Malinicova Lenka, Dubikova Katarina, Piknova Maria, Pristas Peter, Javorsky Peter
Institute of Animal Physiology, Slovak Academy of Sciences, Soltesovej 4-6, 04001 Kosice, Slovakia.
Protein Pept Lett. 2012 Sep;19(9):924-9. doi: 10.2174/092986612802084410.
C-terminal domain of peptidoglycan hydrolase enterolysin A (EnlA) is involved in specific recognition and binding to the target cell envelopes and represents true cell wall binding (CWB) domain. Sensitivity/resistance to EnlA is dependent on binding ability/disability of its CWB domain. We assume that main mechanism of resistance against EnlA is absence of the specific receptor on the cell surface, which is necessary for binding of the enzyme molecule. Using competitive and enzymatic assays we have uncovered the chemical nature of the EnlA receptor, which is a lipoteichoic acid.
肽聚糖水解酶肠球菌溶素A（EnlA）的C末端结构域参与对靶细胞包膜的特异性识别和结合，代表真正的细胞壁结合（CWB）结构域。对EnlA的敏感性/抗性取决于其CWB结构域的结合能力/无结合能力。我们假设对EnlA产生抗性的主要机制是细胞表面缺乏特异性受体，而该受体是酶分子结合所必需的。通过竞争性和酶活性测定，我们揭示了EnlA受体的化学性质，即脂磷壁酸。
