ArticleInfection and immunity2005
Comparative secretome analyses of three Bacillus anthracis strains with variant plasmid contents.
Article in Infection and immunity, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 58 citations in OpenAlex.
- TrackingACS omega · 2026Review
- Article
- Molecular engineering of secretory machinery components for high-level secretion of proteins in Bacillus species.Journal of industrial microbiology & biotechnology · 2014Review
- Exocytosis and Endocytosis of Small Vesicles across the Plasma Membrane in Saccharomyces cerevisiae.Membranes · 2014Review
- Identification and validation of specific markers of Bacillus anthracis spores by proteomics and genomics approaches.Molecular & cellular proteomics : MCP · 2014Article
- Glucose induces rapid changes in the secretome of Saccharomyces cerevisiae.Proteome science · 2014Article
- The endocytosis gene END3 is essential for the glucose-induced rapid decline of small vesicles in the extracellular fraction in Saccharomyces cerevisiae.Journal of extracellular vesicles · 2014Article
- Modulation of the Bacillus anthracis secretome by the immune inhibitor A1 protease.Journal of bacteriology · 2014Article
- Identification of peptide sequences as a measure of Anthrax vaccine stability during storage.Human vaccines & immunotherapeutics · 2014Article
- Tracing putative trafficking of the glycolytic enzyme enolase via SNARE-driven unconventional secretion.Eukaryotic cell · 2012Article
- Extracellular Proteins of Mycoplasma synoviae.ISRN veterinary science · 2012Article
- Comparative proteome analysis of Bacillus anthracis with pXO1 plasmid content.Journal of microbiology (Seoul, Korea) · 2010Article
- Transcriptional and apoptotic responses of THP-1 cells to challenge with toxigenic, and non-toxigenic Bacillus anthracis.BMC immunology · 2008Article
- Bacillus anthracis secretome time course under host-simulated conditions and identification of immunogenic proteins.Proteome science · 2007Article
- Identification of in vivo-expressed immunogenic proteins by serological proteome analysis of the Bacillus anthracis secretome.Infection and immunity · 2007Article
- Differential proteomic analysis of the Bacillus anthracis secretome: distinct plasmid and chromosome CO2-dependent cross talk mechanisms modulate extracellular proteolytic activities.Journal of bacteriology · 2006Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacillus anthracis, the causative agent of anthrax, secretes numerous proteins into the extracellular environment during infection. A comparative proteomic approach was employed to elucidate the differences among the extracellular proteomes (secretomes) of three isogenic strains of B. anthracis that differed solely in their plasmid contents. The strains utilized were the wild-type virulent B. anthracis RA3 (pXO1(+) pXO2(+)) and its two nonpathogenic derivative strains: the toxigenic, nonencapsulated RA3R (pXO1(+) pXO2(-)) and the totally cured, nontoxigenic, nonencapsulated RA3:00 (pXO1(-) pXO2(-)). Comparative proteomics using two-dimensional gel electrophoresis followed by computer-assisted gel image analysis was performed to reveal unique, up-regulated, or down-regulated secretome proteins among the strains. In total, 57 protein spots, representing 26 different proteins encoded on the chromosome or pXO1, were identified by peptide mass fingerprinting. S-layer-derived proteins, such as Sap and EA1, were most frequently observed. Many sporulation-associated enzymes were found to be overexpressed in strains containing pXO1(+). This study also provides evidence that pXO2 is necessary for the maximal expression of the pXO1-encoded toxins lethal factor (LF), edema factor (EF), and protective antigen (PA). Several newly identified putative virulence factors were observed; these include enolase, a high-affinity zinc uptake transporter, the peroxide stress-related alkyl hydroperoxide reductase, isocitrate lyase, and the cell surface protein A.
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