This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Wassif, C.
Right arrow Articles by Belas, R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Wassif, C.
Right arrow Articles by Belas, R.

 Previous Article  |  Next Article 

J. Bacteriol., Oct 1995, 5790-5798, Vol 177, No. 20
Copyright © 1995, American Society for Microbiology

Molecular analysis of a metalloprotease from Proteus mirabilis

C Wassif, D Cheek and R Belas
Center of Marine Biotechnology, University of Maryland Biotechnology Institute, Baltimore 21202, USA.

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.


This article has been cited by other articles:

  • Felfoldi, G., Marokhazi, J., Kepiro, M., Venekei, I. (2009). Identification of Natural Target Proteins Indicates Functions of a Serralysin-Type Metalloprotease, PrtA, in Anti-Immune Mechanisms. Appl. Environ. Microbiol. 75: 3120-3126 [Abstract] [Full Text]  
  • Hatfaludi, T., Al-Hasani, K., Dunstone, M., Boyce, J., Adler, B. (2008). Characterization of TolC Efflux Pump Proteins from Pasteurella multocida. Antimicrob. Agents Chemother. 52: 4166-4171 [Abstract] [Full Text]  
  • Phan, V., Belas, R., Gilmore, B. F., Ceri, H. (2008). ZapA, a Virulence Factor in a Rat Model of Proteus mirabilis-Induced Acute and Chronic Prostatitis. Infect. Immun. 76: 4859-4864 [Abstract] [Full Text]  
  • Himpsl, S. D., Lockatell, C. V., Hebel, J. R., Johnson, D. E., Mobley, H. L. T. (2008). Identification of virulence determinants in uropathogenic Proteus mirabilis using signature-tagged mutagenesis. J Med Microbiol 57: 1068-1078 [Abstract] [Full Text]  
  • Jacobsen, S. M., Stickler, D. J., Mobley, H. L. T., Shirtliff, M. E. (2008). Complicated Catheter-Associated Urinary Tract Infections Due to Escherichia coli and Proteus mirabilis. Clin. Microbiol. Rev. 21: 26-59 [Abstract] [Full Text]  
  • Posadas, D. M., Martin, F. A., Sabio y Garcia, J. V., Spera, J. M., Delpino, M. V., Baldi, P., Campos, E., Cravero, S. L., Zorreguieta, A. (2007). The TolC Homologue of Brucella suis Is Involved in Resistance to Antimicrobial Compounds and Virulence. Infect. Immun. 75: 379-389 [Abstract] [Full Text]  
  • Belas, R., Manos, J., Suvanasuthi, R. (2004). Proteus mirabilis ZapA Metalloprotease Degrades a Broad Spectrum of Substrates, Including Antimicrobial Peptides. Infect. Immun. 72: 5159-5167 [Abstract] [Full Text]  
  • Bjerkan, T. M., Bender, C. L., Ertesvag, H., Drablos, F., Fakhr, M. K., Preston, L. A., Skjak-Braek, G., Valla, S. (2004). The Pseudomonas syringae Genome Encodes a Combined Mannuronan C-5-epimerase and O-Acetylhydrolase, Which Strongly Enhances the Predicted Gel-forming Properties of Alginates. J. Biol. Chem. 279: 28920-28929 [Abstract] [Full Text]  
  • Almogren, A., Senior, B. W., Loomes, L. M., Kerr, M. A. (2003). Structural and Functional Consequences of Cleavage of Human Secretory and Human Serum Immunoglobulin A1 by Proteinases from Proteusmirabilis and Neisseriameningitidis. Infect. Immun. 71: 3349-3356 [Abstract] [Full Text]  
  • Dattelbaum, J. D., Lockatell, C. V., Johnson, D. E., Mobley, H. L. T. (2003). UreR, the Transcriptional Activator of the Proteus mirabilis Urease Gene Cluster, Is Required for Urease Activity and Virulence in Experimental Urinary Tract Infections. Infect. Immun. 71: 1026-1030 [Abstract] [Full Text]  
  • Fraser, G. M., Claret, L., Furness, R., Gupta, S., Hughes, C. (2002). Swarming-coupled expression of the Proteus mirabilis hpmBA haemolysin operon. Microbiology 148: 2191-2201 [Abstract] [Full Text]  
  • Palacios, J. L., Zaror, I., Martínez, P., Uribe, F., Opazo, P., Socías, T., Gidekel, M., Venegas, A. (2001). Subset of Hybrid Eukaryotic Proteins Is Exported by the Type I Secretion System of Erwinia chrysanthemi. J. Bacteriol. 183: 1346-1358 [Abstract] [Full Text]  
  • Woods, R. G., Burger, M., Beven, C.-A., Beacham, I. R. (2001). The aprX-lipA operon of Pseudomonas fluorescens B52: a molecular analysis of metalloprotease and lipase production. Microbiology 147: 345-354 [Abstract] [Full Text]  
  • Burger, M., Woods, R. G., McCarthy, C., Beacham, I. R. (2000). Temperature regulation of protease in Pseudomonas fluorescens LS107d2 by an ECF sigma factor and a transmembrane activator. Microbiology 146: 3149-3155 [Abstract] [Full Text]  
  • Belas, R., Schneider, R., Melch, M. (1998). Characterization of Proteus mirabilis Precocious Swarming Mutants: Identification of rsbA, Encoding a Regulator of Swarming Behavior. J. Bacteriol. 180: 6126-6139 [Abstract] [Full Text]  
  • Finnie, C., Zorreguieta, A., Hartley, N. M., Downie, J. A. (1998). Characterization of Rhizobium leguminosarum Exopolysaccharide Glycanases That Are Secreted via a Type I Exporter and Have a Novel Heptapeptide Repeat Motif. J. Bacteriol. 180: 1691-1699 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»