The Interaction of a Histidine-Rich Protein Hpn with the Membrane Mimics: Implications for Pathologic Roles of Hpn in Helicobacter pylori
The Interaction of a Histidine-Rich Protein Hpn with the Membrane Mimics: Implications for Pathologic Roles of Hpn in Helicobacter pylori
复制标题
富含组氨酸的蛋白 Hpn 与膜模拟物的相互作用:对 Hpn 在幽门螺杆菌中病理作用的影响
DOI:
10.1111/hel.12109
复制
发表时间:
2014
期刊:
影响因子:
4.4
通讯作者:
Ge Ruiguang
中科院分区:
文献类型:
--
作者:
Zhou Qinglu;Qi Shuang;Sun Xuesong;Ge Ruiguang
BackgroundHpn is a small histidine‐rich protein in Helicobacter pylori. This protein has been shown to play roles in nickel storage and detoxification and to exhibit cytotoxicity to gastric epithelial cells. Hpn can be secreted outside of the bacterium and forms amyloid‐like structures.ObjectiveTo study the interactions between Hpn and membrane mimics, which may further our understanding of the pathologic roles of this bacterium.MethodsVarious biochemical and biophysical methods, such as secondary structure determination be CD, calcein release assay with fluorescence spectrometry, and Laurdan and Prodan generalized polarization determination have been used to characterize the interaction between Hpn and membrane mimics.ResultsMembrane mimics induced the formation of α‐helix in Hpn. The interaction disrupts the integrity of the membrane mimics and leads to the release of inner calcein probe. The experiments involving the Laurdan and Prodan fluorescence indicated that increasing the total protein/lipid ratio leads to a less ordered and more hydrated lipid membrane structure close to the water/lipid interface of lipid bilayers modeling the mitochondrial inner membrane.ConclusionThe present data indicated that Hpn may take part in the pathological roles of Helicobacter pylori through membrane interactions.