TY - JOUR
T1 - Development of novel monoclonal antibodies directed against catechins for investigation of antibacterial mechanism of catechins
AU - Miyamoto, Takahisa
AU - Zhang, Xiaoguang
AU - Ueyama, Yuuki
AU - Apisada, Kitichalermkiat
AU - Nakayama, Motokazu
AU - Suzuki, Yasuto
AU - Ozawa, Tadahiro
AU - Mitani, Asako
AU - Shigemune, Naofumi
AU - Shimatani, Kanami
AU - Yui, Koji
AU - Honjoh, Ken-ichi
N1 - Publisher Copyright:
© 2017 Elsevier B.V.
PY - 2017/6/1
Y1 - 2017/6/1
N2 - Catechins are major polyphenolic compounds of green tea. To investigate mechanism for antibacterial action of catechins, 11 monoclonal antibodies (MAbs) were raised against a 3-succinyl-epicatechin (EC)-keyhole limpet hemocyanin (KLH) conjugate. Amino acid sequences of variable regions determined for MAbs b-1058, b-1565, and b-2106 confirmed their innovative character. MAb b-1058 strongly interacted with its target substances in the following order of magnitude: theaflavin-3,3′-di-O-gallate (TFDG) > theaflavin-3-O-gallate (TF3G) ≥ theaflavin-3′-O-gallate (TF3’G) > gallocatechin gallate (GCg) > penta-O-galloyl-β-D-glucose (PGG) > epigallocatechin gallate (EGCg), as determined using surface plasmon resonance (SPR) on MAb-immobilized sensor chips. The affinity profiles of MAbs b-1058 and b-2106 to the various polyphenols tested suggested that flavan skeletons with both carbonyl oxygen and hydroxyl groups are important for this interaction to take place. S. aureus cells treated with EGCg showed green fluorescence around the cells after incubation with FITC-labeled MAb b-1058. The fluorescence intensity increased with increasing concentrations of EGCg. These MAbs are effective to investigate antibacterial mechanism of catechins and theaflavins.
AB - Catechins are major polyphenolic compounds of green tea. To investigate mechanism for antibacterial action of catechins, 11 monoclonal antibodies (MAbs) were raised against a 3-succinyl-epicatechin (EC)-keyhole limpet hemocyanin (KLH) conjugate. Amino acid sequences of variable regions determined for MAbs b-1058, b-1565, and b-2106 confirmed their innovative character. MAb b-1058 strongly interacted with its target substances in the following order of magnitude: theaflavin-3,3′-di-O-gallate (TFDG) > theaflavin-3-O-gallate (TF3G) ≥ theaflavin-3′-O-gallate (TF3’G) > gallocatechin gallate (GCg) > penta-O-galloyl-β-D-glucose (PGG) > epigallocatechin gallate (EGCg), as determined using surface plasmon resonance (SPR) on MAb-immobilized sensor chips. The affinity profiles of MAbs b-1058 and b-2106 to the various polyphenols tested suggested that flavan skeletons with both carbonyl oxygen and hydroxyl groups are important for this interaction to take place. S. aureus cells treated with EGCg showed green fluorescence around the cells after incubation with FITC-labeled MAb b-1058. The fluorescence intensity increased with increasing concentrations of EGCg. These MAbs are effective to investigate antibacterial mechanism of catechins and theaflavins.
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U2 - 10.1016/j.mimet.2017.03.014
DO - 10.1016/j.mimet.2017.03.014
M3 - Article
C2 - 28347725
AN - SCOPUS:85016332556
SN - 0167-7012
VL - 137
SP - 6
EP - 13
JO - Journal of Microbiological Methods
JF - Journal of Microbiological Methods
ER -