ArticleProteome science2007
Bacillus anthracis secretome time course under host-simulated conditions and identification of immunogenic proteins.
Article in Proteome science, 2007. 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, 48 citations in OpenAlex.
- Immunoproteomic analysis of Clostridium botulinum type B secretome for identification of immunogenic proteins against botulism.Biotechnology letters · 2021Article
- Serological evidence for human exposure to Bacillus cereus biovar anthracis in the villages around Taï National Park, Côte d'Ivoire.PLoS neglected tropical diseases · 2020Article
- Over-expression, purification, and confirmation of Bacillus anthracis transcriptional regulator NprR.Protein expression and purification · 2016Article
- Design, Synthesis and Evaluation of Triazole-Pyrimidine Analogues as SecA Inhibitors.ChemMedChem · 2016Article
- Review
- Identification of peptide sequences as a measure of Anthrax vaccine stability during storage.Human vaccines & immunotherapeutics · 2014Article
- How are the non-classically secreted bacterial proteins released into the extracellular milieu?Current microbiology · 2013Review
- Root exudate-induced alterations in Bacillus cereus cell wall contribute to root colonization and plant growth promotion.PloS one · 2013Article
- Immunoproteomic analysis of bacterial proteins of Actinobacillus pleuropneumoniae serotype 1.Proteome science · 2011Article
- Bacillus anthracis interacts with plasmin(ogen) to evade C3b-dependent innate immunity.PloS one · 2011Article
- Comparative proteomic analysis of extracellular proteins of Clostridium perfringens type A and type C strains.Infection and immunity · 2010Article
- Expanding the known repertoire of virulence factors produced by Bacillus cereus through early secretome profiling in three redox conditions.Molecular & cellular proteomics : MCP · 2010Article
- An experimental approach for the identification of conserved secreted proteins in trypanosomatids.Journal of biomedicine & biotechnology · 2010Article
- Immunoproteomic analysis of outer membrane proteins and extracellular proteins of Actinobacillus pleuropneumoniae JL03 serotype 3.BMC microbiology · 2009Article
- Differential proteomic analysis of Clostridium perfringens ATCC13124; identification of dominant, surface and structure associated proteins.BMC microbiology · 2009Article
- Identification of novel and cross-species seroreactive proteins from Bacillus anthracis using a ligation-independent cloning-based, SOS-inducible expression system.Microbial pathogenesisArticle
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe secretion time course of Bacillus anthracis strain RA3R (pXO1+/pXO2-) during early, mid, and late log phase were investigated under conditions that simulate those encountered in the host. All of the identified proteins were analyzed by different software algorithms to characterize their predicted mode of secretion and cellular localization. In addition, immunogenic proteins were identified using sera from humans with cutaneous anthrax.
resultsA total of 275 extracellular proteins were identified by a combination of LC MS/MS and MALDI-TOF MS. All of the identified proteins were analyzed by SignalP, SecretomeP, PSORT, LipoP, TMHMM, and PROSITE to characterize their predicted mode of secretion, cellular localization, and protein domains. Fifty-three proteins were predicted by SignalP to harbor the cleavable N-terminal signal peptides and were therefore secreted via the classical Sec pathway. Twenty-three proteins were predicted by SecretomeP for secretion by the alternative Sec pathway characterized by the lack of typical export signal. In contrast to SignalP and SecretomeP predictions, PSORT predicted 171 extracellular proteins, 7 cell wall-associated proteins, and 6 cytoplasmic proteins. Moreover, 51 proteins were predicted by LipoP to contain putative Sec signal peptides (38 have SpI sites), lipoprotein signal peptides (13 have SpII sites), and N-terminal membrane helices (9 have transmembrane helices). The TMHMM algorithm predicted 25 membrane-associated proteins with one to ten transmembrane helices. Immunogenic proteins were also identified using sera from patients who have recovered from anthrax. The charge variants (83 and 63 kDa) of protective antigen (PA) were the most immunodominant secreted antigens, followed by charge variants of enolase and transketolase.
conclusionThis is the first description of the time course of protein secretion for the pathogen Bacillus anthracis. Time course studies of protein secretion and accumulation may be relevant in elucidation of the progression of pathogenicity, identification of therapeutics and diagnostic markers, and vaccine development. This study also adds to the continuously growing list of identified Bacillus anthracis secretome proteins.
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