TY - JOUR
T1 - Effects of Lectins on initial attachment of cariogenic Streptococcus mutans
AU - Ito, Takashi
AU - Yoshida, Yasuhiro
AU - Shiota, Yasuyoshi
AU - Ito, Yuki
AU - Yamamoto, Tadashi
AU - Takashiba, Shogo
N1 - Funding Information:
We would like to thank Drs. Sukeaki Omura and Koji Imamura, MBL/GLYENCE, for kindly providing lectins (rACG, rGRFT, and rOAA) and for their critical advices. This work was supported by New Energy and Industrial Technology Development Organization (NEDO; Subsidy for development of technology applications). All authors have no conflict of interest regarding this paper.
Funding Information:
Acknowledgments We would like to thank Drs. Sukeaki Omura and Koji Imamura, MBL/GLYENCE, for kindly providing lectins (rACG, rGRFT, and rOAA) and for their critical advices. This work was supported by New Energy and Industrial Technology Development Organization (NEDO; Subsidy for development of technology applications).
Publisher Copyright:
© 2017, Springer Science+Business Media, LLC.
PY - 2018/2/1
Y1 - 2018/2/1
N2 - Oral bacteria initiate biofilm formation by attaching to tooth surfaces via an interaction of a lectin-like bacterial protein with carbohydrate chains on the pellicle. This study aimed to find naturally derived lectins that inhibit the initial attachment of a cariogenic bacterial species, Streptococcus mutans (S. mutans), to carbohydrate chains in saliva in vitro. Seventy kinds of lectins were screened for candidate motifs that inhibit the attachment of S. mutans ATCC 25175 to a saliva-coated culture plate. The inhibitory effect of the lectins on attachment of the S. mutans to the plates was quantified by crystal violet staining, and the biofilm was observed under a scanning electron microscope (SEM). Surface plasmon resonance (SPR) analysis was performed to examine the binding of S. mutans to carbohydrate chains and the binding of candidate lectins to carbohydrate chains, respectively. Moreover, binding assay between the biotinylated-lectins and the saliva components was conducted to measure the lectin binding. Lectins recognizing a salivary carbohydrate chain, Galβ1-3GalNAc, inhibited the binding of S. mutans to the plate. In particular, Agaricus bisporus agglutinin (ABA) markedly inhibited the binding. This inhibition was confirmed by SEM observation. SPR analysis indicated that S. mutans strongly binds to Galβ1-3GalNAc, and ABA binds to Galβ1-3GalNAc. Finally, the biotinylated Galβ1-3GalNAc-binding lectins including ABA demonstrated marked binding to the saliva components. These results suggest that ABA lectin inhibited the attachment of S. mutans to Galβ1-3GalNAc in saliva and ABA can be useful as a potent inhibitor for initial attachment of oral bacteria and biofilm formation.
AB - Oral bacteria initiate biofilm formation by attaching to tooth surfaces via an interaction of a lectin-like bacterial protein with carbohydrate chains on the pellicle. This study aimed to find naturally derived lectins that inhibit the initial attachment of a cariogenic bacterial species, Streptococcus mutans (S. mutans), to carbohydrate chains in saliva in vitro. Seventy kinds of lectins were screened for candidate motifs that inhibit the attachment of S. mutans ATCC 25175 to a saliva-coated culture plate. The inhibitory effect of the lectins on attachment of the S. mutans to the plates was quantified by crystal violet staining, and the biofilm was observed under a scanning electron microscope (SEM). Surface plasmon resonance (SPR) analysis was performed to examine the binding of S. mutans to carbohydrate chains and the binding of candidate lectins to carbohydrate chains, respectively. Moreover, binding assay between the biotinylated-lectins and the saliva components was conducted to measure the lectin binding. Lectins recognizing a salivary carbohydrate chain, Galβ1-3GalNAc, inhibited the binding of S. mutans to the plate. In particular, Agaricus bisporus agglutinin (ABA) markedly inhibited the binding. This inhibition was confirmed by SEM observation. SPR analysis indicated that S. mutans strongly binds to Galβ1-3GalNAc, and ABA binds to Galβ1-3GalNAc. Finally, the biotinylated Galβ1-3GalNAc-binding lectins including ABA demonstrated marked binding to the saliva components. These results suggest that ABA lectin inhibited the attachment of S. mutans to Galβ1-3GalNAc in saliva and ABA can be useful as a potent inhibitor for initial attachment of oral bacteria and biofilm formation.
KW - Biofilm
KW - Carbohydrate chains
KW - Inhibitor
KW - Initial attachment
KW - Lectin
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U2 - 10.1007/s10719-017-9795-2
DO - 10.1007/s10719-017-9795-2
M3 - Article
C2 - 28887741
AN - SCOPUS:85028983121
SN - 0282-0080
VL - 35
SP - 41
EP - 51
JO - Glycoconjugate Journal
JF - Glycoconjugate Journal
IS - 1
ER -