ZapA, a possible virulence factor from Proteus mirabilis exhibits broad protease substrate specificity
Autor(a) principal: | |
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Data de Publicação: | 2001 |
Outros Autores: | , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Brazilian Journal of Medical and Biological Research |
Texto Completo: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2001001100004 |
Resumo: | 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. |
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Brazilian Journal of Medical and Biological Research |
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ZapA, a possible virulence factor from Proteus mirabilis exhibits broad protease substrate specificityProteus mirabilismetalloproteasesubstrate specificityfluorogenic peptidesIgAinsulin ß-chainThe 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.Associação Brasileira de Divulgação Científica2001-11-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2001001100004Brazilian Journal of Medical and Biological Research v.34 n.11 2001reponame:Brazilian Journal of Medical and Biological Researchinstname:Associação Brasileira de Divulgação Científica (ABDC)instacron:ABDC10.1590/S0100-879X2001001100004info:eu-repo/semantics/openAccessAnéas,M.A.F.Portaro,F.C.V.Lebrun,I.Juliano,L.Palma,M.S.Fernandes,B.L.eng2001-11-07T00:00:00Zoai:scielo:S0100-879X2001001100004Revistahttps://www.bjournal.org/https://old.scielo.br/oai/scielo-oai.phpbjournal@terra.com.br||bjournal@terra.com.br1414-431X0100-879Xopendoar:2001-11-07T00:00Brazilian Journal of Medical and Biological Research - Associação Brasileira de Divulgação Científica (ABDC)false |
dc.title.none.fl_str_mv |
ZapA, a possible virulence factor from Proteus mirabilis exhibits broad protease substrate specificity |
title |
ZapA, a possible virulence factor from Proteus mirabilis exhibits broad protease substrate specificity |
spellingShingle |
ZapA, a possible virulence factor from Proteus mirabilis exhibits broad protease substrate specificity Anéas,M.A.F. Proteus mirabilis metalloprotease substrate specificity fluorogenic peptides IgA insulin ß-chain |
title_short |
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_sort |
ZapA, a possible virulence factor from Proteus mirabilis exhibits broad protease substrate specificity |
author |
Anéas,M.A.F. |
author_facet |
Anéas,M.A.F. Portaro,F.C.V. Lebrun,I. Juliano,L. Palma,M.S. Fernandes,B.L. |
author_role |
author |
author2 |
Portaro,F.C.V. Lebrun,I. Juliano,L. Palma,M.S. Fernandes,B.L. |
author2_role |
author author author author author |
dc.contributor.author.fl_str_mv |
Anéas,M.A.F. Portaro,F.C.V. Lebrun,I. Juliano,L. Palma,M.S. Fernandes,B.L. |
dc.subject.por.fl_str_mv |
Proteus mirabilis metalloprotease substrate specificity fluorogenic peptides IgA insulin ß-chain |
topic |
Proteus mirabilis metalloprotease substrate specificity fluorogenic peptides IgA insulin ß-chain |
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. |
publishDate |
2001 |
dc.date.none.fl_str_mv |
2001-11-01 |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2001001100004 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2001001100004 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/S0100-879X2001001100004 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
text/html |
dc.publisher.none.fl_str_mv |
Associação Brasileira de Divulgação Científica |
publisher.none.fl_str_mv |
Associação Brasileira de Divulgação Científica |
dc.source.none.fl_str_mv |
Brazilian Journal of Medical and Biological Research v.34 n.11 2001 reponame:Brazilian Journal of Medical and Biological Research instname:Associação Brasileira de Divulgação Científica (ABDC) instacron:ABDC |
instname_str |
Associação Brasileira de Divulgação Científica (ABDC) |
instacron_str |
ABDC |
institution |
ABDC |
reponame_str |
Brazilian Journal of Medical and Biological Research |
collection |
Brazilian Journal of Medical and Biological Research |
repository.name.fl_str_mv |
Brazilian Journal of Medical and Biological Research - Associação Brasileira de Divulgação Científica (ABDC) |
repository.mail.fl_str_mv |
bjournal@terra.com.br||bjournal@terra.com.br |
_version_ |
1754302931323060224 |