Proteomic Analysis of Extracellular Proteins from Escherichia coli W3110

Citations Over TimeTop 13% of 2006 papers

Abstract

While numerous proteomic analyses have been carried out on Escherichia coli, the vast majority have focused on expression of intracellular proteins. Yet, recent literature reports imply that even in laboratory strains, significant proteins may be found outside the cell. Here, we identify extracellular proteins associated with nonpathogenic E. coli strain W3110. Two-dimensional gel electrophoresis (2DE) revealed approximately 66 prominent protein spots during exponential growth (4 and 8 h shake flask culture) in minimal medium. The absence of detectable nucleic acids in the culture supernatant implies these proteins did not result from cell lysis. MALDI-TOF MS was used to identify 44 proteins, most of which have been previously identified as either outer membrane or extracellular proteins. In addition, 2DE protease zymogram analysis was carried out which facilitated identification of three extracellular proteases, one of which was not observed during standard 2DE. Our results are consistent with previous findings which imply outer membrane proteins are shed during growth.

Related Papers

• → In search of partners: linking extracellular proteases to substrates(2007)344 cited
• → Are bacterial proteases important virulence factors?(1997)90 cited
• → Proteases in the diet of monogastric animals(2021)2 cited
• ANALYSIS OF PROTEASE KINDS AND ACTIVITIES IN SEVEN KINDS OF TISSUES AND ORGANS OF ANDRIAS DAVIDIANUS(2004)
• [Partial purification and properties of proteases of bitoxibacillin].(1980)