ZapA, a possible virulence factor from Proteus mirabilis exhibits broad protease substrate specificity
| Autor: | Beatriz L. Fernandes, Fernanda C. V. Portaro, M. A. F. Anéas, Ivo Lebrun, Mario Sergio Palma, L. Juliano |
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| Přispěvatelé: | Universidade de São Paulo (USP), Instituto Butantan, Universidade Federal de São Paulo (UNIFESP), Universidade Estadual Paulista (Unesp) |
| Jazyk: | angličtina |
| Rok vydání: | 2001 |
| Předmět: |
metalloprotease
Physiology substrate specificity Immunology Biophysics Virulence Biology Cleavage (embryo) Biochemistry Mass Spectrometry Virulence factor Hydrolysis Bacterial Proteins General Pharmacology Toxicology and Pharmaceutics lcsh:QH301-705.5 Proteus mirabilis insulin ß-chain chemistry.chemical_classification Metalloproteinase lcsh:R5-920 General Neuroscience Metalloendopeptidases Cell Biology General Medicine fluorogenic peptides biology.organism_classification Enzyme chemistry lcsh:Biology (General) lcsh:Medicine (General) Bacteria IgA |
| Zdroj: | SciELO Repositório Institucional da UNESP Universidade Estadual Paulista (UNESP) instacron:UNESP Brazilian Journal of Medical and Biological Research v.34 n.11 2001 Brazilian Journal of Medical and Biological Research Associação Brasileira de Divulgação Científica (ABDC) instacron:ABDC Brazilian Journal of Medical and Biological Research, Vol 34, Iss 11, Pp 1397-1403 (2001) Brazilian Journal of Medical and Biological Research, Volume: 34, Issue: 11, Pages: 1397-1403, Published: NOV 2001 |
| ISSN: | 0100-879X |
| Popis: | Submitted by Guilherme Lemeszenski (guilherme@nead.unesp.br) on 2013-08-22T18:52:39Z No. of bitstreams: 1 S0100-879X2001001100004.pdf: 65223 bytes, checksum: 70eb4858923bff83dbb8b171af5b0ae0 (MD5) Made available in DSpace on 2013-08-22T18:52:39Z (GMT). No. of bitstreams: 1 S0100-879X2001001100004.pdf: 65223 bytes, checksum: 70eb4858923bff83dbb8b171af5b0ae0 (MD5) Previous issue date: 2001-11-01 Made available in DSpace on 2013-09-30T19:44:03Z (GMT). No. of bitstreams: 2 S0100-879X2001001100004.pdf: 65223 bytes, checksum: 70eb4858923bff83dbb8b171af5b0ae0 (MD5) S0100-879X2001001100004.pdf.txt: 25554 bytes, checksum: 06ea4d348f37b61b5cedabdcabfb43c2 (MD5) Previous issue date: 2001-11-01 Submitted by Vitor Silverio Rodrigues (vitorsrodrigues@reitoria.unesp.br) on 2014-05-20T13:54:58Z No. of bitstreams: 2 S0100-879X2001001100004.pdf: 65223 bytes, checksum: 70eb4858923bff83dbb8b171af5b0ae0 (MD5) S0100-879X2001001100004.pdf.txt: 25554 bytes, checksum: 06ea4d348f37b61b5cedabdcabfb43c2 (MD5) Made available in DSpace on 2014-05-20T13:54:58Z (GMT). No. of bitstreams: 2 S0100-879X2001001100004.pdf: 65223 bytes, checksum: 70eb4858923bff83dbb8b171af5b0ae0 (MD5) S0100-879X2001001100004.pdf.txt: 25554 bytes, checksum: 06ea4d348f37b61b5cedabdcabfb43c2 (MD5) Previous issue date: 2001-11-01 The opportunistic bacterium Proteus mirabilis secretes a metalloprotease, ZapA, considered to be one of its virulence factors due to its IgA-degrading activity. However, the substrate specificity of this enzyme has not yet been fully characterized. In the present study we used fluorescent peptides derived from bioactive peptides and the oxidized ß-chain of insulin to determine the enzyme specificity. The bradykinin- and dynorphin-derived peptides were cleaved at the single bonds Phe-Ser and Phe-Leu, with catalytic efficiencies of 291 and 13 mM/s, respectively. Besides confirming already published cleavage sites, a novel cleavage site was determined for the ß-chain of insulin (Val-Asn). Both the natural and the recombinant enzyme displayed the same broad specificity, demonstrated by the presence of hydrophobic, hydrophilic, charged and uncharged amino acid residues at the scissile bonds. Native IgA, however, was resistant to hydrolysis by ZapA. Universidade de São Paulo Instituto de Ciências Biomédicas Departamento de Microbiologia Instituto Butantan CEPID-FAPESP Centro de Toxinologia Aplicada Universidade Federal de São Paulo (UNIFESP) CEPID-FAPESP Centro de Toxinologia Aplicada Universidade Estadual Paulista CEPID-FAPESP Centro de Toxinologia Aplicada Universidade Estadual Paulista CEPID-FAPESP Centro de Toxinologia Aplicada |
| Databáze: | OpenAIRE |
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