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      Streptococcal adhesin SspA/B analogue peptide inhibits adherence and impacts biofilm formation of Streptococcus mutans

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          Abstract

          Streptococcus mutans, the major causative agent of dental caries, adheres to tooth surfaces via the host salivary glycoprotein-340 (gp340). This adherence can be competitively inhibited by peptides derived from the SspA/B adhesins of Streptococcus gordonii, a human commensal microbe that competes for the same binding sites. Ssp(A4K-A11K), a double-lysine substituted SspA/B peptide analogue, has been shown to exhibit superior in vitro binding affinity for a gp340-derived peptide (SRCRP2), suggesting that Ssp(A4K-A11K) may be of clinical interest. In the present work, we tested the inhibitory effects of Ssp(A4K-A11K) on adherence and biofilm formation of S. mutans by reconstructing an artificial oral environment using saliva-coated polystyrene plates and hydroxyapatite disks. Bacterial adherence (adherence period: 1 h) was assessed by an enzyme-linked immunosorbent assay using biotinylated bacterial cells. Biofilm formation (periods: 8, 11, or 14 h) was assessed by staining and imaging of the sessile cells, or by recovering biofilm cells and plating for cell counts. The pH values of the culture media were measured as a biofilm acidogenicity indicator. Bactericidality was measured by loss of optical density during culturing in the presence of the peptide. We observed that 650 μM Ssp(A4K-A11K) significantly inhibited adherence of S. mutans to saliva-coated polystyrene; a similar effect was seen on bacterial affinity for SRCRP2. Ssp(A4K-A11K) had lesser effects on the adherence of commensal streptococci. Pretreatment of polystyrene and hydroxyapatite with 650 μM Ssp(A4K-A11K) significantly attenuated biofilm formation, whether tested with glucose- or sucrose-containing media. The SspA/B peptide’s activity did not reflect bactericidality. Strikingly, pH in Ssp-treated 8-h (6.8 ± 0.06) and 11-h (5.5 ± 0.06) biofilms showed higher values than the critical pH. Thus, Ssp(A4K-A11K) acts by inhibiting bacterial adherence and cariogrnic biofilm formation. We further consider these results in the context of the safety, specificity, and stability properties of the Ssp(A4K-A11K) peptide.

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          Most cited references33

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          Biology, immunology, and cariogenicity of Streptococcus mutans.

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            Histatins, a novel family of histidine-rich proteins in human parotid secretion. Isolation, characterization, primary structure, and fungistatic effects on Candida albicans.

            Histatins 1, 3, and 5 from human parotid secretion were isolated by gel filtration on Bio-Gel P-2 and reverse phase high performance liquid chromatography. The complete amino acid sequences of histatins determined by automated Edman degradation of the proteins, Staphylococcus aureus V8 protease, and tryptic peptides, are as follows: (Sequence: see text). Histatins 1, 3, and 5 contain 38, 32, and 24 amino acid residues, have molecular weights of 4929, 4063, and 3037, respectively, and contain 7 residues of histidine. Histatin 1 contains 1 mol of phosphate/mol of protein; histatins 3 and 5 lack phosphate. With the exception of Glu (residue 4) and Arg (residue 11) in histatin 1, the first 22 amino acid residues of all three histatins are identical, and the carboxyl-terminal 7 residues of histatins 1 and 3 are also identical. The sequence, -Glu-Phe-Pro-Phe-Tyr-Gly-Asp-Tyr-Gly- (residues 23-29), in histatin 1 is absent in histatin 3; and the sequence, -Gly-Tyr-Arg- (residues 23-25), in histatin 3 is absent in histatin 1. The complete sequence of histatin 5 is contained within the amino terminal 24 residues of histatin 3. The structural data suggest that histatins 1 and 3 are derived from different structural genes, whereas histatin 5 is a proteolytic product of histatin 3. All three histatins exhibit the ability to kill the pathogenic yeast, Candida albicans.
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              Why and how are peptide-lipid interactions utilized for self-defense? Magainins and tachyplesins as archetypes.

              Animals as well as plants defend themselves against invading pathogenic microorganisms utilizing cationic antimicrobial peptides, which rapidly kill various microbes without exerting toxicity against the host. Physicochemical peptide-lipid interactions provide attractive mechanisms for innate immunity. Many of these peptides form cationic amphipathic secondary structures, typically alpha-helices and beta-sheets, which can selectively interact with anionic bacterial membranes by the aid of electrostatic interactions. Rapid, peptide-induced membrane permeabilization is an effective mechanism of antimicrobial action. This review article summarizes interactions with lipid bilayers of magainins (alpha-helix) and tachyplesins (beta-sheet) discovered in frog skin and horseshoe crab hemolymph, respectively, as archetypes, emphasizing that the mode of interaction is strongly dependent on the physicochemical properties not only of the peptide, but also of the target membrane.
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                Author and article information

                Contributors
                Role: Editor
                Journal
                PLoS One
                PLoS ONE
                plos
                plosone
                PLoS ONE
                Public Library of Science (San Francisco, CA USA )
                1932-6203
                10 April 2017
                2017
                : 12
                : 4
                : e0175483
                Affiliations
                [1 ]Department of Pediatric Dentistry, Nihon University School of Dentistry at Matsudo, Chiba, Japan
                [2 ]Nihon University Research Institute of Oral Science, Chiba, Japan
                LSU Health Sciences Center School of Dentistry, UNITED STATES
                Author notes

                Competing Interests: The authors have declared that no competing interests exist.

                • Conceptualization: T. Ito TS.

                • Data curation: T. Ito T. Ichinosawa.

                • Formal analysis: T. Ito T. Ichinosawa TS.

                • Funding acquisition: T. Ito.

                • Methodology: T. Ito TS T. Ichinosawa.

                • Project administration: T. Ito TS.

                • Resources: T. Ito.

                • Validation: T. Ito TS.

                • Visualization: T. Ito T. Ichinosawa.

                • Writing – original draft: T. Ito T. Ichinosawa.

                • Writing – review & editing: T. Ito T. Ichinosawa TS.

                Article
                PONE-D-16-34953
                10.1371/journal.pone.0175483
                5386287
                28394940
                01642304-c80d-4234-8fd6-6bc7bfa2c5ca
                © 2017 Ito et al

                This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

                History
                : 31 August 2016
                : 27 March 2017
                Page count
                Figures: 6, Tables: 1, Pages: 15
                Funding
                Funded by: The Ministry of Education, Culture, Sports, Science and Technology, Japan
                Award ID: Grant-in-Aid for Young Scientists (B) 15K20610
                Award Recipient :
                This work was supported by a Grant-in-Aid for Young Scientists (B) 15K20610 from the Ministry of Education, Culture, Sports, Science and Technology of Japan ( http://www.mext.go.jp). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.
                Categories
                Research Article
                Biology and Life Sciences
                Organisms
                Bacteria
                Streptococcus
                Streptococcus Mutans
                Biology and Life Sciences
                Microbiology
                Medical Microbiology
                Microbial Pathogens
                Bacterial Pathogens
                Streptococcus
                Streptococcus Mutans
                Medicine and Health Sciences
                Pathology and Laboratory Medicine
                Pathogens
                Microbial Pathogens
                Bacterial Pathogens
                Streptococcus
                Streptococcus Mutans
                Biology and Life Sciences
                Microbiology
                Biofilms
                Biology and Life Sciences
                Microbiology
                Bacteriology
                Bacterial Biofilms
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                Microbiology
                Biofilms
                Bacterial Biofilms
                Research and Analysis Methods
                Biological Cultures
                Cell Culturing Techniques
                Biofilm Culture
                Biology and Life Sciences
                Anatomy
                Body Fluids
                Saliva
                Medicine and Health Sciences
                Anatomy
                Body Fluids
                Saliva
                Biology and Life Sciences
                Physiology
                Body Fluids
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                Medicine and Health Sciences
                Physiology
                Body Fluids
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                Physical Sciences
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                Polymer Chemistry
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                Polystyrene
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                Biology and Life Sciences
                Microbiology
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                Medicine and Health Sciences
                Pathology and Laboratory Medicine
                Pathogens
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                Physical Sciences
                Chemistry
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                Basic Amino Acids
                Lysine
                Biology and Life Sciences
                Biochemistry
                Proteins
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                Basic Amino Acids
                Lysine
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