ParkinsonFranceV1, Hal, Corpus, bibRecord, 000026

A family of diverse Kunitz inhibitors from Echinococcus granulosus potentially involved in host-parasite cross-talk.

Identifieur interne : 000026 ( Hal/Corpus ); précédent : 000025; suivant : 000027

A family of diverse Kunitz inhibitors from Echinococcus granulosus potentially involved in host-parasite cross-talk.

Auteurs : Silvia González ; Martín Fl ; Mariana Margenat ; Rosario Durán ; Gualberto González-Sapienza ; Martín Gra A ; John Parkinson ; Rick M. Maizels ; Gustavo Salinas ; Beatriz Alvarez ; Cecilia Fernández

Source :

PLoS ONE [ 1932-6203 ] ; 2009.

RBID : Hal:pasteur-00508939

Abstract

The cestode Echinococcus granulosus, the agent of hydatidosis/echinococcosis, is remarkably well adapted to its definitive host. However, the molecular mechanisms underlying the successful establishment of larval worms (protoscoleces) in the dog duodenum are unknown. With the aim of identifying molecules participating in the E. granulosus-dog cross-talk, we surveyed the transcriptomes of protoscoleces and protoscoleces treated with pepsin at pH 2. This analysis identified a multigene family of secreted monodomain Kunitz proteins associated mostly with pepsin/H(+)-treated worms, suggesting that they play a role at the onset of infection. We present the relevant molecular features of eight members of the E. granulosus Kunitz family (EgKU-1 - EgKU-8). Although diverse, the family includes three pairs of close paralogs (EgKU-1/EgKU-4; EgKU-3/EgKU-8; EgKU-6/EgKU-7), which would be the products of recent gene duplications. In addition, we describe the purification of EgKU-1 and EgKU-8 from larval worms, and provide data indicating that some members of the family (notably, EgKU-3 and EgKU-8) are secreted by protoscoleces. Detailed kinetic studies with native EgKU-1 and EgKU-8 highlighted their functional diversity. Like most monodomain Kunitz proteins, EgKU-8 behaved as a slow, tight-binding inhibitor of serine proteases, with global inhibition constants (K(I) (*)) versus trypsins in the picomolar range. In sharp contrast, EgKU-1 did not inhibit any of the assayed peptidases. Interestingly, molecular modeling revealed structural elements associated with activity in Kunitz cation-channel blockers. We propose that this family of inhibitors has the potential to act at the E. granulosus-dog interface and interfere with host physiological processes at the initial stages of infection.

Url:

https://hal-riip.archives-ouvertes.fr/pasteur-00508939

DOI: 10.1371/journal.pone.0007009

Links to Exploration step

Hal:pasteur-00508939

Le document en format XML

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<author><name sortKey="Fernandez, Cecilia" sort="Fernandez, Cecilia" uniqKey="Fernandez C" first="Cecilia" last="Fernández">Cecilia Fernández</name>
<affiliation><hal:affiliation type="laboratory" xml:id="struct-131694" status="INCOMING">  <orgName>Cátedra de Inmunología</orgName>
  <desc>    <address>      <addrLine>Universidad de la República Montevideo</addrLine>
      <country key="UY"></country>
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  </desc>
  <listRelation>    <relation active="#struct-310031" type="direct"></relation>
  </listRelation>
<tutelles><tutelle active="#struct-310031" type="direct"><org type="institution" xml:id="struct-310031" status="INCOMING">  <orgName>Facultad de Quimica</orgName>
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<idno type="DOI">10.1371/journal.pone.0007009</idno>
<series><title level="j">PLoS ONE</title>
<idno type="ISSN">1932-6203</idno>
<imprint><date type="datePub">2009</date>
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<front><div type="abstract" xml:lang="en">The cestode Echinococcus granulosus, the agent of hydatidosis/echinococcosis, is remarkably well adapted to its definitive host. However, the molecular mechanisms underlying the successful establishment of larval worms (protoscoleces) in the dog duodenum are unknown. With the aim of identifying molecules participating in the E. granulosus-dog cross-talk, we surveyed the transcriptomes of protoscoleces and protoscoleces treated with pepsin at pH 2. This analysis identified a multigene family of secreted monodomain Kunitz proteins associated mostly with pepsin/H(+)-treated worms, suggesting that they play a role at the onset of infection. We present the relevant molecular features of eight members of the E. granulosus Kunitz family (EgKU-1 - EgKU-8). Although diverse, the family includes three pairs of close paralogs (EgKU-1/EgKU-4; EgKU-3/EgKU-8; EgKU-6/EgKU-7), which would be the products of recent gene duplications. In addition, we describe the purification of EgKU-1 and EgKU-8 from larval worms, and provide data indicating that some members of the family (notably, EgKU-3 and EgKU-8) are secreted by protoscoleces. Detailed kinetic studies with native EgKU-1 and EgKU-8 highlighted their functional diversity. Like most monodomain Kunitz proteins, EgKU-8 behaved as a slow, tight-binding inhibitor of serine proteases, with global inhibition constants (K(I) (*)) versus trypsins in the picomolar range. In sharp contrast, EgKU-1 did not inhibit any of the assayed peptidases. Interestingly, molecular modeling revealed structural elements associated with activity in Kunitz cation-channel blockers. We propose that this family of inhibitors has the potential to act at the E. granulosus-dog interface and interfere with host physiological processes at the initial stages of infection.</div>
</front>
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<hal api="V3">          <titleStmt>            <title xml:lang="en">A family of diverse Kunitz inhibitors from Echinococcus granulosus potentially involved in host-parasite cross-talk.</title>
            <author role="aut">              <persName>                <forename type="first">Silvia</forename>
                <surname>González</surname>
              </persName>
              <idno type="halauthorid">516127</idno>
              <affiliation ref="#struct-131694"></affiliation>
            </author>
            <author role="aut">              <persName>                <forename type="first">Martín</forename>
                <surname>Fló</surname>
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              <idno type="halauthorid">516128</idno>
              <affiliation ref="#struct-131694"></affiliation>
              <affiliation ref="#struct-131695"></affiliation>
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            <author role="aut">              <persName>                <forename type="first">Mariana</forename>
                <surname>Margenat</surname>
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              <idno type="halauthorid">516129</idno>
              <affiliation ref="#struct-131694"></affiliation>
            </author>
            <author role="aut">              <persName>                <forename type="first">Rosario</forename>
                <surname>Durán</surname>
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              <idno type="halauthorid">516130</idno>
              <affiliation ref="#struct-55924"></affiliation>
            </author>
            <author role="aut">              <persName>                <forename type="first">Gualberto</forename>
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              <affiliation ref="#struct-131694"></affiliation>
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            <author role="aut">              <persName>                <forename type="first">Martín</forename>
                <surname>Graña</surname>
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              <idno type="halauthorid">516132</idno>
              <affiliation ref="#struct-55924"></affiliation>
            </author>
            <author role="aut">              <persName>                <forename type="first">John</forename>
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              <idno type="halauthorid">516133</idno>
              <affiliation ref="#struct-131696"></affiliation>
            </author>
            <author role="aut">              <persName>                <forename type="first">Rick M</forename>
                <surname>Maizels</surname>
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              <idno type="halauthorid">516134</idno>
              <affiliation ref="#struct-131697"></affiliation>
            </author>
            <author role="aut">              <persName>                <forename type="first">Gustavo</forename>
                <surname>Salinas</surname>
              </persName>
              <idno type="halauthorid">516135</idno>
              <affiliation ref="#struct-131694"></affiliation>
            </author>
            <author role="aut">              <persName>                <forename type="first">Beatriz</forename>
                <surname>Alvarez</surname>
              </persName>
              <idno type="halauthorid">516136</idno>
              <affiliation ref="#struct-131695"></affiliation>
            </author>
            <author role="crp">              <persName>                <forename type="first">Cecilia</forename>
                <surname>Fernández</surname>
              </persName>
              <email type="md5">85b28fe4bc843afd1af65bc9e46be72a</email>
              <email type="domain">fq.edu.uy</email>
              <idno type="halauthorid">516137</idno>
              <affiliation ref="#struct-131694"></affiliation>
            </author>
            <editor role="depositor">              <persName>                <forename>Martín</forename>
                <surname>Graña</surname>
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              <email type="md5">c6f32c284cbf49d6bbb95a51a93c3ead</email>
              <email type="domain">pasteur.edu.uy</email>
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          <editionStmt>            <edition n="v1" type="current">              <date type="whenSubmitted">2010-11-04 10:25:59</date>
              <date type="whenModified">2010-11-04 10:27:16</date>
              <date type="whenReleased">2010-11-04 10:27:16</date>
              <date type="whenProduced">2009</date>
              <date type="whenEndEmbargoed">2010-11-04</date>
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              <name key="153059">                <persName>                  <forename>Martín</forename>
                  <surname>Graña</surname>
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                <email type="domain">pasteur.edu.uy</email>
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            <idno type="halRefHtml">PLoS ONE, Public Library of Science, 2009, 4 (9), pp.e7009. <10.1371/journal.pone.0007009></idno>
            <idno type="halRef">PLoS ONE, Public Library of Science, 2009, 4 (9), pp.e7009. <10.1371/journal.pone.0007009></idno>
          </publicationStmt>
          <seriesStmt>            <idno type="stamp" n="RIIP_MONTEVIDEO" p="RIIP">Institut Pasteur de Montevideo</idno>
            <idno type="stamp" n="RIIP">Institut Pasteur RIIP (Réseau International)</idno>
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          <notesStmt>            <note type="audience" n="2">International</note>
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          <sourceDesc>            <biblStruct>              <analytic>                <title xml:lang="en">A family of diverse Kunitz inhibitors from Echinococcus granulosus potentially involved in host-parasite cross-talk.</title>
                <author role="aut">                  <persName>                    <forename type="first">Silvia</forename>
                    <surname>González</surname>
                  </persName>
                  <idno type="halauthorid">516127</idno>
                  <affiliation ref="#struct-131694"></affiliation>
                </author>
                <author role="aut">                  <persName>                    <forename type="first">Martín</forename>
                    <surname>Fló</surname>
                  </persName>
                  <idno type="halauthorid">516128</idno>
                  <affiliation ref="#struct-131694"></affiliation>
                  <affiliation ref="#struct-131695"></affiliation>
                </author>
                <author role="aut">                  <persName>                    <forename type="first">Mariana</forename>
                    <surname>Margenat</surname>
                  </persName>
                  <idno type="halauthorid">516129</idno>
                  <affiliation ref="#struct-131694"></affiliation>
                </author>
                <author role="aut">                  <persName>                    <forename type="first">Rosario</forename>
                    <surname>Durán</surname>
                  </persName>
                  <idno type="halauthorid">516130</idno>
                  <affiliation ref="#struct-55924"></affiliation>
                </author>
                <author role="aut">                  <persName>                    <forename type="first">Gualberto</forename>
                    <surname>González-Sapienza</surname>
                  </persName>
                  <idno type="halauthorid">516131</idno>
                  <affiliation ref="#struct-131694"></affiliation>
                </author>
                <author role="aut">                  <persName>                    <forename type="first">Martín</forename>
                    <surname>Graña</surname>
                  </persName>
                  <idno type="halauthorid">516132</idno>
                  <affiliation ref="#struct-55924"></affiliation>
                </author>
                <author role="aut">                  <persName>                    <forename type="first">John</forename>
                    <surname>Parkinson</surname>
                  </persName>
                  <idno type="halauthorid">516133</idno>
                  <affiliation ref="#struct-131696"></affiliation>
                </author>
                <author role="aut">                  <persName>                    <forename type="first">Rick M</forename>
                    <surname>Maizels</surname>
                  </persName>
                  <idno type="halauthorid">516134</idno>
                  <affiliation ref="#struct-131697"></affiliation>
                </author>
                <author role="aut">                  <persName>                    <forename type="first">Gustavo</forename>
                    <surname>Salinas</surname>
                  </persName>
                  <idno type="halauthorid">516135</idno>
                  <affiliation ref="#struct-131694"></affiliation>
                </author>
                <author role="aut">                  <persName>                    <forename type="first">Beatriz</forename>
                    <surname>Alvarez</surname>
                  </persName>
                  <idno type="halauthorid">516136</idno>
                  <affiliation ref="#struct-131695"></affiliation>
                </author>
                <author role="crp">                  <persName>                    <forename type="first">Cecilia</forename>
                    <surname>Fernández</surname>
                  </persName>
                  <email type="md5">85b28fe4bc843afd1af65bc9e46be72a</email>
                  <email type="domain">fq.edu.uy</email>
                  <idno type="halauthorid">516137</idno>
                  <affiliation ref="#struct-131694"></affiliation>
                </author>
              </analytic>
              <monogr>                <idno type="halJournalId" status="VALID">28700</idno>
                <idno type="issn">1932-6203</idno>
                <title level="j">PLoS ONE</title>
                <imprint>                  <publisher>Public Library of Science</publisher>
                  <biblScope unit="volume">4</biblScope>
                  <biblScope unit="issue">9</biblScope>
                  <biblScope unit="pp">e7009</biblScope>
                  <date type="datePub">2009</date>
                </imprint>
              </monogr>
              <idno type="doi">10.1371/journal.pone.0007009</idno>
              <idno type="pubmed">19759914</idno>
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          </sourceDesc>
          <profileDesc>            <langUsage>              <language ident="en">English</language>
            </langUsage>
            <textClass>              <classCode scheme="mesh">Amino Acid Sequence</classCode>
              <classCode scheme="mesh">Animals</classCode>
              <classCode scheme="mesh">Pepsin A</classCode>
              <classCode scheme="mesh">Protease Inhibitors</classCode>
              <classCode scheme="mesh">Protein Structure, Tertiary</classCode>
              <classCode scheme="mesh">Sequence Homology, Amino Acid</classCode>
              <classCode scheme="mesh">Serine Proteases</classCode>
              <classCode scheme="mesh">Dogs</classCode>
              <classCode scheme="mesh">Dose-Response Relationship, Drug</classCode>
              <classCode scheme="mesh">Echinococcus granulosus</classCode>
              <classCode scheme="mesh">Gene Expression Profiling</classCode>
              <classCode scheme="mesh">Genes, Helminth</classCode>
              <classCode scheme="mesh">Host-Parasite Interactions</classCode>
              <classCode scheme="mesh">Hydrogen-Ion Concentration</classCode>
              <classCode scheme="mesh">Molecular Sequence Data</classCode>
              <classCode scheme="halDomain" n="info.info-bi">Computer Science [cs]/Bioinformatics [q-bio.QM]</classCode>
              <classCode scheme="halDomain" n="sdv.bibs">Life Sciences [q-bio]/Quantitative Methods [q-bio.QM]</classCode>
              <classCode scheme="halTypology" n="ART">Journal articles</classCode>
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            <abstract xml:lang="en">The cestode Echinococcus granulosus, the agent of hydatidosis/echinococcosis, is remarkably well adapted to its definitive host. However, the molecular mechanisms underlying the successful establishment of larval worms (protoscoleces) in the dog duodenum are unknown. With the aim of identifying molecules participating in the E. granulosus-dog cross-talk, we surveyed the transcriptomes of protoscoleces and protoscoleces treated with pepsin at pH 2. This analysis identified a multigene family of secreted monodomain Kunitz proteins associated mostly with pepsin/H(+)-treated worms, suggesting that they play a role at the onset of infection. We present the relevant molecular features of eight members of the E. granulosus Kunitz family (EgKU-1 - EgKU-8). Although diverse, the family includes three pairs of close paralogs (EgKU-1/EgKU-4; EgKU-3/EgKU-8; EgKU-6/EgKU-7), which would be the products of recent gene duplications. In addition, we describe the purification of EgKU-1 and EgKU-8 from larval worms, and provide data indicating that some members of the family (notably, EgKU-3 and EgKU-8) are secreted by protoscoleces. Detailed kinetic studies with native EgKU-1 and EgKU-8 highlighted their functional diversity. Like most monodomain Kunitz proteins, EgKU-8 behaved as a slow, tight-binding inhibitor of serine proteases, with global inhibition constants (K(I) (*)) versus trypsins in the picomolar range. In sharp contrast, EgKU-1 did not inhibit any of the assayed peptidases. Interestingly, molecular modeling revealed structural elements associated with activity in Kunitz cation-channel blockers. We propose that this family of inhibitors has the potential to act at the E. granulosus-dog interface and interfere with host physiological processes at the initial stages of infection.</abstract>
          </profileDesc>
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A family of diverse Kunitz inhibitors from Echinococcus granulosus potentially involved in host-parasite cross-talk.

A family of diverse Kunitz inhibitors from Echinococcus granulosus potentially involved in host-parasite cross-talk.

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