ArticleJournal of bacteriology1995
Molecular analysis of a metalloprotease from Proteus mirabilis.
Article in Journal of bacteriology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
What it found
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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
28 citing papers in PubMed, 87 citations in OpenAlex.
- Impact of COVID-19 pandemic on antimicrobial resistance of Proteus mirabilis in a Brazilian hospital.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2025Article
- Overview ofFrontiers in microbiology · 2024Review
- Hacking the Immune Response to Solid Tumors: Harnessing the Anti-Cancer Capacities of Oncolytic Bacteria.Pharmaceutics · 2023Review
- A CpxR-RegulatedInfection and immunity · 2020Article
- Pathogenesis ofEcoSal Plus · 2018Review
- Induction of Different Apoptosis Pathways by TwoFrontiers in physiology · 2018Article
- The detrimental impact of extracellular bacterial proteases on wound healing.International wound journal · 2017Review
- Proteus mirabilis and Urinary Tract Infections.Microbiology spectrum · 2015Review
- Review
- Transcriptome of Proteus mirabilis in the murine urinary tract: virulence and nitrogen assimilation gene expression.Infection and immunity · 2011Article
- RTX proteins: a highly diverse family secreted by a common mechanism.FEMS microbiology reviews · 2010Review
- Zinc uptake contributes to motility and provides a competitive advantage to Proteus mirabilis during experimental urinary tract infection.Infection and immunity · 2010Article
- Identification of natural target proteins indicates functions of a serralysin-type metalloprotease, PrtA, in anti-immune mechanisms.Applied and environmental microbiology · 2009Article
- The effect of monoterpenes on swarming differentiation and haemolysin activity in Proteus mirabilis.Molecules (Basel, Switzerland) · 2008Article
- Characterization of TolC efflux pump proteins from Pasteurella multocida.Antimicrobial agents and chemotherapy · 2008Article
- ZapA, a virulence factor in a rat model of Proteus mirabilis-induced acute and chronic prostatitis.Infection and immunity · 2008Article
- Complicated catheter-associated urinary tract infections due to Escherichia coli and Proteus mirabilis.Clinical microbiology reviews · 2008Review
- The TolC homologue of Brucella suis is involved in resistance to antimicrobial compounds and virulence.Infection and immunity · 2007Article
- Virulence of Pseudomonas aeruginosa cells surviving photodynamic treatment with toluidine blue.Current microbiology · 2005Article
- Proteus mirabilis ZapA metalloprotease degrades a broad spectrum of substrates, including antimicrobial peptides.Infection and immunity · 2004Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 2 countries.
Funding
Abstract
Proteus mirabilis is known for its ability to differentiate from swimmer to swarmer cells, a process crucial for the pathogenesis of these bacteria during urinary tract infections. Among the many virulence factors produced during swarmer cell differentiation is an extracellular metalloprotease. A cosmid containing a large fragment of P. mirabilis chromosomal DNA was obtained by measuring protease expression in recombinant Escherichia coli. The recombinant and native enzymes were purified to over 95% homogeneity from culture supernatants by use of phenyl-Sepharose affinity chromatography and found to be identical. The activity of the 55-kDa enzyme was stimulated by divalent cations (Ca2+ > Mg2+) and inhibited by a chelator of these cations. The enzyme possesses substrate specificity for both serum and secretory forms of immunoglobulin A1 (IgA1) and IgA2 as well as IgG and, unlike classic IgA proteases, digested to completion both human and mouse IgA. Following subcloning, a 5-kb DNA fragment encoding recombinant protease activity was identified by insertional mutagenesis with Tn5. Four open reading frames were identified within this 5-kb region by limited nucleotide sequence analysis of DNA flanking the transposon. The nucleotide and deduced amino acid sequences of the metalloprotease structural gene (zapA) were obtained. Computerized homology studies revealed that the P. mirabilis metalloprotein is a member of the serralysin family of proteases and may be part of an operon comprising genes encoding an ATP-dependent ABC transporter in addition to the metalloprotease. The relevance of the metalloprotease to swarmer cell differentiation and pathogenicity is discussed.
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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.