Dipartimento di Biologia Molecolare, Università degli Studi di Siena, via Fiorentina, Siena, Italy.
Proteomics. 2011 Apr;11(7):1351-8. doi: 10.1002/pmic.201000406. Epub 2011 Feb 17.
To investigate the phosphorylation capability of serogroup A Neisseria meningitidis (MenA) and to implement our knowledge in meningococcal biology and in bacterial post-translational modifications, cell extracts were separated by 2-DE and 51 novel phosphoproteins were revealed by the use of the highly specific Ser/Thr/Tyr-phosphorylated proteins staining by Pro-Q Diamond and identified by MALDI-ToF/MS. Our results indicate that phosphorylation in MenA is comparable to that of other bacterial species. A first functional characterization of the identified modified proteins was also given, in order to understand their role in meningococcal physiopathology.
为了研究 A 群脑膜炎奈瑟菌（MenA）的磷酸化能力，并将我们的知识应用于脑膜炎奈瑟菌生物学和细菌翻译后修饰中，使用 Pro-Q Diamond 特异性地对丝氨酸/苏氨酸/酪氨酸磷酸化蛋白进行染色，通过二维电泳分离细胞提取物，揭示了 51 种新型磷酸蛋白，并通过 MALDI-ToF/MS 进行鉴定。我们的结果表明，MenA 的磷酸化与其他细菌物种相当。我们还对鉴定出的修饰蛋白进行了初步的功能表征，以了解它们在脑膜炎奈瑟菌病理生理学中的作用。
