Journal
JOURNAL OF BACTERIOLOGY
Volume 188, Issue 7, Pages 2411-2420Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JB.188.7.2411-2420.2006
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Funding
- NIAID NIH HHS [R01 AI049978, AI49978] Funding Source: Medline
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Salmonella enterica serovar Typhimurium encodes two type III secretion systems (TTSSs) within pathogenicity island 1 (SPI-1) and island 2 (SPI-2). These type III protein secretion and translocation systems transport a panel of bacterial effector proteins across both the bacterial and the host cell membranes to promote bacterial entry and subsequent survival inside host cells. Effector proteins contain secretion and translocation signals that are often located at their N termini. We have developed a ruffling-based translocation reporter system that uses the secretion- and translocation-deficient catalytic domain of SopE, SopE(78-240), as a reporter. Using this assay, we determined that the N-terminall 45 amino acid residues of Salmonella SopA are necessary and sufficient for directing its secretion and translocation through the SPI-1 TTSS. SopA(1-45), but not SopA(1-44), is also able to bind to its chaperone, InvB, indicating that SPI-1 type III secretion and translocation of SopA require its chaperone.
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