Hörmann Sebastian, Scheyhing Carsten, Behr Jürgen, Pavlovic Melanie, Ehrmann Matthias, Vogel Rudi F
Lehrstuhl für Technische Mikrobiologie, Technische Universität München, Freising-Weihenstephan, Germany.
Proteomics. 2006 Mar;6(6):1878-85. doi: 10.1002/pmic.200402086.
High hydrostatic pressure (HHP) exerts diverse effects on microorganisms, leading to stress response and cell death. While inactivation of microorganisms by lethal HHP is well investigated in the context of food preservation and the hygienic safety of minimal food processes, sublethal HHP stress response and its effect on adaptation and cross-protection is less understood. In this study, the HHP stress response of Lactobacillus sanfranciscensis was characterized and compared with cold, heat, salt, acid and starvation stress at the proteome level by using 2-DE so as to provide insight into general versus specific stress responses. Sixteen proteins were found to be affected by HHP and were identified by using N-terminal amino acid sequencing and MS. Only one slightly increased protein was specific to the HHP response and showed homology to a clp protease. The other proteins were influenced by most of the investigated stresses in a similar way as HHP. The highest similarity in the HHP proteome was found to be with cold- and NaCl-stressed cells, with 11 overlapping proteins. At the proteome level, L. sanfranciscensis appears to use overlapping subsets of stress-inducible proteins rather than stereotype responses. Our data suggest that a specific pressure response does not exist in this bacteria.
高静水压（HHP）对微生物具有多种影响，可导致应激反应和细胞死亡。虽然在食品保鲜和最少加工食品的卫生安全背景下，致死性高静水压对微生物的灭活作用已得到充分研究，但亚致死性高静水压应激反应及其对适应性和交叉保护的影响却鲜为人知。在本研究中，通过二维电泳（2-DE）在蛋白质组水平上对旧金山乳杆菌的高静水压应激反应进行了表征，并与冷、热、盐、酸和饥饿应激进行了比较，以便深入了解一般应激反应与特异性应激反应。发现有16种蛋白质受高静水压影响，并通过N端氨基酸测序和质谱进行了鉴定。只有一种略有增加的蛋白质是高静水压反应所特有的，与一种Clp蛋白酶具有同源性。其他蛋白质受大多数所研究应激的影响方式与高静水压相似。在高静水压蛋白质组中，发现与冷应激和NaCl应激细胞的相似性最高，有11种重叠蛋白质。在蛋白质组水平上，旧金山乳杆菌似乎使用应激诱导蛋白的重叠子集，而不是刻板反应。我们的数据表明，这种细菌不存在特异性压力反应。
