Abstract:
:Type VI secretion systems (T6SS) are trans-envelope machines dedicated to the secretion of virulence factors into eukaryotic or prokaryotic cells, therefore required for pathogenesis and/or for competition towards neighboring bacteria. The T6SS apparatus resembles the injection device of bacteriophage T4, and is anchored to the cell envelope through a membrane complex. This membrane complex is composed of the TssL, TssM and TagL inner membrane anchored proteins and of the TssJ outer membrane lipoprotein. Here, we report the crystal structure of the enteroaggregative Escherichia coli Sci1 TssJ lipoprotein, a two four-stranded β-sheets protein that exhibits a transthyretin fold with an additional α-helical domain and a protruding loop. We showed that TssJ contacts TssM through this loop since a loop depleted mutant failed to interact with TssM in vitro or in vivo. Biophysical analysis of TssM and TssJ-TssM interaction suggest a structural model of the membrane-anchored outer shell of T6SS. Collectively, our results provide an improved understanding of T6SS assembly and encourage structure-aided drug design of novel antimicrobials targeting T6SS.
journal_name
PLoS Pathogjournal_title
PLoS pathogensauthors
Felisberto-Rodrigues C,Durand E,Aschtgen MS,Blangy S,Ortiz-Lombardia M,Douzi B,Cambillau C,Cascales Edoi
10.1371/journal.ppat.1002386subject
Has Abstractpub_date
2011-11-01 00:00:00pages
e1002386issue
11eissn
1553-7366issn
1553-7374pii
PPATHOGENS-D-11-01602journal_volume
7pub_type
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