mg/l, and for cola drinks 57.7-71.9 mg/l. Twenty-two beverages had a significantly greater calcium release than the cola drinks (p = .009-.014). The surface etching of the enamel was seen in the SEM analysis after beverage exposure. CONCLUSIONS: Tea-based beverages have even higher erosive potential than cola drinks. Kombuchas especially, displayed a considerable erosive potential.


Asunto(s)
Hielo , Erosión de los Dientes , Humanos , Hielo/análisis , Calcio , Fluoruros , Erosión de los Dientes/etiología , Bebidas , Bebidas Gaseosas/efectos adversos , , Concentración de Iones de Hidrógeno
5.
Int J Mol Sci ; 24(3)2023 Jan 25.
Artículo en Inglés | MEDLINE | ID: mdl-36768711

RESUMEN

Elevated serum immunoglobulin (Ig) antibody levels are observed in Crohn's disease patients. The aim of this study was to evaluate the salivary IgA and IgG antibody levels against Porphyromonas gingivalis, Tannerella forsythia, Aggregatibacter actinomycetemcomitans, and Prevotella intermedia in Crohn's disease patients. Eighty-eight participants (47 Crohn's disease patients and 41 systemically healthy age- and gender-matched controls) were included in the study. Oral and medical health statuses were recorded and salivary samples were collected. Salivary P. gingivalis, T. forsythia, A. actinomycetemcomitans, and P. intermedia carriage were analyzed with DNA sequencing technique, salivary levels of IgG1, IgG2, IgG3, IgG4, and IgM were measured with the Luminex® xMAP™ technique, and salivary IgA and IgG antibody levels against P. gingivalis, T. forsythia, A. actinomycetemcomitans, and P. intermedia were detected by ELISA. As result, higher salivary IgG2 (p = 0.011) and IgG3 (p = 0.006), P. gingivalis IgA (p < 0.001), A. actinomycetemcomitans IgG (p = 0.001), and P. intermedia IgG (p < 0.001) antibody levels were detected in the Crohn's disease group compared to the controls. Salivary P. gingivalis carriage was lower in the Crohn's disease group in comparison to the controls (p = 0.024). In conclusion, salivary IgA antibody responses against P. gingivalis and IgG antibody responses against P. intermedia have independent associations with Crohn's disease.


Asunto(s)
Enfermedad de Crohn , Periodontitis , Humanos , Inmunoglobulina G , Formación de Anticuerpos , Porphyromonas gingivalis , Inmunoglobulina A , Aggregatibacter actinomycetemcomitans , Anticuerpos Antibacterianos
6.
Med Microbiol Immunol ; 211(5-6): 261-267, 2022 Dec.
Artículo en Inglés | MEDLINE | ID: mdl-36053360

RESUMEN

Streptococcus pyogenes, also called group A streptococcus (GAS), is a human pathogen causing a wide range of infections ranging from mild tonsillitis to severe, life threatening conditions such as bacteraemia, necrotizing fasciitis, and streptococcal toxic shock syndrome. GAS may also colonise the oropharynx without causing any signs of disease which is known as asymptomatic carriage. This study aims to investigate IgA responses against GAS and oral streptococci from saliva samples collected from healthy Finnish adults. In addition, asymptomatic throat GAS carriage was studied. The study participants consisted of healthy adult volunteers who provided one saliva sample, a throat swab, and a background questionnaire. Total salivary IgA, and GAS specific IgA were analysed from the saliva samples using enzyme-linked immunosorbent assays (ELISA) and the results were compared to oral streptococci specific IgA levels. Asymptomatic GAS throat carriers were identified by bacterial culture, and the isolates were emm typed. Samples from a total of 182 individuals were analysed. The median salivary IgA concentration was 62.9 µg/ml (range 17.3-649.9 µg/ml), and median GAS and oral streptococcal specific IgA concentrations 2.7 and 3.3 arbitrary units (AU, range 1.4-7.4 AU and 1.6-12.0 AU), respectively. Three individuals with asymptomatic GAS throat carriage were identified.


Asunto(s)
Infecciones Estreptocócicas , Streptococcus pyogenes , Adulto , Humanos , Finlandia/epidemiología , Infecciones Estreptocócicas/epidemiología , Infecciones Estreptocócicas/microbiología , Inmunoglobulina A Secretora , Faringe/microbiología
7.
BMC Microbiol ; 20(1): 184, 2020 06 29.
Artículo en Inglés | MEDLINE | ID: mdl-32600259

RESUMEN

BACKGROUND: Regular consumption of xylitol decreases the number of cariogenic streptococci in dental plaque. In vitro biofilm models to study the mechanism of xylitol action have been set-up, but the obtained results are contradictory. Biofilm growth is a dynamic process with time-specific characteristics that may remain undetected in conventional end-point biofilm tests. In this study we used an impedance spectroscopy instrument, xCELLigence Real Time Cell Analyzer (RTCA), that allows label-free, non-invasive real-time monitoring of biofilm formation, to explore effects of xylitol on biofilm formation by Streptococcus mutans. Based on the obtained information of biofilm dynamics, we assessed the number of viable bacteria, the polysaccharide content, and the expression levels of selected genes involved in glucan-mediated biofilm formation in different biofilm stages. Xylitol inhibition was compared with that of erythritol; another polyol suggested to have a positive impact on oral health. RESULTS: Our results showed that real-time monitoring provided new information of polyol-induced changes in S. mutans biofilm formation dynamics. The inhibitory effect of polyols was more pronounced in the early stages of biofilm formation but affected also the measured total amount of formed biofilm. Effects seen in the real-time biofilm assay were only partially explained by changes in CFU values and polysaccharide amounts in the biofilms. Both xylitol and erythritol inhibited real-time biofilm formation by all the nine tested S. mutans strains. Sensitivity of the strains to inhibition varied: some were more sensitive to xylitol and some to erythritol. Xylitol also modified the expression levels of gbpB, gtfB, gtfC and gtfD genes that are important in polysaccharide-mediated adherence of S. mutans. CONCLUSION: The erythritol- and xylitol- induced inhibition of biofilm formation was only partly explained by decrease in the number of viable S. mutans cells or the amount of polysaccharides in the biofilm matrix, suggesting that in addition to reduced proliferation also the matrix composition and thereby the surface attachment quality of biofilm matrix may be altered by the polyols.


Asunto(s)
Biopelículas/efectos de los fármacos , Eritritol/farmacología , Streptococcus mutans/fisiología , Xilitol/farmacología , Proteínas Bacterianas/genética , Biopelículas/crecimiento & desarrollo , Espectroscopía Dieléctrica/instrumentación , Regulación Bacteriana de la Expresión Génica/efectos de los fármacos , Viabilidad Microbiana/efectos de los fármacos , Polisacáridos Bacterianos/metabolismo , Streptococcus mutans/efectos de los fármacos
8.
J Immunol ; 193(10): 5240-8, 2014 Nov 15.
Artículo en Inglés | MEDLINE | ID: mdl-25320275

RESUMEN

The salivary scavenger and agglutinin (SALSA), also known as gp340 and dmbt1, is an antimicrobial and inflammation-regulating molecule located at the mucosal surfaces. The present study revealed that SALSA was present in the amniotic fluid (AF) and exceptionally enriched in both meconium and feces of infants. Based on immunological and mass spectrometric analysis, SALSA was estimated to constitute up to 4-10% of the total protein amount in meconium, making it one of the most abundant proteins. SALSA proteins in the AF and intestinal samples were polymorphic and exhibited varying polypeptide compositions. In particular, a different abundance of peptides corresponding to functionally important structures was found in the AF and intestinal SALSA. The AF form of SALSA had a more intact structure and contained peptides from the zona pellucida domain, which is involved in cell differentiation and oligomerization. In contrast, the intestinal SALSA was more enriched with the scavenger receptor cysteine-rich domains. The AF, but not the meconium SALSA, bound to Streptococcus pyogenes, S. agalactiae, S. gordonii, and Escherichia coli. Furthermore, differential binding was observed also to known endogenous ligands C1q, mannose-binding lectin, and secretory IgA. Our results have thus identified mucosal body compartments, where SALSA is particularly abundant, and suggest that SALSA exhibits varying functions in the different mucosal locations. The high levels of SALSA in AF and the infant intestine suggest a robust and important function for SALSA during the fetal development and in the mucosal innate immune defense of infants.


Asunto(s)
Líquido Amniótico/inmunología , Inmunidad Mucosa , Intestinos/inmunología , Fragmentos de Péptidos/química , Receptores de Superficie Celular/química , Secuencia de Aminoácidos , Líquido Amniótico/química , Proteínas de Unión al Calcio , Complemento C1q/inmunología , Complemento C1q/metabolismo , Proteínas de Unión al ADN , Escherichia coli/química , Escherichia coli/inmunología , Expresión Génica , Humanos , Inmunoglobulina A/inmunología , Inmunoglobulina A/metabolismo , Recién Nacido , Intestinos/química , Lectina de Unión a Manosa/inmunología , Lectina de Unión a Manosa/metabolismo , Meconio/química , Meconio/inmunología , Modelos Moleculares , Datos de Secuencia Molecular , Especificidad de Órganos , Mapeo Peptídico , Unión Proteica , Estructura Terciaria de Proteína , Receptores de Superficie Celular/inmunología , Receptores de Superficie Celular/metabolismo , Streptococcus/química , Streptococcus/inmunología , Proteínas Supresoras de Tumor
9.
Dent J (Basel) ; 12(2)2024 Feb 17.
Artículo en Inglés | MEDLINE | ID: mdl-38392244

RESUMEN

S. mutans is a key pathogen in dental caries initiation and progression. It promotes oral biofilm dysbiosis and biofilm acidification. Sodium resinate is a salt of pine-oil-derived resin which has antimicrobial properties. Pine-oil-derived resin consists of terpenes, diterpenes, and abietic acids. The aim of this study was to determine the effects of pine (Pinus sylvestris) oil resinate (RS) on growth and acid production of cariogenic S. mutans strains in planktonic form and biofilm. The S. mutans type strain NCTC10449 and clinical isolate CI2366 were grown on 96-well plates for testing of RS effects on growth and biofilm formation, and on plates with integrated pH-sensitive optical ensors for real-time measurements of the effects of RS on bacterial acid production. We found that even short-time exposure to RS inhibits the growth and acid production of S. mutans in the planktonic phase and biofilms. In addition, RS was able to penetrate the biofilm matrix and reduce acid production inside S. mutans biofilm. RS thus shows potential as a novel antibacterial agent against cariogenic bacteria in biofilm.

10.
Artículo en Inglés | MEDLINE | ID: mdl-23695577

RESUMEN

Streptococcus pyogenes protein 0843 (Spy0843) is a recently identified protein with a potential adhesin function. Sequence analysis has shown that Spy0843 contains two leucine-rich repeat (LRR) domains that mediate interactions with the gp340 receptor. Here, the C-terminal LRR domain was overexpressed in Escherichia coli, purified and crystallized in the presence of 1.7-1.8 M ammonium sulfate pH 7.4 as precipitant. Data were collected from a single crystal to 1.59 Šresolution at 100 K at a synchrotron-radiation source. The crystal was found to belong to space group I41, with unit-cell parameters a = b = 121.4, c = 51.5 Šand one molecule in the asymmetric unit. Elucidation of the crystal structure will provide insights into the interactions of Spy0843 with the gp340 receptor and a better understanding of the role of Spy0843 in streptococcal infections.


Asunto(s)
Proteínas Bacterianas/química , Proteínas Bacterianas/aislamiento & purificación , Regulación Bacteriana de la Expresión Génica , Streptococcus pyogenes , Proteínas Bacterianas/genética , Cristalización , Leucina/química , Leucina/metabolismo , Estructura Terciaria de Proteína , Infecciones Estreptocócicas/metabolismo , Streptococcus pyogenes/química , Streptococcus pyogenes/genética
11.
J Periodontol ; 94(1): 130-140, 2023 01.
Artículo en Inglés | MEDLINE | ID: mdl-35712915

RESUMEN

BACKGROUND: The aim of this study was to evaluate oral bacteria- and interleukin (IL)-1ß-induced protein and mRNA expression profiles of monocyte chemoattractant protein-1-induced protein (MCPIP)-1 and mucosa-associated lymphoid tissue lymphoma translocation protein (MALT)-1 in human gingival keratinocyte monolayers and organotypic oral mucosal models. METHODS: Human gingival keratinocyte (HMK) monolayers were incubated with Porphyromonas gingivalis, Fusobacterium nucleatum, P. gingivalis lipopolysaccharide (LPS) and IL-1ß. The protein levels of MCPIP-1 and MALT-1 were examined by immunoblots and mRNA levels by qPCR. MCPIP-1 and MALT-1 protein expression levels were also analyzed immunohistochemically using an organotypic oral mucosal model. One-way analysis of variance followed by Tukey correction was used in statistical analyses. RESULTS: In keratinocyte monolayers, MCPIP-1 protein expression was suppressed by F. nucleatum and MALT-1 protein expression was suppressed by F. nucleatum, P. gingivalis LPS and IL-1ß. P. gingivalis seemed to degrade MCPIP-1 and MALT-1 at all tested time points and degradation was inhibited when P. gingivalis was heat-killed. MCPIP-1 mRNA levels were increased by P. gingivalis, F. nucleatum, and IL-1ß, however, no changes were observed in MALT-1 mRNA levels. CONCLUSION: Gingival keratinocyte MCPIP-1 and MALT-1 mRNA and protein expression responses are regulated by infection and inflammatory mediators. These findings suggest that periodontitis-associated bacteria-induced modifications in MCPIP-1 and MALT-1 responses can be a part of periodontal disease pathogenesis.


Asunto(s)
Lipopolisacáridos , Linfoma de Células B de la Zona Marginal , Humanos , Interleucina-1beta/metabolismo , Lipopolisacáridos/farmacología , Lipopolisacáridos/metabolismo , Quimiocina CCL2/metabolismo , Proteína 1 de la Translocación del Linfoma del Tejido Linfático Asociado a Mucosas/metabolismo , Linfoma de Células B de la Zona Marginal/metabolismo , Encía/metabolismo , Porphyromonas gingivalis/metabolismo , Fusobacterium nucleatum/fisiología , Queratinocitos/metabolismo , ARN Mensajero/metabolismo
12.
J Bacteriol ; 194(10): 2509-19, 2012 May.
Artículo en Inglés | MEDLINE | ID: mdl-22389474

RESUMEN

Glutamine synthetase (GS) and glucose-6-phosphate isomerase (GPI) were identified as novel adhesive moonlighting proteins of Lactobacillus crispatus ST1. Both proteins were bound onto the bacterial surface at acidic pHs, whereas a suspension of the cells to pH 8 caused their release into the buffer, a pattern previously observed with surface-bound enolase and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) of L. crispatus. The pH shift was associated with a rapid and transient increase in cell wall permeability, as measured by cell staining with propidium iodide. A gradual increase in the release of the four moonlighting proteins was also observed after the treatment of L. crispatus ST1 cells with increasing concentrations of the antimicrobial cationic peptide LL-37, which kills bacteria by disturbing membrane integrity and was here observed to increase the cell wall permeability of L. crispatus ST1. At pH 4, the fusion proteins His(6)-GS, His(6)-GPI, His(6)-enolase, and His(6)-GAPDH showed localized binding to cell division septa and poles of L. crispatus ST1 cells, whereas no binding to Lactobacillus rhamnosus GG was detected. Strain ST1 showed a pH-dependent adherence to the basement membrane preparation Matrigel. Purified His(6)-GS and His(6)-GPI proteins bound to type I collagen, and His(6)-GS also bound to laminin, and their level of binding was higher at pH 5.5 than at pH 6.5. His(6)-GS also expressed a plasminogen receptor function. The results show the strain-dependent surface association of moonlighting proteins in lactobacilli and that these proteins are released from the L. crispatus surface after cell trauma, under conditions of alkaline stress, or in the presence of the antimicrobial peptide LL-37 produced by human cells.


Asunto(s)
Péptidos Catiónicos Antimicrobianos/farmacología , Regulación Bacteriana de la Expresión Génica/fisiología , Glucosa-6-Fosfato Isomerasa/metabolismo , Glutamato-Amoníaco Ligasa/metabolismo , Lactobacillus/efectos de los fármacos , Lactobacillus/enzimología , Adhesión Bacteriana/fisiología , Proteínas Bacterianas/genética , Proteínas Bacterianas/metabolismo , Clonación Molecular , Regulación Enzimológica de la Expresión Génica/fisiología , Glucosa-6-Fosfato Isomerasa/genética , Glutamato-Amoníaco Ligasa/genética , Humanos , Concentración de Iones de Hidrógeno , Lactobacillus/citología , Lactobacillus/genética , Proteínas de la Membrana/genética , Proteínas de la Membrana/metabolismo , Unión Proteica , Catelicidinas
13.
J Biol Chem ; 286(45): 38854-64, 2011 Nov 11.
Artículo en Inglés | MEDLINE | ID: mdl-21908601

RESUMEN

Bacterial adhesion is often a prerequisite for infection, and host cell surface carbohydrates play a major role as adhesion receptors. Streptococci are a leading cause of infectious diseases. However, only few carbohydrate-specific streptococcal adhesins are known. Streptococcus suis is an important pig pathogen and a zoonotic agent causing meningitis in pigs and humans. In this study, we have identified an adhesin that mediates the binding of S. suis to galactosyl-α1-4-galactose (Galα1-4Gal)-containing host receptors. A functionally unknown S. suis cell wall protein (SSU0253), designated here as SadP (streptococcal adhesin P), was identified using a Galα1-4Gal-containing affinity matrix and LC-ESI mass spectrometry. Although the function of the protein was not previously known, it was recently identified as an immunogenic cell wall protein in a proteomic study. Insertional inactivation of the sadP gene abolished S. suis Galα1-4Gal-dependent binding. The adhesin gene sadP was cloned and expressed in Escherichia coli. Characterization of its binding specificity showed that SadP recognizes Galα1-4Gal-oligosaccharides and binds its natural glycolipid receptor, GbO(3) (CD77). The N terminus of SadP was shown to contain a Galα1-Gal-binding site and not to have apparent sequence similarity to other bacterial adhesins, including the E. coli P fimbrial adhesins, or to E. coli verotoxin or Pseudomonas aeruginosa lectin I also recognizing the same Galα1-4Gal disaccharide. The SadP and E. coli P adhesins represent a unique example of convergent evolution toward binding to the same host receptor structure.


Asunto(s)
Adhesinas Bacterianas , Disacáridos , Evolución Molecular , Streptococcus suis , Trihexosilceramidas/química , Trihexosilceramidas/metabolismo , Adhesinas Bacterianas/química , Adhesinas Bacterianas/genética , Adhesinas Bacterianas/metabolismo , Animales , Clonación Molecular , Disacáridos/química , Disacáridos/genética , Disacáridos/metabolismo , Escherichia coli/química , Escherichia coli/genética , Escherichia coli/metabolismo , Expresión Génica , Glicoproteínas/química , Glicoproteínas/genética , Glicoproteínas/metabolismo , Humanos , Espectrometría de Masas , Mutación , Unión Proteica , Proteómica , Streptococcus suis/química , Streptococcus suis/genética , Streptococcus suis/metabolismo , Porcinos , Enfermedades de los Porcinos
14.
Biochem Biophys Res Commun ; 423(3): 577-82, 2012 Jul 06.
Artículo en Inglés | MEDLINE | ID: mdl-22695115

RESUMEN

Pathogenesis of many bacterially-induced inflammatory diseases is driven by Toll-like receptor (TLR) mediated immune responses following recognition of bacterial factors by different TLRs. Periodontitis is a chronic inflammation of the tooth supporting apparatus often leading to tooth loss, and is caused by a Gram-negative bacterial consortium that includes Tannerella forsythia. This bacterium expresses a virulence factor, the BspA, which drives periodontal inflammation by activating TLR2. The N-terminal portion of the BspA protein comprises a leucine-rich repeat (LRR) domain previously shown to be involved in the binding and activation of TLR2. The objective of the current study was to identify specific epitopes in the LRR domain of BspA that interact with TLR2. Our results demonstrate that a sequence motif GC(S/T)GLXSIT is involved in mediating the interaction of BspA with TLR2. Thus, our study has identified a peptide motif that mediates the binding of a bacterial protein to TLR2 and highlights the promiscuous nature of TLR2 with respect to ligand binding. This work could provide a structural basis for designing peptidomimetics to modulate the activity of TLR2 in order to block bacterially-induced inflammation.


Asunto(s)
Proteínas Bacterianas/metabolismo , Bacteroidetes/metabolismo , Proteínas de la Membrana/metabolismo , Receptor Toll-Like 2/metabolismo , Secuencias de Aminoácidos , Secuencia de Aminoácidos , Animales , Proteínas Bacterianas/química , Células HEK293 , Humanos , Leucina , Proteínas de la Membrana/química , Ratones , Ratones Endogámicos BALB C , Datos de Secuencia Molecular , Fragmentos de Péptidos/química , Fragmentos de Péptidos/metabolismo , Periodontitis/microbiología , Mapas de Interacción de Proteínas , Estructura Terciaria de Proteína , Receptor Toll-Like 2/química , Receptor Toll-Like 2/genética , Tripsina/química
15.
J Infect Dis ; 204(1): 65-73, 2011 Jul 01.
Artículo en Inglés | MEDLINE | ID: mdl-21628660

RESUMEN

BACKGROUND: Decorin adherence is crucial in the pathogenesis of Lyme borreliosis. Decorin-binding proteins (Dbp) A and B are the adhesins that mediate this interaction. DbpA and B of Borrelia garinii, Borrelia afzelii, and Borrelia burgdorferi sensu stricto (ss) differ in their amino acid sequence, but little attention has been paid to the potential difference in their decorin binding. METHODS: We expressed recombinant DbpA and DbpB of B. garinii, B. afzelii, and B. burgdorferi ss and studied their binding to decorin. We also generated recombinant Borrelia strains to study the role of DbpA and DbpB in the adhesion of live spirochetes to decorin and decorin-expressing cells. RESULTS. Recombinant DbpA of B. garinii and DbpB of B. garinii and B. burgdorferi ss showed strong binding to decorin, whereas DbpA of B. burgdorferi ss and both DbpA and DbpB of B. afzelii exhibited no or only minor binding activity. DbpA and DbpB of B. garinii and B. burgdorferi ss also supported the adhesion of whole spirochetes to decorin and decorin-expressing cells, whereas DbpA and DbpB of B. afzelii did not exhibit this activity. CONCLUSIONS: Dbp A and B of B. garinii and B. burgdorferi ss mediate the interaction between the spirochete and decorin, whereas the same adhesins of B. afzelii show only negligible activity.


Asunto(s)
Adhesinas Bacterianas/metabolismo , Grupo Borrelia Burgdorferi/metabolismo , Borrelia burgdorferi/metabolismo , Decorina/metabolismo , Expresión Génica , Humanos , Unión Proteica , Proteínas Recombinantes/metabolismo
16.
Viruses ; 14(11)2022 11 20.
Artículo en Inglés | MEDLINE | ID: mdl-36423177

RESUMEN

Oral infections with high-risk (hr)HPV genotypes are associated with a subset of head and neck squamous cell carcinomas. Oral hrHPV infections may result from having oral sex, but also from horizontal infection from mouth to mouth. In such cases, saliva can serve as a vehicle for HPV transmission. Still, the prevalence and dynamics of salivary HPV antibodies in healthy non-vaccinated individuals are poorly known and the role of the salivary antibodies in protection from oral HPV infection is unclear. We used an ELISA assay to evaluate the dynamics and correlation of oral HPV16 infection and HPV16L1 and E7 specific antibody levels in saliva and serum samples among 39 women, 13 of which had persistent oral HPV16 infection. The women were mothers-to-be, sampled before delivery and followed up for 36 months postpartum. HPV16L1 IgG and sIgA antibodies were regularly detected in saliva. Antibody levels in serum remained stable during the 36-month follow-up, while antibody levels in saliva fluctuated. There was considerable individual variation in salivary HPV16L1 antibody levels, and some women had persistent oral HPV16 infection but no salivary antibodies. No differences in salivary HPV16L1 levels were found between the women with persistent or transient oral HPV16 infection.


Asunto(s)
Neoplasias de Cabeza y Cuello , Enfermedades de la Boca , Infecciones por Papillomavirus , Humanos , Femenino , Embarazo , Papillomavirus Humano 16 , Mujeres Embarazadas , Anticuerpos Antivirales
17.
Microorganisms ; 10(11)2022 Nov 07.
Artículo en Inglés | MEDLINE | ID: mdl-36363792

RESUMEN

Previous studies have indicated that the exopolysaccharides of lactic acid bacteria exhibit antibiofilm activity against non-oral bacteria by preventing their initial adhesion to surfaces and by downregulating the expression of genes responsible for their biofilm formation. The aims of this study were to (1) characterize the exopolysaccharides (EPSs) of Lactobacillus plantarum EIR/IF-1 postbiotics, (2) test their antibiofilm effect on dual biofilms, and (3) evaluate their bacterial auto-aggregation, co-aggregation, and hydrocarbon-binding inhibitory activity. The EPSs were characterized by FTIR, HPLC, and thermogravimetric analysis. Bacterial auto- and co-aggregation were tested by Kolenbrander's method and hydrocarbon binding was tested by Rosenberg's method. Dual biofilms were formed by culturing Fusobacterium nucleatum ATCC 25586 with one of the following bacteria: Prevotella denticola ATCC 33185, P. denticola AHN 33266, Porphyromonas gingivalis ATCC 33277, P. gingivalis AHN 24155, and Filifactor alocis ATCC 35896. The EPSs contained fractions with different molecular weights (51 and 841 kDa) and monosaccharides of glucose, galactose, and fructose. The EPSs showed antibiofilm activity in all the biofilm models tested. The EPSs may have inhibited bacterial aggregation and binding to hydrocarbons by reducing bacterial hydrophobicity. In conclusion, the EPSs of L. plantarum EIR/IF-1, which consists of two major fractions, exhibited antibiofilm activity against oral bacteria, which can be explained by the inhibitory effect of EPSs on the auto-aggregation and co-aggregation of bacteria and their binding to hydrocarbons.

18.
Phytother Res ; 24 Suppl 1: S95-101, 2010 Jan.
Artículo en Inglés | MEDLINE | ID: mdl-19610031

RESUMEN

Antiadhesion therapy is a promising approach to the fight against pathogens. Antibiotic resistance and the lack of effective vaccines have increased the search for new methods to prevent infectious diseases. Previous studies have shown the antiadhesion activity of juice from cultivated cranberries (Vaccinium macrocarpon Ait.) against bacteria, especially E. coli. In this study, the binding of two streptococcal strains, Streptococcus pneumoniae and Streptococcus agalactiae, to molecular size fractions (FI, FII and FIII, <10 kDa, 10-100 kDa, and >100 kDa, respectively) of berries and berry and fruit juices from 12 plant species were studied using a microtiter well assay. For Streptococcus suis a hemagglutination inhibition assay was used. In general, binding activity was detected especially to wild cranberry (Vaccinium oxycoccos L.) and to other Vaccinium species. S. pneumoniae cells bound most to cranberry juice fraction FI and S. agalactiae cells to cranberry fraction FIII. Hemagglutination induced by S. suis was most effectively inhibited by cranberry fraction FII. NMR spectra of some characteristic active and non-active fractions were also measured. They indicate that fractions FII and FIII contained proanthocyanidins and/or other phenolic compounds. The results suggest Vaccinium berries as possible sources of antiadhesives against bacterial infections.


Asunto(s)
Adhesión Bacteriana/efectos de los fármacos , Frutas/química , Extractos Vegetales/farmacología , Vaccinium/química , Antibacterianos/farmacología , Bebidas , Eritrocitos/efectos de los fármacos , Eritrocitos/microbiología , Pruebas de Inhibición de Hemaglutinación , Humanos , Streptococcus agalactiae/efectos de los fármacos , Streptococcus pneumoniae/efectos de los fármacos , Streptococcus suis/efectos de los fármacos
19.
Life Sci Alliance ; 3(4)2020 04.
Artículo en Inglés | MEDLINE | ID: mdl-32098784

RESUMEN

The scavenger receptor cysteine-rich (SRCR) family of proteins comprises more than 20 membrane-associated and secreted molecules. Characterised by the presence of one or more copies of the ∼110 amino-acid SRCR domain, this class of proteins have widespread functions as antimicrobial molecules, scavenger receptors, and signalling receptors. Despite the high level of structural conservation of SRCR domains, no unifying mechanism for ligand interaction has been described. The SRCR protein SALSA, also known as DMBT1/gp340, is a key player in mucosal immunology. Based on detailed structural data of SALSA SRCR domains 1 and 8, we here reveal a novel universal ligand-binding mechanism for SALSA ligands. The binding interface incorporates a dual cation-binding site, which is highly conserved across the SRCR superfamily. Along with the well-described cation dependency on most SRCR domain-ligand interactions, our data suggest that the binding mechanism described for the SALSA SRCR domains is applicable to all SRCR domains. We thus propose to have identified in SALSA a conserved functional mechanism for the SRCR class of proteins.


Asunto(s)
Proteínas de Unión al Calcio/genética , Proteínas de Unión al Calcio/ultraestructura , Proteínas de Unión al ADN/genética , Proteínas de Unión al ADN/ultraestructura , Proteínas Supresoras de Tumor/genética , Proteínas Supresoras de Tumor/ultraestructura , Secuencia de Aminoácidos/genética , Sitios de Unión/genética , Proteínas de Unión al Calcio/metabolismo , Cisteína/metabolismo , Proteínas de Unión al ADN/metabolismo , Humanos , Ligandos , Unión Proteica/genética , Dominios Proteicos/genética , Receptores de Superficie Celular/genética , Receptores de Superficie Celular/metabolismo , Receptores Depuradores/genética , Receptores Depuradores/metabolismo , Receptores Depuradores/ultraestructura , Proteínas Supresoras de Tumor/metabolismo
20.
J Virol Methods ; 270: 26-33, 2019 08.
Artículo en Inglés | MEDLINE | ID: mdl-31004663

RESUMEN

Human papilloma viruses (HPV) are a common cause of transient infections on mucosal surfaces, also in the oral cavity. Some infections remain persistent and can, especially with high risk HPV genotypes, lead to malignancies in the oral-oropharyngeal area. Our understanding of the natural course of oral HPV infections is limited, and the local host responses are poorly known. In this study we show that anti-HPV16L1 antibodies, the IgA response being most abundant, can be measured in saliva of asymptomatic males. HPV16L1 specific multiplex serology and commercial ELISA methods were compared and also the total salivary IgA levels measured. The total salivary IgA concentrations varied from 36 to 163 µg/ml. All the assays could detect anti-HPV16 IgA from saliva, but the correlation between assays varied from non-significant 0.22 to highly significant 0.81, p < 0.01. Salivary antibody responses did not correlate with the antibody responses detected in serum (Spearman correlations between -0.12 and 0.16) not even after adjusting the specific responses to differences in total IgA in saliva. Only six of 34 individuals were HPV16 DNA positive at the time of the sampling, but interestingly, three out of four with oral HPV16 DNA had salivary anti-HPV16 IgA responses below average. In conclusion, our results show that anti-HPV16 antibodies can be measured from saliva and the salivary response differs from that of serum. Individual differences in total salivary antibody concentrations may affect also the amount of HPV16 specific antibodies in saliva. Furthermore, different assay methods showed different specificities; thus comparisons between studies must be done with care.


Asunto(s)
Anticuerpos Antivirales/análisis , Ensayo de Inmunoadsorción Enzimática , Papillomavirus Humano 16/inmunología , Inmunoglobulina A/análisis , Saliva/inmunología , Suero/inmunología , Adulto , Formación de Anticuerpos , Voluntarios Sanos , Humanos , Masculino , Boca , Infecciones por Papillomavirus/inmunología , Estudios Prospectivos
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