A temperature downshift results in stabilized secondary structure formation in mRNA that halts translation to which Escherichia coli responds by synthesizing a set of proteins termed as cold shock proteins (Csps). To cope with the sudden temperature drop, gene expression patterns are reprogrammed to induce Csps at the cost of other proteins. Out of the nine homologous proteins in the CspA family, CspA, CspB, CspG, and CspI have major roles in protecting the cell under a cold shock. Additionally, a subset of Csps has conferred the organism an ability to adapt to various stresses along the lines of nutrient deprivation, oxidative, heat, acid, and antibiotic stresses. Stressors like C group translational inhibitors stall the translational apparatus and produce a response similar to that observed under a temperature downshift. Conditions set by the antibiotic therefore elicit a cold shock response and induce the major Csps, thereby pointing out to a common mechanism existing between the two. In the current review, we briefly describe the induction of E. coli Csps under an antibiotic stress acquired from data published previously and help establish the role of Csps in protecting the cell against the inducing agents and as a participant in the organisms’ complex stress response network.

温度下降导致 mRNA 中稳定的二级结构形成，从而阻止大肠杆菌转化为通过合成一组称为冷休克蛋白 (Csps) 的蛋白质来做出反应。为了应对突然的温度下降，基因表达模式被重新编程，以其他蛋白质为代价来诱导 Csps。在 CspA 家族的九种同源蛋白中，CspA、CspB、CspG 和 CspI 在冷休克下保护细胞方面发挥着重要作用。此外，Csps 的一个子集赋予生物体适应营养缺乏、氧化、热、酸和抗生素胁迫等各种胁迫的能力。像 C 组翻译抑制剂这样的压力源会使翻译装置停滞，并产生类似于在温度降档下观察到的反应。因此，抗生素设定的条件会引起冷休克反应并诱发主要的 Csps，从而指出了两者之间存在的共同机制。在当前的综述中，我们简要描述了诱导E.coli Csps 在抗生素应激下从先前发表的数据中获得，并有助于确定 Csps 在保护细胞免受诱导剂侵害方面的作用，以及作为生物体复杂应激反应网络的参与者。