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Calcium-mediated Protein Folding and Stabilization of Salmonella Biofilm-associated Protein A

机译:钙介导的蛋白质折叠和沙门氏菌生物膜相关蛋白A的稳定化

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Biofilm-associated proteins (BAPs) are important for early biofilm formation (adhesion) by bacteria and are also found in mature biofilms. BapA from Salmonella is a similar to 386-kDa surface protein, comprising 27 tandem repeats predicted to be bacterial lg-like (Big) domains. Such tandem repeats are conserved for BAPs across different bacterial species, but the function of these domains is not completely understood. In this work, we report the first study of the mechanical stability of the BapA protein. Using magnetic tweezers, we show that the folding of BapA Blg domains requires calcium binding and the folded domains have differential mechanical stabilities. Importantly, we identify that 100 nM concentration of calcium is needed for folding of the Blg domains, and the stability of the folded Blg domains is regulated by calcium over a wide concentration range from sub-micromolar (mu M) to millimolar (mM). Only at mM calcium concentrations, as found in the extracellular environment, do the Blg domains have the saturated mechanical stability. BapA has been suggested to be involved in Salmonella invasion, and it is likely a crucial mechanical component of biofilms. Therefore, our results provide new insights into the potential roles of BapA as a structural maintenance component of Salmonella biofilm and also Salmonella invasion. (C) 2018 Elsevier Ltd. All rights reserved.
机译:生物膜相关的蛋白质(BAPS)对于细菌的早期生物膜形成(粘附)是重要的,并且也存在于成熟生物膜中。来自沙门氏菌的Bapa是类似于386 kda表面蛋白质,包含27个串联重复预测是细菌Lg样(大)结构域。这种串联重复在不同的细菌物种上被保守,但是这些域的​​功能并不完全理解。在这项工作中,我们报告了对BAPA蛋白的机械稳定性的第一次研究。使用磁性镊子,我们表明BAPA BLG结构域的折叠需要钙结合,并且折叠的域具有差动的机械稳定性。重要的是,我们鉴定该&折叠BLG结构域需要100nm浓度的钙,并且折叠的BLG结构域的稳定性通过钙从亚微粒(mum)到毫米摩尔(MM)的谱浓度范围内调节钙。 )。只有MM钙浓度,如细胞外环境中发现,BLG结构域的饱和机械稳定性是饱和的机械稳定性。 BAPA已建议参与沙门氏菌侵袭,并且可能是生物膜的重要机械成分。因此,我们的结果为BAPA作为沙门氏菌的结构维持成分和沙门氏菌侵袭的潜在作用提供了新的见解。 (c)2018年elestvier有限公司保留所有权利。

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