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Leo, F., Lood, R., Thomsson, K. A., Nilsson, J., Svensäter, G. & Wickström, C. (2024). Characterization of MdpS: an in-depth analysis of a MUC5B-degrading protease from Streptococcus oralis. Frontiers in Microbiology, 15, Article ID 1340109.
Open this publication in new window or tab >>Characterization of MdpS: an in-depth analysis of a MUC5B-degrading protease from Streptococcus oralis
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2024 (English)In: Frontiers in Microbiology, E-ISSN 1664-302X, Vol. 15, article id 1340109Article in journal (Refereed) Published
Abstract [en]

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, contributes significantly to the formation of which, 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 evolutionary conservation, 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 a calcium or magnesium dependent serine protease with strict physicochemical preferences, including narrow pH and temperature tolerance, and high sensitivity to increasing concentrations of sodium chloride and reducing agents. Furthermore, MdpS primarily hydrolyzes proteins with O-glycans, but also shows activity toward 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 for carbon and nitrogen sequestration for S. oralis or oral biofilm cross-feeding. Moreover, depending on substrate glycosylation, the amino acids serine, threonine or cysteine triggers the enzymatic action. 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, since MdpS does not rely on O-glycan removal prior to extensive peptide backbone hydrolysis, the MdpS data challenges the current model of MUC5B degradation. These findings emphasize the necessity for further research in this field.

Place, publisher, year, edition, pages
Frontiers Media S.A., 2024
Keywords
MUC5B, O-glycosylation, Streptococcus oralis, mucin degradation, oral biofilm, serine protease.
National Category
Dentistry
Identifiers
urn:nbn:se:mau:diva-66146 (URN)10.3389/fmicb.2024.1340109 (DOI)001155181600001 ()38304711 (PubMedID)2-s2.0-85183933839 (Scopus ID)
Available from: 2024-02-27 Created: 2024-02-27 Last updated: 2024-02-27Bibliographically approved
Leo, F., Svensäter, G., Lood, R. & Wickström, C. (2023). Characterization of a highly conserved MUC5B-degrading protease, MdpL, from Limosilactobacillus fermentum. Frontiers in Microbiology, 14, Article ID 1127466.
Open this publication in new window or tab >>Characterization of a highly conserved MUC5B-degrading protease, MdpL, from Limosilactobacillus fermentum
2023 (English)In: Frontiers in Microbiology, E-ISSN 1664-302X, Vol. 14, article id 1127466Article in journal (Refereed) Published
Abstract [en]

MUC5B is the predominant glycoprotein in saliva and is instrumental in the establishment and maintenance of multi-species eubiotic biofilms in the oral cavity. Investigations of the aciduric Lactobacillaceae family, and its role in biofilms emphasizes the diversity across different genera of the proteolytic systems involved in the nutritional utilization of mucins. We have characterized a protease from Limosilactobacillus fermentum, MdpL (Mucin degrading protease from Limosilactobacillus) with a high protein backbone similarity with commensals that exploit mucins for attachment and nutrition. MdpL was shown to be associated with the bacterial cell surface, in close proximity to MUC5B, which was sequentially degraded into low molecular weight fragments. Mapping the substrate preference revealed multiple hydrolytic sites of proteins with a high O-glycan occurrence, although hydrolysis was not dependent on the presence of O-glycans. However, since proteolysis of immunoglobulins was absent, and general protease activity was low, a preference for glycoproteins similar to MUC5B in terms of glycosylation and structure is suggested. MdpL preferentially hydrolyzed C-terminally located hydrophobic residues in peptides larger than 20 amino acids, which hinted at a limited sequence preference. To secure proper enzyme folding and optimal conditions for activity, L. fermentum incorporates a complex system that establishes a reducing environment. The importance of overall reducing conditions was confirmed by the activity boosting effect of the added reducing agents L-cysteine and DTT. High activity was retained in low to neutral pH 5.5-7.0, but the enzyme was completely inhibited in the presence of Zn2+. Here we have characterized a highly conserved mucin degrading protease from L. fermentum. MdpL, that together with the recently discovered O-glycanase and O-glycoprotease enzyme groups, increases our understanding of mucin degradation and complex biofilm dynamics.

Place, publisher, year, edition, pages
Frontiers Media S.A., 2023
Keywords
MUC5B, Limosilactobacillus fermentum, O-glycan, oral microbiota, mucin degradation, protease
National Category
Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:mau:diva-59286 (URN)10.3389/fmicb.2023.1127466 (DOI)000948293900001 ()36925480 (PubMedID)2-s2.0-85150177439 (Scopus ID)
Available from: 2023-04-19 Created: 2023-04-19 Last updated: 2024-02-27Bibliographically approved
Neilands, J., Svensäter, G., Boisen, G., Robertsson, C., Wickström, C. & Davies, J. R. (2023). Formation and Analysis of Mono-species and Polymicrobial Oral Biofilms in Flow-Cell Models. In: Bacterial Pathogenesis: Methods and Protocols, (pp. 33-52). Springer
Open this publication in new window or tab >>Formation and Analysis of Mono-species and Polymicrobial Oral Biofilms in Flow-Cell Models
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2023 (English)In: Bacterial Pathogenesis: Methods and Protocols,, Springer, 2023, p. 33-52Chapter in book (Refereed)
Abstract [en]

The oral microbiota, which is known to include at least 600 different bacterial species, is found on the teethand mucosal surfaces as multi-species communities or biofilms. The oral surfaces are covered with a pellicleof proteins absorbed from saliva, and biofilm formation is initiated when primary colonizers, which expresssurface adhesins that bind to specific salivary components, attach to the oral tissues. Further developmentthen proceeds through co-aggregation of additional species. Over time, the composition of oral biofilms,which varies between different sites throughout the oral cavity, is determined by a combination ofenvironmental factors such as the properties of the underlying surface, nutrient availability and oxygenlevels, and bacterial interactions within the community. A complex equilibrium between biofilm communities and the host is responsible for the maintenance of a healthy biofilm phenotype (eubiosis). In the faceof sustained environmental perturbation, however, biofilm homeostasis can break down giving rise todysbiosis, which is associated with the development of oral diseases such as caries and periodontitis.In vitro models have an important part to play in increasing our understanding of the complex processesinvolved in biofilm development in oral health and disease, and the requirements for experimental system,microbial complexity, and analysis techniques will necessarily vary depending on the question posed. In thischapter we describe some current and well-established methods used in our laboratory for studying oralbacteria in biofilm models which can be adapted to suit the needs of individual users. 

Place, publisher, year, edition, pages
Springer, 2023
Series
Methods in Molecular Biology, E-ISSN 1940-6029 ; 2674
National Category
Cell and Molecular Biology
Identifiers
urn:nbn:se:mau:diva-62874 (URN)10.1007/978-1-0716-3243-7_2 (DOI)37258958 (PubMedID)2-s2.0-85160680476 (Scopus ID)978-1-0716-3242-0 (ISBN)978-1-0716-3243-7 (ISBN)
Available from: 2023-09-29 Created: 2023-09-29 Last updated: 2023-10-06Bibliographically approved
Robertsson, C., Svensäter, G., Davies, J. R., Bay Nord, A., Malmodin, D. & Wickström, C. (2023). Synergistic metabolism of salivary MUC5B in oral commensal bacteria during early biofilm formation. Microbiology Spectrum, 11(6)
Open this publication in new window or tab >>Synergistic metabolism of salivary MUC5B in oral commensal bacteria during early biofilm formation
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2023 (English)In: Microbiology Spectrum, E-ISSN 2165-0497, Vol. 11, no 6Article in journal (Refereed) Published
Abstract [en]

Bacterial metabolism in oral biofilms is comprised of complex networks of nutritional chains and biochemical regulations. These processes involve both intraspecies and interspecies networks as well as interactions with components from host saliva, gingival crevicular fluid, and dietary intake. In a previous paper, a large salivary glycoprotein, mucin MUC5B, was suggested to promote a dental health-related phenotype in the oral type strain of Streptococcus gordonii DL1, by regulating bacterial adhesion and protein expression. In this study, nuclear magnetic resonance-based metabolomics was used to examine the effects on the metabolic output of monospecies compared to dual species early biofilms of two clinical strains of oral commensal bacteria, S. gordonii and Actinomyces naeslundii, in the presence of MUC5B. The presence of S. gordonii increased colonization of A. naeslundii on salivary MUC5B, and both commensals were able to utilize MUC5B as a sole nutrient source during early biofilm formation. The metabolomes suggested that the bacteria were able to release mucin carbohydrates from oligosaccharide side chains as well as amino acids from the protein core. Synergistic effects were also seen in the dual species biofilm metabolome compared to the monospecies, indicating that A. naeslundii and S. gordonii cooperated in the degradation of salivary MUC5B. A better understanding of bacterial interactions and salivary-mediated regulation of early dental biofilm activity is meaningful for understanding oral biofilm physiology and may contribute to the development of future prevention strategies for biofilm-induced oral disease.

IMPORTANCE: The study of bacterial interactions and salivary-mediated regulation of early dental biofilm activity is of interest for understanding oral microbial adaptation to environmental cues and biofilm maturation. Findings in oral commensals can prove useful from the perspectives of both oral and systemic health of the host, as well as the understanding of general microbial biofilm physiology. The knowledge may provide a basis for the development of prognostic biomarkers, or development of new treatment strategies, related to oral health and disease and possibly also to other biofilm-induced conditions. The study is also an important step toward developing the methodology for similar studies in other species and/or growth conditions.

Place, publisher, year, edition, pages
ASM International, 2023
Keywords
MUC5B, NMR, actinomyces, bacterial metabolism, biofilm physiology, dental biofilm, metabolomics, oral microbiology, saliva, streptococci
National Category
Dentistry
Identifiers
urn:nbn:se:mau:diva-63213 (URN)10.1128/spectrum.02704-23 (DOI)001085549500001 ()37855449 (PubMedID)2-s2.0-85180007534 (Scopus ID)
Available from: 2023-10-23 Created: 2023-10-23 Last updated: 2024-01-10Bibliographically approved
Gonzalez-Martinez, J. F., Boyd, H., Gutfreund, P., Welbourn, R. J., Robertsson, C., Wickström, C., . . . Sotres, J. (2022). MUC5B mucin films under mechanical confinement: A combined neutron reflectometry and atomic force microscopy study.. Journal of Colloid and Interface Science, 614, 120-129, Article ID S0021-9797(22)00109-6.
Open this publication in new window or tab >>MUC5B mucin films under mechanical confinement: A combined neutron reflectometry and atomic force microscopy study.
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2022 (English)In: Journal of Colloid and Interface Science, ISSN 0021-9797, E-ISSN 1095-7103, Vol. 614, p. 120-129, article id S0021-9797(22)00109-6Article in journal (Refereed) Published
Abstract [en]

HYPOTHESIS: Among other functions, mucins hydrate and protect biological interfaces from mechanical challenges. Mucins also attract interest as biocompatible coatings with excellent lubrication performance. Therefore, it is of high interest to understand the structural response of mucin films to mechanical challenges. We hypothesized that this could be done with Neutron Reflectometry using a novel sample environment where mechanical confinement is achieved by inflating a membrane against the films.

EXPERIMENTS: Oral MUC5B mucin films were investigated by Force Microscopy/Spectroscopy and Neutron Reflectometry both at solid-liquid interfaces and under mechanical confinement.

FINDINGS: NR indicated that MUC5B films were almost completely compressed and dehydrated when confined at 1 bar. This was supported by Force Microscopy/Spectroscopy investigations. Force Spectroscopy also indicated that MUC5B films could withstand mechanical confinement by means of steric interactions for pressures lower than ∼ 0.5 bar i.e., mucins could protect interfaces from mechanical challenges of this magnitude while keeping them hydrated. To investigate mucin films under these pressures by means of the employed sample environment for NR, further technological developments are needed. The most critical would be identifying or developing more flexible membranes that would still meet certain requirements like chemical homogeneity and very low roughness.

Place, publisher, year, edition, pages
Elsevier, 2022
Keywords
Atomic force microscopy, Force spectroscopy, Mechanical confinement, Mucins, Neutron reflectometry
National Category
Physical Chemistry
Identifiers
urn:nbn:se:mau:diva-50061 (URN)10.1016/j.jcis.2022.01.096 (DOI)000750672100013 ()35091141 (PubMedID)2-s2.0-85123366668 (Scopus ID)
Available from: 2022-02-09 Created: 2022-02-09 Last updated: 2024-02-05Bibliographically approved
Lima, B. P., Davies, J. R., Wickström, C., Johnstone, K. F., Hall, J. W., Svensäter, G. & Herzberg, M. C. (2022). Streptococcus gordonii Poised for Glycan Feeding through a MUC5B-Discriminating, Lipoteichoic Acid-Mediated Outside-In Signaling Circuit. Journal of Bacteriology, 204(6), Article ID e00118-22.
Open this publication in new window or tab >>Streptococcus gordonii Poised for Glycan Feeding through a MUC5B-Discriminating, Lipoteichoic Acid-Mediated Outside-In Signaling Circuit
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2022 (English)In: Journal of Bacteriology, ISSN 0021-9193, E-ISSN 1098-5530, Vol. 204, no 6, article id e00118-22Article in journal (Refereed) Published
Abstract [en]

Many oral bacteria employ cell wall-anchored adhesins to bind to the salivary films coating the teeth and mucosal surfaces. Surface binding prevents clearance and facilitates catabolism of salivary film glycoproteins. We asked whether Streptococcus gordonii adhesin expression changes in response to surface salivary cues using a eukaryote-like, outside-in recognition and signaling circuit. To determine whether the cues were discriminated, S. gordonii was tested during cell adhesion and biofilm formation on a MUC5B-rich or lower-molecular-mass salivary fraction or an uncoated abiotic surface. Cells were recovered and analyzed for differences in gene expression and proteins in cell wall fractions. In salivary-free conditions, planktonic S. gordonii presented three prominent cell wall LPXTG-motif proteins, SGO_1487, SGO_0890, and MbpA (mucin-binding protein A; SGO_0707). During biofilm formation on MUC5B-coated surfaces, MbpA, a MUC5B-binding protein, and key genes in the tagatose and quorum-sensing pathways were strongly promoted. The response to MUC5B required the two-component system (TCS), streptococcal regulator of adhesins sensor and regulator (SraSR, SGO_1180/81), lipoteichoic acid (LTA), and the homologous paired adhesins, SspA and SspB (SspAB). LTA appears to link the outside signal (MUC5B) to intramembrane SraSR. Tagatose pathway gene expression may poise cells to metabolize MUC5B glycans and, with a quorum-sensing gene (luxS), may direct formation of a consortium to facilitate glycan cross-feeding by S. gordonii. We now show that a Gram-positive bacterium discriminates specific surface environmental cues using an outside-in signaling mechanism to apparently optimize colonization of saliva-coated surfaces. IMPORTANCE All organisms throughout the tree of life sense and respond to their surface environments. To discriminate among mucosal surface environmental cues, we report that Streptococcus gordonii recognizes a high-molecular-weight mucin glycoprotein, MUC5B, using the paired adhesins SspAB and lipoteichoic acid; the latter bridges the outside signal to an intramembrane two-component system to transcriptionally regulate a MUC5B-specific adhesin and genes that may facilitate glycan catabolism. All organisms throughout the tree of life sense and respond to their surface environments. To discriminate among mucosal surface environmental cues, we report that Streptococcus gordonii recognizes a high-molecular-weight mucin glycoprotein, MUC5B, using the paired adhesins SspAB and lipoteichoic acid; the latter bridges the outside signal to an intramembrane two-component system to transcriptionally regulate a MUC5B-specific adhesin and genes that may facilitate glycan catabolism.

Place, publisher, year, edition, pages
ASM International, 2022
Keywords
Streptococcus gordonii, signaling circuit, glycan feeding, MUC5B, adhesins, lipoteichoic acid, two-component system
National Category
Dentistry
Identifiers
urn:nbn:se:mau:diva-53384 (URN)10.1128/jb.00118-22 (DOI)000809024700001 ()35652671 (PubMedID)2-s2.0-85132455432 (Scopus ID)
Available from: 2022-06-22 Created: 2022-06-22 Last updated: 2024-02-05Bibliographically approved
Boyd, H., Gonzalez-Martinez, J. F., Welbourn, R. J., Gutfreund, P., Klechikov, A., Robertsson, C., . . . Sotres, J. (2021). A comparison between the structures of reconstituted salivary pellicles and oral mucin (MUC5B) films.. Journal of Colloid and Interface Science, 584, 660-668, Article ID S0021-9797(20)31464-8.
Open this publication in new window or tab >>A comparison between the structures of reconstituted salivary pellicles and oral mucin (MUC5B) films.
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2021 (English)In: Journal of Colloid and Interface Science, ISSN 0021-9797, E-ISSN 1095-7103, Vol. 584, p. 660-668, article id S0021-9797(20)31464-8Article in journal (Refereed) Published
Abstract [en]

HYPOTHESIS: Salivary pellicles i.e., thin films formed upon selective adsorption of saliva, protect oral surfaces against chemical and mechanical insults. Pellicles are also excellent aqueous lubricants. It is generally accepted that reconstituted pellicles have a two-layer structure, where the outer layer is mainly composed of MUC5B mucins. We hypothesized that by comparing the effect of ionic strength on reconstituted pellicles and MUC5B films we could gain further insight into the pellicle structure.

EXPERIMENTS: Salivary pellicles and MUC5B films reconstituted on solid surfaces were investigated at different ionic strengths by Force Spectroscopy, Quartz Crystal Microbalance with Dissipation, Null Ellipsometry and Neutron Reflectometry.

FINDINGS: Our results support the two-layer structure for reconstituted salivary pellicles. The outer layer swelled when ionic strength decreased, indicating a weak polyelectrolyte behavior. While initially the MUC5B films exhibited a similar tendency, this was followed by a drastic collapse indicating an interaction between exposed hydrophobic domains. This suggests that mucins in the pellicle outer layer form complexes with other salivary components that prevent this interaction. Lowering ionic strength below physiological values also led to a partial removal of the pellicle inner layer. Overall, our results highlight the importance that the interactions of mucins with other pellicle components play on their structure.

Place, publisher, year, edition, pages
Elsevier, 2021
Keywords
Ionic strength, MUC5B, Mucin, Salivary pellicle, Steric forces
National Category
Dentistry
Identifiers
urn:nbn:se:mau:diva-37667 (URN)10.1016/j.jcis.2020.10.124 (DOI)000600220000006 ()33198975 (PubMedID)2-s2.0-85096107333 (Scopus ID)
Available from: 2020-12-21 Created: 2020-12-21 Last updated: 2023-10-30Bibliographically approved
Robertsson, C., Svensäter, G., Blum, Z., Jakobsson, M. E. & Wickström, C. (2021). Proteomic response in Streptococcus gordonii DL1 biofilm cells during attachment to salivary MUC5B. Journal of Oral Microbiology, 13(1), Article ID 1967636.
Open this publication in new window or tab >>Proteomic response in Streptococcus gordonii DL1 biofilm cells during attachment to salivary MUC5B
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2021 (English)In: Journal of Oral Microbiology, ISSN 2000-2297, E-ISSN 2000-2297, Vol. 13, no 1, article id 1967636Article in journal (Refereed) Published
Abstract [en]

Background Salivary mucin MUC5B seems to promote biodiversity in dental biofilms, and thereby oral health, for example, by inducing synergistic 'mucolytic' activities in a variety of microbial species that need to cooperate for the release of nutrients from the complex glycoprotein. Knowledge of how early colonizers interact with host salivary proteins is integral to better understand the maturation of putatively harmful oral biofilms and could provide key insights into biofilm physiology. Methods The early oral colonizer Streptococcus gordonii DL1 was grown planktonically and in biofilm flow cell systems with uncoated, MUC5B or low-density salivary protein (LDP) coated surfaces. Bacterial cell proteins were extracted and analyzed using a quantitative mass spectrometry-based workflow, and differentially expressed proteins were identified. Results and conclusions Overall, the proteomic profiles of S. gordonii DL1 were similar across conditions. Six novel biofilm cell proteins and three planktonic proteins absent in all biofilm cultures were identified. These differences may provide insights into mechanisms for adaptation to biofilm growth in this species. Salivary MUC5B also elicited specific responses in the biofilm cell proteome. These regulations may represent mechanisms by which this mucin could promote colonization of the commensal S. gordonii in oral biofilms.

Place, publisher, year, edition, pages
Taylor & Francis, 2021
Keywords
Salivary mucin, MUC5B, oral streptococci, Streptococcus gordonii, oral biofilm, saliva, mass spectrometry, protein expression, proteomics
National Category
Dentistry
Identifiers
urn:nbn:se:mau:diva-45857 (URN)10.1080/20002297.2021.1967636 (DOI)000687414300001 ()34447490 (PubMedID)2-s2.0-85120853173 (Scopus ID)
Available from: 2021-09-14 Created: 2021-09-14 Last updated: 2024-02-05Bibliographically approved
Robertsson, C., Svensäter, G., Blum, Z. & Wickström, C. (2020). Intracellular Ser/Thr/Tyr phosphoproteome of the oral commensal Streptococcus gordonii DL1. BMC Microbiology, 20(1), Article ID 280.
Open this publication in new window or tab >>Intracellular Ser/Thr/Tyr phosphoproteome of the oral commensal Streptococcus gordonii DL1
2020 (English)In: BMC Microbiology, E-ISSN 1471-2180, Vol. 20, no 1, article id 280Article in journal (Refereed) Published
Abstract [en]

BACKGROUND: To respond and adapt to environmental challenges, prokaryotes regulate cellular processes rapidly and reversibly through protein phosphorylation and dephosphorylation. This study investigates the intracellular proteome and Ser/Thr/Tyr phosphoproteome of the oral commensal Streptococcus gordonii. Intracellular proteins from planktonic cells of S. gordonii DL1 were extracted and subjected to 2D-gel electrophoresis. Proteins in general were visualized using Coomassie Brilliant Blue and T-Rex staining. Phosphorylated proteins were visualized with Pro-Q Diamond Phosphoprotein Gel Stain. Proteins were identified by LC-MS/MS and sequence analysis.

RESULTS: In total, sixty-one intracellular proteins were identified in S. gordonii DL1, many of which occurred at multiple isoelectric points. Nineteen of these proteins were present as one or more Ser/Thr/Tyr phosphorylated form. The identified phosphoproteins turned out to be involved in a variety of cellular processes.

CONCLUSION: Nineteen phosphoproteins involved in various cellular functions were identified in S. gordonii. This is the first time the global intracellular Ser/Thr/Tyr phosphorylation profile has been analysed in an oral streptococcus. Comparison with phosphoproteomes of other species from previous studies showed many similarities. Proteins that are consistently found in a phosphorylated state across several species and growth conditions may represent a core phosphoproteome profile shared by many bacteria.

Place, publisher, year, edition, pages
BioMed Central, 2020
Keywords
2DE, Oral bacteria, Phosphoproteome, Pro-Q diamond, Streptococci, Streptococcus gordonii
National Category
Dentistry
Identifiers
urn:nbn:se:mau:diva-18388 (URN)10.1186/s12866-020-01944-y (DOI)000573079700001 ()32928109 (PubMedID)2-s2.0-85091053882 (Scopus ID)
Available from: 2020-09-24 Created: 2020-09-24 Last updated: 2024-02-05Bibliographically approved
Sonesson, M., Svensäter, G. & Wickström, C. (2019). Glucosidase activity in dental biofilms in adolescent patients with fixed orthodontic appliances - a putative marker for white spot lesions - a clinical exploratory trial (ed.). Archives of Oral Biology, 102, 122-127
Open this publication in new window or tab >>Glucosidase activity in dental biofilms in adolescent patients with fixed orthodontic appliances - a putative marker for white spot lesions - a clinical exploratory trial
2019 (English)In: Archives of Oral Biology, ISSN 0003-9969, E-ISSN 1879-1506, Vol. 102, p. 122-127Article in journal (Refereed) Published
Abstract [en]

Objectives: Approximately 25% of the adolescents in the Scandinavian population are treated with a fixed orthodontic appliance (FOA). Adverse effects such as enamel decalcification (white spot lesions - WSL), seem to affect over 30% of patients. WSL have only a limited ability to improve, thus seriously jeopardising the treatment outcome. The aim of present study was to explore the biofilm phenotype by investigating plaque collected: 1) adjacent to brackets, and 2) in gingival margin of maxillary incisors in adolescents with FOA. Incidence of WSL after treatment was also assessed. Design: In eight adolescent patients treated with FOA, supra-gingival plaque formed on: 1) brackets, and 2) along the gingival margin of the maxillary incisors, was collected after 6-8 months of treatment. The patients were documented before and after treatment by intraoral photos. Plaque samples were tested for glycosidase(fluorogenic substrates) and protease (FITC-labelled casein substrate) activities. The plaque samples were visualised by Live/Dead BacLight stain, following which cells were investigated by confocal scanning laser microscopy. Results: In the collected plaque samples, all enzymes tested displayed small variations in activity between the individuals, except glucosidases, which varied significantly. Four patients developed WSL. The patients displayed higher glucosidase activity in plaque of brackets compared to patients without WSL. In seven patients, plaque at the gingival margin displayed higher protease activity than plaque of brackets. Conclusions: The current study shows two distinct environmentally induced biofilm phenotypes: 1) brackets with higher glucosidase activity, and 2) gingival margin with higher protease activity. Glucosidase activity might thus be used as a putative biomarker for risk of WSL.

Place, publisher, year, edition, pages
Elsevier, 2019
Keywords
Dental biofilm, Fixed appliance, Glucosidase, Marker, Orthodontics, White spot lesions
National Category
Dentistry
Identifiers
urn:nbn:se:mau:diva-6981 (URN)10.1016/j.archoralbio.2019.04.003 (DOI)000471206900016 ()31004977 (PubMedID)2-s2.0-85064329139 (Scopus ID)30143 (Local ID)30143 (Archive number)30143 (OAI)
Available from: 2020-02-28 Created: 2020-02-28 Last updated: 2024-03-18Bibliographically approved
Projects
Regulation of Surface Protein - Presentation on Streptococcus gordonii
Organisations
Identifiers
ORCID iD: ORCID iD iconorcid.org/0000-0002-8183-8846

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