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Effect of human secretory calcium-binding phosphoprotein proline-glutamine rich 1 protein on Porphyromonas gingivalis and identification of its active portions.
- Source :
-
Scientific reports [Sci Rep] 2021 Dec 09; Vol. 11 (1), pp. 23724. Date of Electronic Publication: 2021 Dec 09. - Publication Year :
- 2021
-
Abstract
- The mouth environment comprises the second most significant microbiome in the body, and its equilibrium is critical in oral health. Secretory calcium-binding phosphoprotein proline-glutamine rich 1 (SCPPPQ1), a protein normally produced by the gingival epithelium to mediate its attachment to teeth, was suggested to be bactericidal. Our aim was to further explore the antibacterial potential of human SCPPPQ1 by characterizing its mode of action and identifying its active portions. In silico analysis showed that it has molecular parallels with antimicrobial peptides. Incubation of Porphyromonas gingivalis, a major periodontopathogen, with the full-length protein resulted in decrease in bacterial number, formation of aggregates and membrane disruptions. Analysis of SCPPPQ1-derived peptides indicated that these effects are sustained by specific regions of the molecule. Altogether, these data suggest that human SCPPPQ1 exhibits antibacterial capacity and provide new insight into its mechanism of action.<br /> (© 2021. The Author(s).)
- Subjects :
- Amino Acid Sequence
Antimicrobial Peptides biosynthesis
Antimicrobial Peptides chemistry
Antimicrobial Peptides pharmacology
Calcium-Binding Proteins metabolism
Disease Resistance
Host-Pathogen Interactions
Humans
Microbial Sensitivity Tests
Models, Molecular
Phosphoproteins metabolism
Protein Binding
Protein Conformation
Structure-Activity Relationship
Calcium-Binding Proteins chemistry
Calcium-Binding Proteins pharmacology
Phosphoproteins chemistry
Phosphoproteins pharmacology
Porphyromonas gingivalis drug effects
Subjects
Details
- Language :
- English
- ISSN :
- 2045-2322
- Volume :
- 11
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Scientific reports
- Publication Type :
- Academic Journal
- Accession number :
- 34887426
- Full Text :
- https://doi.org/10.1038/s41598-021-02661-w