Comparison of surface proteomes of enterotoxigenic (ETEC) and commensal Escherichia coli strains

Sommer, Ulf; Petersen, Jørn Henrik; Pfeiffer, M.; Schrotz‐King, Petra; Morsczeck, Christian

doi:10.1016/j.mimet.2010.07.011

Cited by 18 publications

(14 citation statements)

References 18 publications

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“…Similar to our findings, L-asparaginase II and EF-Tu have been reported to be immunogenic in other pathogenic bacteria (49,(54)(55)(56)(57)(58)(59). In addition, other studies have described the presence of EF-Tu in E. coli OM or OMP extracts (32,(60)(61)(62)(63)(64), as well as the interaction of EF-Tu with fibronectin (65), indicating the participation of EF-Tu in adhesion to human intestinal cells and mucin (66)(67)(68). It is also possible that EF-Tu belongs to the group of moonlighting proteins (69,70), which can be found in various locations within the bacterial cell and fulfill specific functions that vary by location.…”

Section: Discussionsupporting

confidence: 91%

Immunoproteomic Analysis To Identify Shiga Toxin-Producing Escherichia coli Outer Membrane Proteins Expressed during Human Infection

et al. 2014

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b Shiga-toxin producing Escherichia coli (STEC) is the etiologic agent of acute diarrhea, dysentery, and hemolytic-uremic syndrome (HUS). There is no approved vaccine for STEC infection in humans, and antibiotic use is contraindicated, as it promotes Shiga toxin production. In order to identify STEC-associated antigens and immunogenic proteins, outer membrane proteins (OMPs) were extracted from STEC O26:H11, O103, O113:H21, and O157:H7 strains, and commensal E. coli strain HS was used as a control. SDS-PAGE, two-dimensional-PAGE analysis, Western blot assays using sera from pediatric HUS patients and controls, and matrix-assisted laser desorption ionization-tandem time of flight analyses were used to identify 12 immunogenic OMPs, some of which were not reactive with control sera. Importantly, seven of these proteins have not been previously reported to be immunogenic in STEC strains. Among these seven proteins, OmpT and Cah displayed IgG and IgA reactivity with sera from HUS patients. Genes encoding these two proteins were present in a majority of STEC strains. Knowledge of the antigens produced during infection of the host and the immune response to those antigens will be important for future vaccine development.

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Section: Discussionsupporting

confidence: 91%

Immunoproteomic Analysis To Identify Shiga Toxin-Producing Escherichia coli Outer Membrane Proteins Expressed during Human Infection

et al. 2014

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“…Indeed, across a variety of Rickettsia species, several candidate MLPs have demonstrated immunoreactivity; e.g., cell division protein FtsZ, translation initiation factor 2, cysteinyl-tRNA synthetase, Tuf, ribosomal proteins RplY and RpsB, cytosol aminopeptidase, uncharacterized protein YbgF, AtpD, and chaperones GroES, GroEL, PrsA, SurA and DnaK (Renesto et al ., 2005, Hajem et al ., 2009, Pornwiroon et al ., 2009, Qi et al ., 2013). Furthermore, some of these candidate MLPs have been identified on the cell surfaces of Anaplasmataceae species (Ge & Rikihisa, 2007, Ge & Rikihisa, 2007, Noh et al ., 2008, Gibson et al , 2010), as well as other bacteria (Rhomberg et al ., 2004, Boonjakuakul et al ., 2007, Desvaux et al ., 2010, Sommer et al ., 2010). Collectively, these data suggest that highly conserved proteins with usual cytoplasmic or periplasmic functions are moonlighting on the cell surface of divergent rickettsial species.…”

Section: Secretory Proteins At the Host Interfacementioning

confidence: 99%

Secretome of obligate intracellularRickettsia

et al. 2014

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The genus Rickettsia (Alphaproteobacteria; Rickettsiales; Rickettsiaceae) is comprised of obligate intracellular parasites, with virulent species of interest both as causes of emerging infectious diseases and for their potential deployment as bioterrorism agents. Currently there are no effective commercially available vaccines, with treatment limited primarily to tetracycline antibiotics, though others (e.g., josamycin, ciprofloxacin, chloramphenicol and azithromycin) are also effective. Much of the recent research geared towards understanding mechanisms underlying rickettsial pathogenicity has centered on characterization of secreted proteins that directly engage eukaryotic cells. Herein, we review all aspects of the Rickettsia secretome, including six secretion systems, 19 characterized secretory proteins, and potential moonlighting proteins identified on surfaces of multiple Rickettsia species. Employing bioinformatics and phylogenomics, we present novel structural and functional insight on each secretion system. Unexpectedly, our investigation revealed that the majority of characterized secretory proteins have not been assigned to their cognate secretion pathways. Furthermore, for most secretion pathways, the requisite signal sequences mediating translocation are poorly understood. As a blueprint for all known routes of protein translocation into host cells, this resource will assist research aimed at uniting characterized secreted proteins with their apposite secretion pathways. Furthermore, our work will help in the identification of novel secreted proteins involved in rickettsial “life on the inside”.

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“…Based on genomic comparisons with non-pathogenic E. coli, virulence factors that contribute to bacterial pathogenesis have been singled out and targets for therapeutic interventions have been proposed. In addition, mass spectrometry approaches have been used to map the proteome of various bacterial pathogens and from these data identify vaccine candidates (Berlanda et al, 2008;Zielke et al, 2014;Choi et al, 2011;Hagan and Mobley, 2007;Fleckenstein et al, 2006;Nouwens et al, 2000;Altindis et al, 2014;Sommer et al, 2010). Moreover, these studies have revealed that, in addition to unique virulence proteins, the outer membrane and OMVs released by pathogenic bacteria harbor a large number of proteins, which are also found in commensal strains.…”

Section: Introductionmentioning

confidence: 99%