ArticleInfection and immunity2004
Camelysin is a novel surface metalloproteinase from Bacillus cereus.
Article in Infection and immunity, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
18 citing papers in PubMed, 45 citations in OpenAlex.
- Archaeal bundling pili ofProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Tandem Mass Tag-Based Quantitative Proteomics and Virulence Phenotype of Hemolymph-Treated Bacillus thuringiensis kurstaki Cells Reveal New Insights on Bacterial Pathogenesis in Insects.Microbiology spectrum · 2021Article
- SpoVG is an important regulator of sporulation and affects biofilm formation by regulating Spo0A transcription in Bacillus cereus 0-9.BMC microbiology · 2021Article
- TheMicrobiology (Reading, England) · 2021Article
- The Distribution of Several Genomic Virulence Determinants Does Not Corroborate the Established Serotyping Classification ofInternational journal of molecular sciences · 2021Article
- The Food Poisoning Toxins ofToxins · 2021Review
- Expression ofMicroorganisms · 2020Article
- AtxA-Controlled Small RNAs ofFrontiers in microbiology · 2020Article
- Repertoire of theToxins · 2019Review
- Structural changes of TasA in biofilm formation ofProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Alternative modes of biofilm formation by plant-associated Bacillus cereus.MicrobiologyOpen · 2015Article
- Proteomic analysis of Bacillus thuringiensis at different growth phases by using an automated online two-dimensional liquid chromatography-tandem mass spectrometry strategy.Applied and environmental microbiology · 2012Article
- A Bacillus anthracis strain deleted for six proteases serves as an effective host for production of recombinant proteins.Protein expression and purification · 2011Article
- Bacillus anthracis sin locus and regulation of secreted proteases.Journal of bacteriology · 2011Article
- Isolation, characterization and biological role of camelysin from Bacillus thuringiensis subsp. israelensis.Current microbiology · 2010Article
- Bacillus cereus-induced permeability of the blood-ocular barrier during experimental endophthalmitis.Investigative ophthalmology & visual science · 2009Article
- A novel immunogenic spore coat-associated protein in Bacillus anthracis: characterization via proteomics approaches and a vector-based vaccine system.Protein expression and purification · 2008Article
- 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
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacillus cereus frequently causes food poisoning or nosocomial diseases. Vegetative cells express the novel surface metalloproteinase camelysin (casein-cleaving metalloproteinase) during exponential growth on complex, peptide-rich media. Camelysin is strongly bound to the cell surface and can be solubilized only by detergents or butanol. Camelysin spontaneously migrates from the surface of intact bacterial cells to preformed liposomes. The complete sequence of the camelysin-encoding gene, calY, was determined by reverse PCR on the basis of the N-terminal sequence and some internal tryptic cleavage peptides. The calY gene codes for a polypeptide of 21.569 kDa with a putative signal peptide of 27 amino acids (2.513 kDa) preceding the mature protein (19.056 kDa). Although the predicted amino acid sequence of CalY does not exhibit a typical metalloprotease consensus sequence, high-pressure liquid chromatography-purified camelysin contains one zinc ion per protein molecule. Matrix-assisted laser desorption ionization-time-of-flight mass spectrometry and tryptic peptide mass fingerprinting confirmed the identity of this zinc-binding protein as CalY. Disruption of the calY gene results in a strong decrease in the cell-bound proteolytic activity on various substrates.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.