Recognization of receptors on bone marrow-derived dendritic cells bound with Pholiota nameko polysaccharides

被引：19

作者：

Li, Haiping ^{[1
]}

Tao, Yongqing ^{[1
]}

Zhao, Pei ^{[1
]}

Ban, Xiaopan ^{[1
]}

Zhi, Dexian ^{[1
]}

Li, Guoliang ^{[1
]}

Wang, Fenlin ^{[1
]}

Yang, Xiaoli ^{[1
]}

Huai, Lihua ^{[1
]}

机构：

[1] Tianjin Univ Commerce, Fac Biotechnol & Food Sci, Tianjin Key Lab Food Biotechnol, Tianjin 300134, Peoples R China

来源：

INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES | 2015年 / 72卷

基金：

中国国家自然科学基金;

关键词：

Pholiota Nameko; Polysaccharide; Dendritic cells; Receptors; Recogniazation; Immunomodulation; KINETICS;

D O I：

10.1016/j.ijbiomac.2014.08.013

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Three major active polysaccharides isolated from Pholiota nameko (PNPS), including PNPS-1, PNPS-2 and PNPS-3, had been proved to inhibit the maturation of the murine bone marrow-derived dendritic cells (BMDCs). This paper recognized the affinity bind between PNPS and the five receptors (TLR2, TLR4, CD14, Dectin-1 and Mannose receptor) on BMDCs, using the bio-layer interferometry (BLI)-based biosensor technology developed by ForteBio on Octet RED system (Fortebio, Inc.). From the primary binding experiment, the gradient binding experiment and the inhibition binding experiment between the receptor proteins and PNPS, combined with the binding experiment between PNPS and the BMDCs membranes, we found that PNPS-1, PNPS-2 and PNPS-3 presented strong affinity bind with both TLR2 and Dectin-1 on BMDCs, only PNPS-3 with Mannose receptor. These data confirmed that PNPS could interact with TLR2, Dectin-1 and Mannose receptor that were very important for the affinity bind of these receptors and PNPS, which triggered the further stimulation on BMDCs. (C) 2014 Elsevier B.V. All rights reserved.

引用

页码：649 / 657

页数：9

共 23 条

[1] Determining kinetics and affinities of protein interactions using a parallel real-time label-free biosensor, the Octet [J].