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.

Bernardini, G., Laschi, M., Serchi, T., Arena, S., D'Ambrosio, C., Braconi, D., et al. (2011). Mapping phosphoproteins in Neisseria meningitidis serogroup A. PROTEOMICS, 11(7), 1351-1358 [10.1002/pmic.201000406].

Mapping phosphoproteins in Neisseria meningitidis serogroup A

BERNARDINI, GIULIA;LASCHI, MARCELLA;BRACONI, DANIELA;SANTUCCI, ANNALISA
2011

Abstract

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.
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/11365/21097
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