Functional Amyloids Keep Quorum-sensing Molecules in Check*
Functional Amyloids Keep Quorum-sensing Molecules in Check*
复制标题
功能性淀粉样蛋白控制群体感应分子*
DOI：
10.1074/jbc.m114.613810
复制
发表时间：
2015
期刊：
影响因子：
--
通讯作者：
M. Dueholm
中科院分区：
文献类型：
--
作者：
T. Seviour;S. H. Hansen;Liang Yang;Y. Yau;V. B. Wang;Marcel R Stenvang;G. Christiansen;E. Marsili;M. Givskov;Yicai Chen;D. Otzen;P. Nielsen;S. Geifman;S. Kjelleberg;M. Dueholm
背景：在生物膜中，细菌通过群体感应（QS）分子进行交流。结果：测定了QS分子与功能性淀粉样蛋白的特异性结合亲和力。结论：功能性淀粉样蛋白可短暂结合并滞留QS分子。意义：功能性淀粉样蛋白对生物膜内的细胞信号传导很重要。细胞外代谢物，包括氧化还原介体和群体感应信号分子，通过生物膜的细胞外基质的交通的机制很少探索。我们假设，功能性淀粉样蛋白，丰富的天然生物膜和具有疏水结构域，保留这些代谢产物。使用表面等离子体共振，我们证明，群体感应（QS）分子，2-庚基-3-羟基-4（1H）-喹诺酮和N-（3-oxodododecanoyl）-l-高丝氨酸内酯，和氧化还原介体绿脓菌素结合与瞬时亲和力功能性淀粉样蛋白从假单胞菌（Fap）。它们的高疏水性使它们易于发生信号-淀粉样蛋白相互作用，但特异性相互作用也起作用。瞬时相互作用允许快速缔合和解离动力学，这使得QS分子具有生物可利用性，同时由于连续结合而固定在细胞外基质内。使用基于铜绿假单胞菌PAO 1的2-庚基-3-羟基-4（1H）-喹诺酮和N-（3-氧代十二烷酰基）-1-高丝氨酸内酯报告基因测定证实了QS分子的保留，表明用QS分子预处理的Fap原纤维即使在连续洗涤后也能活化报告基因。绿脓菌素保留通过对经受相同洗涤过程的绿脓菌素预处理的Fap原纤维的电化学分析来验证。结果表明，QS分子-淀粉样蛋白的相互作用可能是重要的，在动荡的环境中经常遇到的自然栖息地。
Background: In biofilms, bacteria communicate via quorum-sensing (QS) molecules. Results: The specific binding affinity of QS molecules to a functional amyloid is determined. Conclusion: Functional amyloids can transiently bind and retain QS molecules. Significance: Functional amyloids are important for cell signaling within biofilms. The mechanism by which extracellular metabolites, including redox mediators and quorum-sensing signaling molecules, traffic through the extracellular matrix of biofilms is poorly explored. We hypothesize that functional amyloids, abundant in natural biofilms and possessing hydrophobic domains, retain these metabolites. Using surface plasmon resonance, we demonstrate that the quorum-sensing (QS) molecules, 2-heptyl-3-hydroxy-4(1H)-quinolone and N-(3-oxododecanoyl)-l-homoserine lactone, and the redox mediator pyocyanin bind with transient affinity to functional amyloids from Pseudomonas (Fap). Their high hydrophobicity predisposes them to signal-amyloid interactions, but specific interactions also play a role. Transient interactions allow for rapid association and dissociation kinetics, which make the QS molecules bioavailable and at the same time secure within the extracellular matrix as a consequence of serial bindings. Retention of the QS molecules was confirmed using Pseudomonas aeruginosa PAO1-based 2-heptyl-3-hydroxy-4(1H)-quinolone and N-(3-oxododecanoyl)-l-homoserine lactone reporter assays, showing that Fap fibrils pretreated with the QS molecules activate the reporters even after sequential washes. Pyocyanin retention was validated by electrochemical analysis of pyocyanin-pretreated Fap fibrils subjected to the same washing process. Results suggest that QS molecule-amyloid interactions are probably important in the turbulent environments commonly encountered in natural habitats.
登录
查看更多内容
影响因子：
2.9
作者：
Dueholm, Morten S.;Nielsen, Soren B.;Hein, Kim L.;Nissen, Poul;Chapman, Matthew;Christiansen, Gunna;Nielsen, Per Halkjaer;Otzen, Daniel E.
通讯作者：
Otzen, Daniel E.
影响因子：
15.9
作者：
BRITIGAN, BE;ROEDER, TL;COX, CD
通讯作者：
COX, CD
影响因子：
2.8
作者：
Mathee, K;Ciofu, O;Kharazmi, A
通讯作者：
Kharazmi, A
影响因子：
15.9
作者：
Blanco, Luz P.;Evans, Margery L.;Smith, Daniel R.;Badtke, Matthew P.;Chapman, Matthew R.
通讯作者：
Chapman, Matthew R.
DOI：
10.1073/pnas.96.20.11229
发表时间：
1999-09-28
影响因子：
11.1
作者：
Pesci, EC;Milbank, JBJ;Iglewski, BH
通讯作者：
Iglewski, BH