鮑氏不動桿菌(Acinetobacter baumannii)和醫院加護病房感染有關，如呼吸相關的肺炎和腦膜炎。Sulbactam是一種乙內酰胺酶抑制劑(β-lactamase inhibitor)，通常與乙內酰胺類抗生素(β-lactam antibiotic)合併使用來治療感染患者。研究發現單獨使用Sulbactam可用於治療鮑氏不動桿菌引起的感染，儘管殺菌作用機制仍然未知。在這項研究中，蛋白質體學被用來分析蛋白質表現量的變化，並分析出Sulbactam作用後鮑氏不動桿菌的蛋白質變化。總共有54個蛋白質被發現在表現量上有明顯的變化。表現量降低的蛋白質包括ATP結合轉運蛋白(ATP-binding cassette (ABC) transporters proteins)以及30S和50S核糖體亞單位蛋白(30S、50S ribosomal subunit proteins)。這些蛋白質對營養物質的輸入和蛋白質的合成是不可或缺的，對細菌的生存至關重要。增加的蛋白質包括谷氨酰胺合成酶(glutamine synthetase)、蘋果酸酶(malate dehydrogenase)、RNA聚合酶亞單位(RNA polymerase subunit)以及分子伴侶(molecular chaperone)蛋白DnaK和GroEL，它們在新陳代謝、DNA和蛋白質合成以及修復機制中發揮作用。這些增加的蛋白質維持細菌機能，然而它們不能抵抗減少蛋白質的影響，最終導致細菌被殺死。這是第一個研究有關於Sulbactam對鮑氏不動桿菌的殺菌作用中，減少ABC轉運蛋白和30S及50S核糖體亞單位蛋白質起重要的作用。從整個細菌表面上的感測器來看，雙組分調控系統(Two-component regulatory systems, TCSs)對細菌的適應環境能力和調控機能非常重要。在這項研究當中我們鎖定研究兩種TCSs即AdeSR和BaeSR。藉由Swiss-Model比對出一個與TCSs的二聚體和組胺酸磷酸化(DHp)以及催化ATP結合結構(catalytic and ATP-binding, CA)域高相似度的蛋白質。使用分子對接模擬工具SwissDock和ArgusLab將結構上與Sulbactam和其他乙內醯胺抑制劑，與所選的蛋白質序列4JAS對接。用這兩個分析工具的分析結果，Sulbactam可以在4JAS的活性位置上以相對穩定態進行反應。Sulbactam很可能與BaeSR和AdeSR的活性位置相互作用，由於其較小尺寸和與Mg2+形成離子鍵的能力，它有可能與BaeSR和AdeSR中的ATP/ADP競爭來影響鮑氏不動桿菌的繁殖。這是首次利用分子對接分析研究Sulbactam與鮑式不動桿菌中TCSs之間的關聯性。

Acinetobacter baumannii is associated with hospital intensive care unit infections such as respiratory-associated pneumonia and meningitis. It is often used in combination with β-lactam antibiotics to treat patients with infections. Sulbactam alone has been found to be useful in the treatment of infections caused by A. baumannii, although the mechanism of bactericidal action remains unknown. In this study, proteomics was used to analyze the changes in protein expression and to analyze the protein changes in A. baumannii after Sulbactam treatment. A total of 54 proteins were found to have significant changes in intensity. The proteins with reduced expression included ATP-binding cassette (ABC) transporters proteins and 30S and 50S ribosomal subunit proteins. These proteins are essential for nutrient import and protein synthesis and are critical for bacterial survival. The increased proteins include glutamine synthetase, malic enzyme, RNA polymerase subunits, and the molecular chaperone proteins DnaK and GroEL, which play a role in metabolism, DNA and protein synthesis, and repair mechanisms. These increased proteins maintain bacterial function, but they do not resist the effects of reduced proteins, ultimately leading to bacterial killing. This is the first study on the bactericidal effect of Sulbactam on A. baumannii in which the reduction of ABC transport protein and 30S and 50S ribosomal subunit proteins play an important role. On the other hand, the mechanism of sulbactam action from a sensor perspective. Two-component regulatory systems (TCSs) are important for the environmental adaptability and regulatory functions of bacteria, as evidenced by the sensors on the whole bacterial surface. In this study, we targeted two TCSs, AdeSR and BaeSR, and compared a protein with high similarity to the dimerization and histidine phosphorylation (DHp) and catalytic and ATP-binding (CA) domains of the TCSs by Swiss-Model. Molecular docking simulation tools SwissDock and ArgusLab were used to structurally dock Sulbactam and other acetamide inhibitors to the selected protein sequence 4JAS. Using the results of these two analytical tools, Sulbactam can react in a relatively stable state at the active site of 4JAS. Sulbactam is likely to interact with the active sites of BaeSR and AdeSR, and due to its small size and ability to form ionic bonds with Mg2+, it is likely to compete with ATP/ADP in BaeSR and AdeSR. This is the first study of the association between Sulbactam and TCSs in A. baumannii using molecular docking analysis.

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