The first 45 amino acids of SopA are necessary for InvB binding and SPI-1 secretion.
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, SopE78-240, as a reporter. Using this assay, we determined that the N-terminal 45 amino acid residues of Salmonella SopA are necessary and sufficient for directing its secretion and translocation through the SPI-1 TTSS. SopA1-45, but not SopA1-44, is also able to bind to its chaperone, InvB, indicating that SPI-1 type III secretion and translocation of SopA require its chaperone.
Department of Biological Sciences, Purdue University, West Lafayette, IN 47907, USA.
Wendy
W
Higashide
Daoguo
D
Zhou
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism*; D002460:Cell Line; D017353:Gene Deletion; D015964:Gene Expression Regulation, Bacterial; D006801:Humans; D018832:Molecular Chaperones; D011485:Protein Binding; D021381:Protein Transport; D012486:Salmonella typhimurium / Q000235:genetics / Q000378:metabolism*
D001426:Bacterial Proteins; D018832:Molecular Chaperones; C419942:Spi1 protein, Salmonella; C088597:invB protein, Salmonella; C060971:SopA protein, Bacteria