Plasmepsins IX and X are essential and druggable mediators of malaria parasite egress and invasion
Proteases of the malaria parasite Plasmodium falciparum have long been investigated as drug targets. The P. falciparum genome encodes 10 aspartic proteases called plasmepsins, which are involved in diverse cellular processes. Most have been studied extensively but the functions of plasmepsins IX and...
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| Veröffentlicht in: | Science (American Association for the Advancement of Science) 2017-10, Vol.358 (6362), p.518-522 |
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| creator | Nasamu, Armiyaw S. Glushakova, Svetlana Russo, Ilaria Vaupel, Barbara Oksman, Anna Kim, Arthur S. Fremont, Daved H. Tolia, Niraj Beck, Josh R. Meyers, Marvin J. Niles, Jacquin C. Zimmerberg, Joshua Goldberg, Daniel E. |
| description | Proteases of the malaria parasite Plasmodium falciparum have long been investigated as drug targets. The P. falciparum genome encodes 10 aspartic proteases called plasmepsins, which are involved in diverse cellular processes. Most have been studied extensively but the functions of plasmepsins IX and X (PMIX and PMX) were unknown. Here we show that PMIX is essential for erythrocyte invasion, acting on rhoptry secretory organelle biogenesis. In contrast, PMX is essential for both egress and invasion, controlling maturation of the subtilisin-like serine protease SUB1 in exoneme secretory vesicles. We have identified compounds with potent antimalarial activity targeting PMX, including a compound known to have oral efficacy in a mouse model of malaria. |
| doi_str_mv | 10.1126/science.aan1478 |
| format | Article |
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The P. falciparum genome encodes 10 aspartic proteases called plasmepsins, which are involved in diverse cellular processes. Most have been studied extensively but the functions of plasmepsins IX and X (PMIX and PMX) were unknown. Here we show that PMIX is essential for erythrocyte invasion, acting on rhoptry secretory organelle biogenesis. In contrast, PMX is essential for both egress and invasion, controlling maturation of the subtilisin-like serine protease SUB1 in exoneme secretory vesicles. We have identified compounds with potent antimalarial activity targeting PMX, including a compound known to have oral efficacy in a mouse model of malaria.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.aan1478</identifier><identifier>PMID: 29074774</identifier><language>eng</language><publisher>United States: American Association for the Advancement of Science</publisher><subject>Administration, Oral ; Animals ; Antimalarial activity ; Antimalarial agents ; Antimalarials - administration & dosage ; Antimalarials - chemistry ; Antimalarials - pharmacology ; Antimalarials - therapeutic use ; Aspartic Acid Endopeptidases - antagonists & inhibitors ; Blood ; Blood circulation ; Cell membranes ; Disease Models, Animal ; Egress ; Erythrocytes ; Erythrocytes - parasitology ; Fever ; Genomes ; Malaria ; Malaria, Falciparum - drug therapy ; Maturation ; Membranes ; Merozoites ; Mice ; Parasites ; Plasmodium falciparum ; Plasmodium falciparum - drug effects ; Plasmodium falciparum - enzymology ; Plasmodium falciparum - genetics ; Plasmodium falciparum - pathogenicity ; Protease ; Protease inhibitors ; Proteases ; Proteinase inhibitors ; Protozoan Proteins - metabolism ; Secretory vesicles ; Serine ; Serine proteinase ; Subtilisin ; Subtilisins - metabolism ; Vector-borne diseases</subject><ispartof>Science (American Association for the Advancement of Science), 2017-10, Vol.358 (6362), p.518-522</ispartof><rights>Copyright © 2017 by the American Association for the Advancement of Science</rights><rights>Copyright © 2017 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works.</rights><rights>Copyright © 2017 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works</rights><rights>2017 © The Authors, some rights reserved 2017</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3588-fecabf39a6b1f4bcf50f56424ec8283befa3de602223f2586914c9c1f178b2e93</citedby><cites>FETCH-LOGICAL-c3588-fecabf39a6b1f4bcf50f56424ec8283befa3de602223f2586914c9c1f178b2e93</cites><orcidid>0000-0002-5662-3384 ; 0000-0002-6250-8796 ; 0000-0002-0719-8473 ; 0000-0003-4101-6642 ; 0000-0003-3529-8399 ; 0000-0002-1707-3789 ; 0000-0002-2269-7078 ; 0000-0001-5484-619X</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/26400635$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/26400635$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,776,780,799,881,2871,2872,27901,27902,57992,58225</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29074774$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Nasamu, Armiyaw S.</creatorcontrib><creatorcontrib>Glushakova, Svetlana</creatorcontrib><creatorcontrib>Russo, Ilaria</creatorcontrib><creatorcontrib>Vaupel, Barbara</creatorcontrib><creatorcontrib>Oksman, Anna</creatorcontrib><creatorcontrib>Kim, Arthur S.</creatorcontrib><creatorcontrib>Fremont, Daved H.</creatorcontrib><creatorcontrib>Tolia, Niraj</creatorcontrib><creatorcontrib>Beck, Josh R.</creatorcontrib><creatorcontrib>Meyers, Marvin J.</creatorcontrib><creatorcontrib>Niles, Jacquin C.</creatorcontrib><creatorcontrib>Zimmerberg, Joshua</creatorcontrib><creatorcontrib>Goldberg, Daniel E.</creatorcontrib><title>Plasmepsins IX and X are essential and druggable mediators of malaria parasite egress and invasion</title><title>Science (American Association for the Advancement of Science)</title><addtitle>Science</addtitle><description>Proteases of the malaria parasite Plasmodium falciparum have long been investigated as drug targets. The P. falciparum genome encodes 10 aspartic proteases called plasmepsins, which are involved in diverse cellular processes. Most have been studied extensively but the functions of plasmepsins IX and X (PMIX and PMX) were unknown. Here we show that PMIX is essential for erythrocyte invasion, acting on rhoptry secretory organelle biogenesis. In contrast, PMX is essential for both egress and invasion, controlling maturation of the subtilisin-like serine protease SUB1 in exoneme secretory vesicles. We have identified compounds with potent antimalarial activity targeting PMX, including a compound known to have oral efficacy in a mouse model of malaria.</description><subject>Administration, Oral</subject><subject>Animals</subject><subject>Antimalarial activity</subject><subject>Antimalarial agents</subject><subject>Antimalarials - administration & dosage</subject><subject>Antimalarials - chemistry</subject><subject>Antimalarials - pharmacology</subject><subject>Antimalarials - therapeutic use</subject><subject>Aspartic Acid Endopeptidases - antagonists & inhibitors</subject><subject>Blood</subject><subject>Blood circulation</subject><subject>Cell membranes</subject><subject>Disease Models, Animal</subject><subject>Egress</subject><subject>Erythrocytes</subject><subject>Erythrocytes - parasitology</subject><subject>Fever</subject><subject>Genomes</subject><subject>Malaria</subject><subject>Malaria, Falciparum - drug therapy</subject><subject>Maturation</subject><subject>Membranes</subject><subject>Merozoites</subject><subject>Mice</subject><subject>Parasites</subject><subject>Plasmodium falciparum</subject><subject>Plasmodium falciparum - drug effects</subject><subject>Plasmodium falciparum - enzymology</subject><subject>Plasmodium falciparum - genetics</subject><subject>Plasmodium falciparum - pathogenicity</subject><subject>Protease</subject><subject>Protease inhibitors</subject><subject>Proteases</subject><subject>Proteinase inhibitors</subject><subject>Protozoan Proteins - metabolism</subject><subject>Secretory vesicles</subject><subject>Serine</subject><subject>Serine proteinase</subject><subject>Subtilisin</subject><subject>Subtilisins - metabolism</subject><subject>Vector-borne diseases</subject><issn>0036-8075</issn><issn>1095-9203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkcuLFDEQxoMo7jh69qQ0ePHSu3l3chFk8bGwoAcFb6E6UxkzdCdjMr3gf292Z1wflwSqfl_xVX2EPGf0nDGuL6qPmDyeAyQmB_OArBi1qreciodkRanQvaGDOiNPat1R2npWPCZn3NJBDoNckfHzBHXGfY2pdlffOkibrr0FO6wV0yHCdFfblGW7hXHCbsZNhEMutcuhm2GCEqHbQ4EaD021LU14J4npptVyekoeBZgqPjv9a_L1_bsvlx_7608fri7fXvdeKGP6gB7GICzokQU5-qBoUFpyid5wI0YMIDaoKedcBK6Mtkx661lggxk5WrEmb45z98vYTPrmvsDk9iXOUH66DNH920nxu9vmG6csN5LJNuD1aUDJPxasBzfH6nGaIGFeqmNWDVKr2-Ouyav_0F1eSmrrNWqQ1kjJRaMujpQvudaC4d4Mo-42P3fKz53ya4qXf-9wz_8OrAEvjsCutgz-9LWkVAslfgG8FaQY</recordid><startdate>20171027</startdate><enddate>20171027</enddate><creator>Nasamu, Armiyaw S.</creator><creator>Glushakova, Svetlana</creator><creator>Russo, Ilaria</creator><creator>Vaupel, Barbara</creator><creator>Oksman, Anna</creator><creator>Kim, Arthur S.</creator><creator>Fremont, Daved H.</creator><creator>Tolia, Niraj</creator><creator>Beck, Josh R.</creator><creator>Meyers, Marvin J.</creator><creator>Niles, Jacquin C.</creator><creator>Zimmerberg, Joshua</creator><creator>Goldberg, Daniel E.</creator><general>American Association for the Advancement of Science</general><general>The American Association for the Advancement of Science</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QF</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QQ</scope><scope>7QR</scope><scope>7SC</scope><scope>7SE</scope><scope>7SN</scope><scope>7SP</scope><scope>7SR</scope><scope>7SS</scope><scope>7T7</scope><scope>7TA</scope><scope>7TB</scope><scope>7TK</scope><scope>7TM</scope><scope>7U5</scope><scope>7U9</scope><scope>8BQ</scope><scope>8FD</scope><scope>C1K</scope><scope>F28</scope><scope>FR3</scope><scope>H8D</scope><scope>H8G</scope><scope>H94</scope><scope>JG9</scope><scope>JQ2</scope><scope>K9.</scope><scope>KR7</scope><scope>L7M</scope><scope>L~C</scope><scope>L~D</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-5662-3384</orcidid><orcidid>https://orcid.org/0000-0002-6250-8796</orcidid><orcidid>https://orcid.org/0000-0002-0719-8473</orcidid><orcidid>https://orcid.org/0000-0003-4101-6642</orcidid><orcidid>https://orcid.org/0000-0003-3529-8399</orcidid><orcidid>https://orcid.org/0000-0002-1707-3789</orcidid><orcidid>https://orcid.org/0000-0002-2269-7078</orcidid><orcidid>https://orcid.org/0000-0001-5484-619X</orcidid></search><sort><creationdate>20171027</creationdate><title>Plasmepsins IX and X are essential and druggable mediators of malaria parasite egress and invasion</title><author>Nasamu, Armiyaw S. ; Glushakova, Svetlana ; Russo, Ilaria ; Vaupel, Barbara ; Oksman, Anna ; Kim, Arthur S. ; Fremont, Daved H. ; Tolia, Niraj ; Beck, Josh R. ; Meyers, Marvin J. ; Niles, Jacquin C. ; Zimmerberg, Joshua ; Goldberg, Daniel E.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3588-fecabf39a6b1f4bcf50f56424ec8283befa3de602223f2586914c9c1f178b2e93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Administration, Oral</topic><topic>Animals</topic><topic>Antimalarial activity</topic><topic>Antimalarial agents</topic><topic>Antimalarials - 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Science (American Association for the Advancement of Science)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Nasamu, Armiyaw S.</au><au>Glushakova, Svetlana</au><au>Russo, Ilaria</au><au>Vaupel, Barbara</au><au>Oksman, Anna</au><au>Kim, Arthur S.</au><au>Fremont, Daved H.</au><au>Tolia, Niraj</au><au>Beck, Josh R.</au><au>Meyers, Marvin J.</au><au>Niles, Jacquin C.</au><au>Zimmerberg, Joshua</au><au>Goldberg, Daniel E.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Plasmepsins IX and X are essential and druggable mediators of malaria parasite egress and invasion</atitle><jtitle>Science (American Association for the Advancement of Science)</jtitle><addtitle>Science</addtitle><date>2017-10-27</date><risdate>2017</risdate><volume>358</volume><issue>6362</issue><spage>518</spage><epage>522</epage><pages>518-522</pages><issn>0036-8075</issn><eissn>1095-9203</eissn><abstract>Proteases of the malaria parasite Plasmodium falciparum have long been investigated as drug targets. The P. falciparum genome encodes 10 aspartic proteases called plasmepsins, which are involved in diverse cellular processes. Most have been studied extensively but the functions of plasmepsins IX and X (PMIX and PMX) were unknown. Here we show that PMIX is essential for erythrocyte invasion, acting on rhoptry secretory organelle biogenesis. In contrast, PMX is essential for both egress and invasion, controlling maturation of the subtilisin-like serine protease SUB1 in exoneme secretory vesicles. 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| ispartof | Science (American Association for the Advancement of Science), 2017-10, Vol.358 (6362), p.518-522 |
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| language | eng |
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| source | American Association for the Advancement of Science; Jstor Complete Legacy; MEDLINE |
| subjects | Administration, Oral Animals Antimalarial activity Antimalarial agents Antimalarials - administration & dosage Antimalarials - chemistry Antimalarials - pharmacology Antimalarials - therapeutic use Aspartic Acid Endopeptidases - antagonists & inhibitors Blood Blood circulation Cell membranes Disease Models, Animal Egress Erythrocytes Erythrocytes - parasitology Fever Genomes Malaria Malaria, Falciparum - drug therapy Maturation Membranes Merozoites Mice Parasites Plasmodium falciparum Plasmodium falciparum - drug effects Plasmodium falciparum - enzymology Plasmodium falciparum - genetics Plasmodium falciparum - pathogenicity Protease Protease inhibitors Proteases Proteinase inhibitors Protozoan Proteins - metabolism Secretory vesicles Serine Serine proteinase Subtilisin Subtilisins - metabolism Vector-borne diseases |
| title | Plasmepsins IX and X are essential and druggable mediators of malaria parasite egress and invasion |
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