ZapA, a possible virulence factor from Proteus mirabilis exhibits broad protease substrate specificity
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 d...
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| Format: | Article |
| Language: | English |
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Associação Brasileira de Divulgação Científica
2001-11-01
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| Series: | Brazilian Journal of Medical and Biological Research |
| Subjects: | |
| Online Access: | http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2001001100004 |
| _version_ | 1811337247492931584 |
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| author | M.A.F. Anéas F.C.V. Portaro I. Lebrun L. Juliano M.S. Palma B.L. Fernandes |
| author_facet | M.A.F. Anéas F.C.V. Portaro I. Lebrun L. Juliano M.S. Palma B.L. Fernandes |
| author_sort | M.A.F. Anéas |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-04-13T17:52:04Z |
| format | Article |
| id | doaj.art-ffb9878c16ef4542964e4b587a07b01f |
| institution | Directory Open Access Journal |
| issn | 0100-879X 1414-431X |
| language | English |
| last_indexed | 2024-04-13T17:52:04Z |
| publishDate | 2001-11-01 |
| publisher | Associação Brasileira de Divulgação Científica |
| record_format | Article |
| series | Brazilian Journal of Medical and Biological Research |
| spelling | doaj.art-ffb9878c16ef4542964e4b587a07b01f2022-12-22T02:36:40ZengAssociação Brasileira de Divulgação CientíficaBrazilian Journal of Medical and Biological Research0100-879X1414-431X2001-11-0134111397140310.1590/S0100-879X2001001100004ZapA, a possible virulence factor from Proteus mirabilis exhibits broad protease substrate specificityM.A.F. AnéasF.C.V. PortaroI. LebrunL. JulianoM.S. PalmaB.L. FernandesThe 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.http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2001001100004Proteus mirabilismetalloproteasesubstrate specificityfluorogenic peptidesIgAinsulin ß-chain |
| spellingShingle | M.A.F. Anéas F.C.V. Portaro I. Lebrun L. Juliano M.S. Palma B.L. Fernandes ZapA, a possible virulence factor from Proteus mirabilis exhibits broad protease substrate specificity Brazilian Journal of Medical and Biological Research Proteus mirabilis metalloprotease substrate specificity fluorogenic peptides IgA insulin ß-chain |
| title | ZapA, a possible virulence factor from Proteus mirabilis exhibits broad protease substrate specificity |
| title_full | ZapA, a possible virulence factor from Proteus mirabilis exhibits broad protease substrate specificity |
| title_fullStr | ZapA, a possible virulence factor from Proteus mirabilis exhibits broad protease substrate specificity |
| title_full_unstemmed | ZapA, a possible virulence factor from Proteus mirabilis exhibits broad protease substrate specificity |
| title_short | ZapA, a possible virulence factor from Proteus mirabilis exhibits broad protease substrate specificity |
| title_sort | zapa a possible virulence factor from proteus mirabilis exhibits broad protease substrate specificity |
| topic | Proteus mirabilis metalloprotease substrate specificity fluorogenic peptides IgA insulin ß-chain |
| url | http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2001001100004 |
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