Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR29266538_1.fastq.gz | Fastqsanger.gz | |||
| SRR29266538_2.fastq.gz | Fastqsanger.gz | |||
| SRR29266539_1.fastq.gz | Fastqsanger.gz | |||
| SRR29266539_2.fastq.gz | Fastqsanger.gz | |||
| SRR29266540_1.fastq.gz | Fastqsanger.gz |
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Project description:To combat dental implant-associated infections, there is a need for novel materials which effectively inhibit bacterial biofilm formation. In the present study, a titanium surface functionalization based on the “slippery liquid-infused porous surfaces” (SLIPS) principle was analyzed in an oral flow chamber system. The immobilized liquid layer was stable over 13 days of continuous flow. With increasing flow rates, the surface exhibited a significant reduction in attached biofilm of both the oral initial colonizer Streptococcus oralis and an oral multi-species biofilm composed of S. oralis, Actinomyces naeslundii, Veillonella dispar and Porphyromonas gingivalis. Using single cell force spectroscopy, reduced bacterial adhesion forces on the lubricant layer could be measured. Gene expression patterns in biofilms on SLIPS, on control surfaces and planktonic cultures were also compared. For this purpose, the genome of S. oralis strain ATCC® 9811TM was sequenced using PacBio Sequel technology. Even though biofilm cells showed clear changes in gene expression compared to planktonic cells, no differences could be detected between bacteria on SLIPS and on control surfaces. Therefore, it can be concluded that the ability of liquid-infused titanium to repel biofilms is solely due to weakened bacterial adhesion to the underlying liquid interface.
2020-05-10 | GSE129981 | GEO
Project description:Microbial Aggregates in Human Saliva Build the Oral Biofilm
| PRJNA739848 | ENA
Project description:Oral biofilms, comprising hundreds of bacteria and other microorganisms on oral mucosal and dental surfaces, play a central role in oral health and disease dynamics. Streptococcus oralis, a key constituent of these biofilms, contribute significantly to their formation, serving as an early colonizer and microcolony scaffold. The interaction between S. oralis and the orally predominant mucin, MUC5B, is pivotal in biofilm development, yet the mechanism underlying MUC5B degradation remains poorly understood. This study introduces MdpS (Mucin Degrading Protease from Streptococcus oralis), a protease that extensively hydrolyses MUC5B and offers an insight into its sequence homology, physicochemical properties, and substrate- and amino acid specificity. MdpS exhibits high sequence conservation within the species and also explicitly among early biofilm colonizing streptococci. It is characterized as a calcium or magnesium dependent serine protease with strict physicochemical preferences, including narrow pH and temperature tolerance, and high sensitivity to increased sodium chloride and reducing agent concentrations. Furthermore, MdpS primarily hydrolyze proteins with O-glycans, but also show activity towards immunoglobulins IgA1/2 and IgM, suggesting potential immunomodulatory effects. Significantly, MdpS extensively degrades MUC5B in the N- and C-terminal domains, emphasizing its role in mucin degradation with implications in carbon and nitrogen sequestration for S. oralis with a potential function by cross-feeding the oral biofilm. Moreover, the enzyme displays amino acid preferences of serine, threonine or cysteine depending on substrate glycosylation. Understanding the interplay between S. oralis and MUC5B, facilitated by MdpS, has significant implications for the management of a healthy eubiotic oral microenvironment, offering potential targets for interventions aimed at modulating oral biofilm composition and succession. Additionally, the MdpS data challenges the presently acknowledged model of MUC5B degradation, because contrarily MdpS does not necessitate O-glycan removal prior to extensive peptide backbone hydrolysis. These findings emphasize the necessity for further research in this field.
2024-02-14 | PXD046954 | Pride
Project description:Oral biofilms, comprising hundreds of bacteria and other microorganisms on oral mucosal and dental surfaces, play a central role in oral health and disease dynamics. Streptococcus oralis, a key constituent of these biofilms, contribute significantly to their formation, serving as an early colonizer and microcolony scaffold. The interaction between S. oralis and the orally predominant mucin, MUC5B, is pivotal in biofilm development, yet the mechanism underlying MUC5B degradation remains poorly understood. This study introduces MdpS (Mucin Degrading Protease from Streptococcus oralis), a protease that extensively hydrolyses MUC5B and offers an insight into its sequence homology, physicochemical properties, and substrate- and amino acid specificity. MdpS exhibits high sequence conservation within the species and also explicitly among early biofilm colonizing streptococci. It is characterized as a calcium or magnesium dependent serine protease with strict physicochemical preferences, including narrow pH and temperature tolerance, and high sensitivity to increased sodium chloride and reducing agent concentrations. Furthermore, MdpS primarily hydrolyze proteins with O-glycans, but also show activity towards immunoglobulins IgA1/2 and IgM, suggesting potential immunomodulatory effects. Significantly, MdpS extensively degrades MUC5B in the N- and C-terminal domains, emphasizing its role in mucin degradation with implications in carbon and nitrogen sequestration for S. oralis with a potential function by cross-feeding the oral biofilm. Moreover, the enzyme displays amino acid preferences of serine, threonine or cysteine depending on substrate glycosylation. Understanding the interplay between S. oralis and MUC5B, facilitated by MdpS, has significant implications for the management of a healthy eubiotic oral microenvironment, offering potential targets for interventions aimed at modulating oral biofilm composition and succession. Additionally, the MdpS data challenges the presently acknowledged model of MUC5B degradation, because contrarily MdpS does not necessitate O-glycan removal prior to extensive peptide backbone hydrolysis. These findings emphasize the necessity for further research in this field.
2024-04-18 | PXD046810 | Pride