title: Salmonella pathogenicity island 1 (SPI-1) type III secretion of SopD involves N- and C-terminal signals and direct binding to the InvC ATPase.
abstract: Salmonella enterica serovar Typhimurium (S. Typhimurium) is an important pathogen and a causative agent of gastroenteritis. During infection, S. Typhimurium assembles molecular-needle complexes termed type III secretion (T3S) systems to translocate effector proteins from the bacterial cytoplasm directly into the host cell. The T3S signals that direct the secretion of effectors still remain enigmatic. SopD is a key T3S effector contributing to the systemic virulence of S. Typhimurium and the development of gastroenteritis. We have scrutinized the distribution of the SopD T3S signals using in silico analysis and a targeted deletion approach. We show that amino acid residues 6-10 act as the N-terminal secretion signal for Salmonella pathogenicity island 1 (SPI-1) T3S. Furthermore, we show that two putative C-terminal helical regions of SopD are essential for its secretion and also help prevent erroneous secretion through the flagellar T3S machinery. In addition, using protein-protein interaction assays, we have identified an association between SopD and the SPI-1 T3S system ATPase, InvC. These findings demonstrate that T3S of SopD involves multiple signals and protein interactions, providing important mechanistic insights into effector protein secretion.
authors.affiliation: Institute for Cell and Molecular Biosciences and School of Biomedical Sciences, The Medical School, Newcastle University, Framlington Place, Newcastle upon Tyne NE2 4HH, UK.
authors.forename: R
authors.initials: R
authors.lastname: Boonyom
authors.affiliation: Institute for Cell and Molecular Biosciences and School of Biomedical Sciences, The Medical School, Newcastle University, Framlington Place, Newcastle upon Tyne NE2 4HH, UK.
authors.forename: M H
authors.initials: MH
authors.lastname: Karavolos
authors.affiliation: Institute for Cell and Molecular Biosciences and School of Biomedical Sciences, The Medical School, Newcastle University, Framlington Place, Newcastle upon Tyne NE2 4HH, UK.
authors.forename: D M
authors.initials: DM
authors.lastname: Bulmer
authors.affiliation: Institute for Cell and Molecular Biosciences and School of Biomedical Sciences, The Medical School, Newcastle University, Framlington Place, Newcastle upon Tyne NE2 4HH, UK.
authors.forename: C M A
authors.initials: CMA
authors.lastname: Khan
mesh_terms: D000251:Adenosine Triphosphatases / Q000235:genetics / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D044404:Genomic Islands; D054730:Protein Interaction Domains and Motifs; D006180:Proton-Translocating ATPases / Q000737:chemistry / Q000378:metabolism*; D012486:Salmonella typhimurium / Q000235:genetics / Q000378:metabolism* / Q000472:pathogenicity; D037521:Virulence Factors / Q000737:chemistry / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; C116105:SopD protein, Salmonella; D037521:Virulence Factors; C088598:invC protein, Salmonella typhimurium; D000251:Adenosine Triphosphatases; D006180:Proton-Translocating ATPases