ArticlePloS one2014
Assessing the exoproteome of marine bacteria, lesson from a RTX-toxin abundantly secreted by Phaeobacter strain DSM 17395.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 11 citations in OpenAlex.
- The Proteogenome of SymbioticMicroorganisms · 2022Article
- Metaexoproteomics Reveals Microbial Behavior in the Ocean's Interior.Frontiers in microbiology · 2022Article
- Excess labile carbon promotes the expression of virulence factors in coral reef bacterioplankton.The ISME journal · 2018Article
- Exoproteome Analysis of the Seaweed PathogenFrontiers in microbiology · 2017Article
- "You produce while I clean up", a strategy revealed by exoproteomics during Synechococcus-Roseobacter interactions.Proteomics · 2015Article
- Genome sequence of the Roseovarius mucosus type strain (DSM 17069(T)), a bacteriochlorophyll a-containing representative of the marine Roseobacter group isolated from the dinoflagellate Alexandrium ostenfeldii.Standards in genomic sciences · 2015Article
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Authors and funding
3 authors at 2 institutions in 1 country.
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Abstract
Bacteria from the Roseobacter clade are abundant in surface marine ecosystems as over 10% of bacterial cells in the open ocean and 20% in coastal waters belong to this group. In order to document how these marine bacteria interact with their environment, we analyzed the exoproteome of Phaeobacter strain DSM 17395. We grew the strain in marine medium, collected the exoproteome and catalogued its content with high-throughput nanoLC-MS/MS shotgun proteomics. The major component represented 60% of the total protein content but was refractory to either classical proteomic identification or proteogenomics. We de novo sequenced this abundant protein with high-resolution tandem mass spectra which turned out being the 53 kDa RTX-toxin ZP_02147451. It comprised a peptidase M10 serralysin domain. We explained its recalcitrance to trypsin proteolysis and proteomic identification by its unusual low number of basic residues. We found this is a conserved trait in RTX-toxins from Roseobacter strains which probably explains their persistence in the harsh conditions around bacteria. Comprehensive analysis of exoproteomes from environmental bacteria should take into account this proteolytic recalcitrance.
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