原子力显微镜测量揭示了幽门螺杆菌血型抗原结合黏附素与Lewis b配体之间的多个键。
Atomic force microscopy measurements reveal multiple bonds between Helicobacter pylori blood group antigen binding adhesin and Lewis b ligand.
作者信息
Parreira P, Shi Q, Magalhaes A, Reis C A, Bugaytsova J, Borén T, Leckband D, Martins M C L
机构信息
INEB-Instituto de Engenharia Biomédica, Universidade do Porto, Porto, Portugal.
Department of Chemical and Biomolecular Engineering, University of Illinois at Urbana-Champaign, Urbana, IL, USA.
出版信息
J R Soc Interface. 2014 Dec 6;11(101):20141040. doi: 10.1098/rsif.2014.1040.
Abstract
The strength of binding between the Helicobacter pylori blood group antigen-binding adhesin (BabA) and its cognate glycan receptor, the Lewis b blood group antigen (Le(b)), was measured by means of atomic force microscopy. High-resolution measurements of rupture forces between single receptor-ligand pairs were performed between the purified BabA and immobilized Le(b) structures on self-assembled monolayers. Dynamic force spectroscopy revealed two similar but statistically different bond populations. These findings suggest that the BabA may form different adhesive attachments to the gastric mucosa in ways that enhance the efficiency and stability of bacterial adhesion.
摘要
通过原子力显微镜测定了幽门螺杆菌血型抗原结合黏附素（BabA）与其同源聚糖受体——Lewis b血型抗原（Le(b)）之间的结合强度。在自组装单分子层上，对纯化的BabA与固定化的Le(b)结构之间的单个受体-配体对之间的断裂力进行了高分辨率测量。动态力谱揭示了两个相似但在统计学上不同的键群。这些发现表明，BabA可能以提高细菌黏附效率和稳定性的方式，与胃黏膜形成不同的黏附连接。
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