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            <title xml:lang="en">Drosophila immunity: a large-scale in vivo RNAi screen identifies five serine proteases required for Toll activation.</title>
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                <forename type="first">Zakaria</forename>
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                <forename type="first">Sylvain</forename>
                <surname>Brun</surname>
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                <forename type="first">Kuniaki</forename>
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                <forename type="first">Ryu</forename>
                <surname>Ueda</surname>
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                <forename>Nathalie</forename>
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            <funder>Association pour la Recherche contre le Cancer (ARC), the Schlumberger and Bettencourt Foundation, and the Programme Microbiologie (PRMMIP00). Grants from MITILS to R.U. and from the Mext of Japan to K.T. and R.U. - H.-J.N. and W.-J.L. were supported by the BK21 program of the Korea Ministry of Education</funder>
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              <date type="whenSubmitted">2007-02-26 14:39:07</date>
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              <date type="whenReleased">2007-02-26 14:39:07</date>
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            <idno type="halRefHtml">&lt;i&gt;Current Biology&lt;/i&gt;, 2006, 16 (8), pp.808-13. &lt;a target="_blank" href="https://dx.doi.org/10.1016/j.cub.2006.03.020"&gt;&amp;#x27E8;10.1016/j.cub.2006.03.020&amp;#x27E9;&lt;/a&gt;</idno>
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                <title xml:lang="en">Drosophila immunity: a large-scale in vivo RNAi screen identifies five serine proteases required for Toll activation.</title>
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                    <surname>Jang</surname>
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                    <forename type="first">Hyuck-Jin</forename>
                    <surname>Nam</surname>
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                    <forename type="first">Yves</forename>
                    <surname>Romeo</surname>
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                    <surname>Takahashi</surname>
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                  <persName>
                    <forename type="first">Won-Jae</forename>
                    <surname>Lee</surname>
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                  <persName>
                    <forename type="first">Ryu</forename>
                    <surname>Ueda</surname>
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                  <idno type="halauthorid">194871-0</idno>
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                    <forename type="first">Bruno</forename>
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                <title level="j">Current Biology</title>
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                  <publisher>Elsevier</publisher>
                  <biblScope unit="volume">16</biblScope>
                  <biblScope unit="issue">8</biblScope>
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                  <date type="datePub">2006-04-18</date>
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              <classCode scheme="mesh">Animals</classCode>
              <classCode scheme="mesh">Carrier Proteins</classCode>
              <classCode scheme="mesh">Drosophila</classCode>
              <classCode scheme="mesh">Drosophila Proteins</classCode>
              <classCode scheme="mesh">Enterococcus faecalis</classCode>
              <classCode scheme="mesh">Gram-Positive Bacterial Infections</classCode>
              <classCode scheme="mesh">Micrococcus luteus</classCode>
              <classCode scheme="mesh">RNA Interference</classCode>
              <classCode scheme="mesh">Serine Endopeptidases</classCode>
              <classCode scheme="mesh">Toll-Like Receptors</classCode>
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              <p>Unlike mammalian Toll-like Receptors, the Drosophila Toll receptor does not interact directly with microbial determinants but is rather activated upon binding a cleaved form of the cytokine-like molecule Spatzle (Spz). During the immune response, Spz is thought to be processed by secreted serine proteases (SPs) present in the hemolymph that are activated by the recognition of gram-positive bacteria or fungi . In the present study, we have used an in vivo RNAi strategy to inactivate 75 distinct Drosophila SP genes. We then screened this collection for SPs regulating the activation of the Toll pathway by gram-positive bacteria. Here, we report the identification of five novel SPs that function in an extracellular pathway linking the recognition proteins GNBP1 and PGRP-SA to Spz. Interestingly, four of these genes are also required for Toll activation by fungi, while one is specifically associated with signaling in response to gram-positive bacterial infections. These results demonstrate the existence of a common cascade of SPs upstream of Spz, integrating signals sent by various secreted recognition molecules via more specialized SPs.</p>
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