TY - JOUR
T1 - Horseradish peroxidase interacts with the cell wall peptidoglycans on oral bacteria
AU - Mizuno, Hirofumi
AU - Takayama, Eiji
AU - Satoh, Ayano
AU - Into, Takeshi
AU - Adachi, Masanori
AU - Ekuni, Daisuke
AU - Yashiro, Koji
AU - Mizuno-Kamiya, Masako
AU - Nagayama, Motohiko
AU - Saku, Seitaro
AU - Tomofuji, Takaaki
AU - Doi, Yutaka
AU - Murakami, Yukitaka
AU - Kondoh, Nobuo
AU - Morita, Manabu
N1 - Publisher Copyright:
© 2020 Spandidos Publications. All rights reserved.
PY - 2020/9
Y1 - 2020/9
N2 - Salivary peroxidase and myeloperoxidase are known to display antibacterial activity against oral microbes, and previous indications have pointed to the possibility that horseradish peroxidase (HRP) adsorbs onto the membrane of the major oral streptococci, Streptococcus mutans and Streptococcus sanguinis (S. sanguinis). However, the mechanism of interaction between HRP and the bacterial cell wall componentisunclear.Dentalplaquescontainingsalivaryglycoproteins and extracellular microbial products are visualized with ‘dental plaque disclosing agent’, and are controlled within dental therapy. However, current ‘dental plaque disclosing agents’ are difficult to evaluate with just dental plaques, since they stain and disclose not only dental plaques but also pellicle formed with salivary glycoproteins on a tooth surface. In this present study, we have demonstrated that HRP interacted with the cell wall component of the major gram-positive bacterial peptidoglycan, but not the major cell wall component of gram-negative bacteria lipopolysaccharide. Furthermore, we observed that the adsorbed HRP labeled with fluorescence was detected on the major oral gram-positive strains S. sanguinis and Streptococcus salivarius (S. salivarius), but not on a gram-negative strain, Escherichia coli (E. coli). Furthermore, we have demonstrated that the combination of HRP and chromogenic substrate clearly disclosed the dental plaques and the biofilm developed by S. sanguinis, S. salivarius and the major gram-postive bacteria Lactobacillus casei on tooth surfaces, and slightly disclosed the biofilm by E. coli. The combination of HRP and chromogenic substrate did not stain either the dental pellicle with the salivary glycoprotein mucin, or naked tooth surfaces. These results have suggested the possibility that the adsorption activity of HRP not only contributes to the evaluation of dental plaque, but that enzymatic activity of HRP may also contribute to improve dental hygiene.
AB - Salivary peroxidase and myeloperoxidase are known to display antibacterial activity against oral microbes, and previous indications have pointed to the possibility that horseradish peroxidase (HRP) adsorbs onto the membrane of the major oral streptococci, Streptococcus mutans and Streptococcus sanguinis (S. sanguinis). However, the mechanism of interaction between HRP and the bacterial cell wall componentisunclear.Dentalplaquescontainingsalivaryglycoproteins and extracellular microbial products are visualized with ‘dental plaque disclosing agent’, and are controlled within dental therapy. However, current ‘dental plaque disclosing agents’ are difficult to evaluate with just dental plaques, since they stain and disclose not only dental plaques but also pellicle formed with salivary glycoproteins on a tooth surface. In this present study, we have demonstrated that HRP interacted with the cell wall component of the major gram-positive bacterial peptidoglycan, but not the major cell wall component of gram-negative bacteria lipopolysaccharide. Furthermore, we observed that the adsorbed HRP labeled with fluorescence was detected on the major oral gram-positive strains S. sanguinis and Streptococcus salivarius (S. salivarius), but not on a gram-negative strain, Escherichia coli (E. coli). Furthermore, we have demonstrated that the combination of HRP and chromogenic substrate clearly disclosed the dental plaques and the biofilm developed by S. sanguinis, S. salivarius and the major gram-postive bacteria Lactobacillus casei on tooth surfaces, and slightly disclosed the biofilm by E. coli. The combination of HRP and chromogenic substrate did not stain either the dental pellicle with the salivary glycoprotein mucin, or naked tooth surfaces. These results have suggested the possibility that the adsorption activity of HRP not only contributes to the evaluation of dental plaque, but that enzymatic activity of HRP may also contribute to improve dental hygiene.
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U2 - 10.3892/etm.2020.9016
DO - 10.3892/etm.2020.9016
M3 - Article
AN - SCOPUS:85103992921
SN - 1792-0981
VL - 20
SP - 2822
EP - 2827
JO - Experimental and Therapeutic Medicine
JF - Experimental and Therapeutic Medicine
IS - 3
ER -