Refine
Document Type
- Article (32)
Language
- English (32)
Has Fulltext
- yes (32)
Is part of the Bibliography
- no (32)
Keywords
- - (23)
- proteomics (10)
- metaproteomics (4)
- <i>Streptococcus pneumoniae</i> (2)
- LL-37 (2)
- adaptation (2)
- antimicrobial peptides (2)
- mass spectrometry (2)
- metabolomics (2)
- metagenomics (2)
- microbiome (2)
- 16S rRNA gene sequencing (1)
- 16S rRNA gene-sequencing (1)
- 16S sequencing (1)
- 2D PAGE (1)
- <i>Bacillus subtilis</i> (1)
- <i>Clostridiodes difficile</i> (1)
- <i>Enterobacter</i> (1)
- A549 (1)
- Bacillus licheniformis (1)
- Biorefinery process (1)
- C. difficile (1)
- CRISPR-Cas (1)
- Clp proteolysis (1)
- Green algae (1)
- LepB (1)
- Marine polysaccharide (1)
- McsB arginine kinase (1)
- MgsR activity (1)
- MgsR degradation (1)
- RNAlater (1)
- RpoN signaling (1)
- S-thioallylation (1)
- SILAC (1)
- SRM (1)
- Sec-translocon (1)
- Ser/Thr kinases (1)
- Stickland reactions (1)
- Ulvan (1)
- YidC (1)
- absolute protein quantification (1)
- aggregate biofilm (1)
- allicin (1)
- antibiotic (1)
- antibiotic resistance (1)
- antibiotics (1)
- antimicrobial peptide (1)
- archaea (1)
- arginine phosphorylation (1)
- asthma (1)
- bacillithiol (1)
- bacteria (1)
- bacterial membrane vesicles (1)
- bioenergetics (1)
- biofilm (1)
- bioinformatics (1)
- biomedical model swine (1)
- biotechnology (1)
- bivalve (1)
- carbapenem (1)
- cell surface antigens (1)
- co-infection (1)
- colony biofilm (1)
- cystic fibrosis (1)
- dendritic cells (1)
- diallyl polysulfane (1)
- exacerbation (1)
- extracellular vesicles (1)
- flash freezing (1)
- florfenicol (1)
- gastrointestinal microbiome (1)
- hBD3 (1)
- haloarchaea (1)
- host-pathogen interactions (1)
- imipenem (1)
- immuno-magnetic purification (1)
- influenza A virus (1)
- integrated multi-omics (1)
- intestinal tract microbiome (1)
- iron limitation (1)
- label-free quantification (1)
- marine bacteria (1)
- membrane proteins (1)
- metabolism (1)
- metatranscriptomics (1)
- methanogenesis (1)
- methanogenic archaea (1)
- microbial community (1)
- microbiota (1)
- mitochondria (1)
- multi-omics (1)
- nasal microbiome (1)
- nisin (1)
- osmotic stress (1)
- outer membrane vesicles (1)
- oxidative stress (1)
- pathogen vacuole (1)
- periplasm (1)
- phosphatases (1)
- phosphopeptide enrichment (1)
- phosphoproteomics (1)
- pneumococci (1)
- posttranslational modification (PTM) (1)
- primary macrophages (1)
- protein production (1)
- protein synthesis (1)
- proteomic analysis (1)
- recombinant protein (1)
- resistance (1)
- respiration (1)
- sample storage (1)
- shotgun-proteomics (1)
- small RNA (1)
- spectral library (1)
- sputum (1)
- starvation (1)
- subcellular fractionation (1)
- supercomplexes (1)
- temperature (1)
- toxin formation (1)
- ubiquitin (1)
- vaccines (1)
- zinc transport (1)
Institute
- Abteilung für Mikrobiologie und Molekularbiologie (13)
- Institut für Mikrobiologie - Abteilung für Genetik & Biochemie (8)
- Institut für Pharmazie (5)
- Institut für Chemie und Biochemie (2)
- Interfakultäres Institut für Genetik und Funktionelle Genomforschung (UMG) (2)
- Friedrich-Loeffler-Institut für Medizinische Mikrobiologie (1)
- Institut für Diagnostische Radiologie (1)
- Interfakultäres Institut für Genetik und Funktionelle Genomforschung (MNF) (1)
Publisher
- Frontiers Media S.A. (13)
- MDPI (11)
- Nature Publishing Group (2)
- BioMed Central (BMC) (1)
- Frontiers (1)
- John Wiley & Sons, Inc. (1)
- John Wiley & Sons, Ltd (1)
- Springer Nature (1)
- Wiley (1)
Bacillus subtilis has been extensively used as a microbial cell factory for industrial enzymes due to its excellent capacities for protein secretion and large-scale fermentation. This bacterium is also an attractive host for biopharmaceutical production. However, the secretion potential of this organism is not fully utilized yet, mostly due to a limited understanding of critical rearrangements in the membrane proteome upon high-level protein secretion. Recently, it was shown that bottlenecks in heterologous protein secretion can be resolved by genome minimization. Here, we present for the first time absolute membrane protein concentrations of a genome-reduced B. subtilis strain (“midiBacillus”) expressing the immunodominant Staphylococcus aureus antigen A (IsaA). We quantitatively characterize the membrane proteome adaptation of midiBacillus during production stress on the level of molecules per cell for more than 400 membrane proteins, including determination of protein concentrations for ∼61% of the predicted transporters. We demonstrate that ∼30% of proteins with unknown functions display a significant increase in abundance, confirming the crucial role of membrane proteins in vital biological processes. In addition, our results show an increase of proteins dedicated to translational processes in response to IsaA induction. For the first time reported, we provide accumulation rates of a heterologous protein, demonstrating that midiBacillus secretes 2.41 molecules of IsaA per minute. Despite the successful secretion of this protein, it was found that there is still some IsaA accumulation occurring in the cytosol and membrane fraction, leading to a severe secretion stress response, and a clear adjustment of the cell’s array of transporters. This quantitative dataset offers unprecedented insights into bioproduction stress responses in a synthetic microbial cell.