A newly discovered protein export machine in malaria parasites

Several hundred malaria parasite proteins are exported beyond an encasing vacuole and into the cytosol of the host erythrocyte, a process that is central to the virulence and viability of the causative Plasmodium species. The trafficking machinery responsible for this export is unknown. Here we iden...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Nature (London) 2009-06, Vol.459 (7249), p.945-949
Hauptverfasser: Lundie, Rachel J, Rug, Melanie, Sanders, Paul R, Boddey, Justin A, Gilson, Paul R, Maier, Alexander G, de Koning-Ward, Tania F, Smith, Brian J, Papenfuss, Anthony T, Cowman, Alan F, Crabb, Brendan S
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 949
container_issue 7249
container_start_page 945
container_title Nature (London)
container_volume 459
creator Lundie, Rachel J
Rug, Melanie
Sanders, Paul R
Boddey, Justin A
Gilson, Paul R
Maier, Alexander G
de Koning-Ward, Tania F
Smith, Brian J
Papenfuss, Anthony T
Cowman, Alan F
Crabb, Brendan S
description Several hundred malaria parasite proteins are exported beyond an encasing vacuole and into the cytosol of the host erythrocyte, a process that is central to the virulence and viability of the causative Plasmodium species. The trafficking machinery responsible for this export is unknown. Here we identify in Plasmodium falciparum a translocon of exported proteins (PTEX), which is located in the vacuole membrane. The PTEX complex is ATP-powered, and comprises heat shock protein 101 (HSP101; a ClpA/B-like ATPase from the AAA+ superfamily, of a type commonly associated with protein translocons), a novel protein termed PTEX150 and a known parasite protein, exported protein 2 (EXP2). EXP2 is the potential channel, as it is the membrane-associated component of the core PTEX complex. Two other proteins, a new protein PTEX88 and thioredoxin 2 (TRX2), were also identified as PTEX components. As a common portal for numerous crucial processes, this translocon offers a new avenue for therapeutic intervention. Malaria parasite virulence During intracellular infection of erythrocytes, malaria parasites reside in vacuoles from where they export many proteins into the host cell. These protein secretions play an important role in the virulence and viability of the Plasmodium parasite. The protein export machinery involved in this process has now been identified. Termed PTEX (for Plasmodium Translocon of EXported proteins), it is an ATP-powered complex located in the vacuole membrane, and may provide a new target for antimalarial drugs. Malaria parasites reside in vacuoles during intracellular infection of erythrocytes and export many proteins into the host cell, a process that is essential for the virulence and viability of Plasmodium . Whereas transport across the parasite membrane is known to rely on the secretory pathway, the transporter responsible for the translocation of proteins across the vacuole membrane is now identified.
doi_str_mv 10.1038/nature08104
format Article
fullrecord <record><control><sourceid>gale_proqu</sourceid><recordid>TN_cdi_proquest_miscellaneous_67387813</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><galeid>A630206457</galeid><sourcerecordid>A630206457</sourcerecordid><originalsourceid>FETCH-LOGICAL-c851t-380651b1db3ae88058aa1f9bb5fe147903d1e5d188a73d598dd4a893287fe8a23</originalsourceid><addsrcrecordid>eNqV099r1TAUB_AiirtOn3yXqiiIdiZN0yQvg8vFH4OhoBMfy2l7es1o0y5p3fbfm9HLbq90XKUPhZNPvjmlOUHwlJIjSph8b6AfLBJJSXIvWNBEpFGSSnE_WBASy4hIlh4Ej5w7J4RwKpKHwQFVnKUxF4vgeBkavKyvw1K7ov2NFsuws22P2oR41bW2DxsofmmDoa80UIPVEHZgweke3ePgQQW1wyeb92Hw4-OHs9Xn6PTrp5PV8jQqJKd9xCRJOc1pmTNAKQmXALRSec4r9A0rwkqKvKRSgmAlV7IsE5CKxVJUKCFmh8HrMdf3djGg67PG94t1DQbbwWWpYFJIyvbCmCjGFZcevvgLnreDNf4jvEmSlCmqPHo5ojXUmGlTtb2F4iYxW6aMxCRNuPAqmlFrNGihbg1W2pf_28ck5v4fUb5tdccXnb7IpqF3omnS0QzyT4mNLmZb_acN0xPe7Gzwpserfg2Dc9nJ92-74fvsNPft3XZ59nP1ZTd5v57JLmzrnMUq66xuwF5nlGQ3I5ZNRszrZ5uLM-QNllu7mSkPXm0AuALqyoIptLt1MeWJEop69250zi-ZNdrtDZw_9_nIx-Jt3tT8AcPfPyU</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>204463919</pqid></control><display><type>article</type><title>A newly discovered protein export machine in malaria parasites</title><source>MEDLINE</source><source>Nature Journals Online</source><source>Alma/SFX Local Collection</source><creator>Lundie, Rachel J ; Rug, Melanie ; Sanders, Paul R ; Boddey, Justin A ; Gilson, Paul R ; Maier, Alexander G ; de Koning-Ward, Tania F ; Smith, Brian J ; Papenfuss, Anthony T ; Cowman, Alan F ; Crabb, Brendan S</creator><creatorcontrib>Lundie, Rachel J ; Rug, Melanie ; Sanders, Paul R ; Boddey, Justin A ; Gilson, Paul R ; Maier, Alexander G ; de Koning-Ward, Tania F ; Smith, Brian J ; Papenfuss, Anthony T ; Cowman, Alan F ; Crabb, Brendan S</creatorcontrib><description>Several hundred malaria parasite proteins are exported beyond an encasing vacuole and into the cytosol of the host erythrocyte, a process that is central to the virulence and viability of the causative Plasmodium species. The trafficking machinery responsible for this export is unknown. Here we identify in Plasmodium falciparum a translocon of exported proteins (PTEX), which is located in the vacuole membrane. The PTEX complex is ATP-powered, and comprises heat shock protein 101 (HSP101; a ClpA/B-like ATPase from the AAA+ superfamily, of a type commonly associated with protein translocons), a novel protein termed PTEX150 and a known parasite protein, exported protein 2 (EXP2). EXP2 is the potential channel, as it is the membrane-associated component of the core PTEX complex. Two other proteins, a new protein PTEX88 and thioredoxin 2 (TRX2), were also identified as PTEX components. As a common portal for numerous crucial processes, this translocon offers a new avenue for therapeutic intervention. Malaria parasite virulence During intracellular infection of erythrocytes, malaria parasites reside in vacuoles from where they export many proteins into the host cell. These protein secretions play an important role in the virulence and viability of the Plasmodium parasite. The protein export machinery involved in this process has now been identified. Termed PTEX (for Plasmodium Translocon of EXported proteins), it is an ATP-powered complex located in the vacuole membrane, and may provide a new target for antimalarial drugs. Malaria parasites reside in vacuoles during intracellular infection of erythrocytes and export many proteins into the host cell, a process that is essential for the virulence and viability of Plasmodium . Whereas transport across the parasite membrane is known to rely on the secretory pathway, the transporter responsible for the translocation of proteins across the vacuole membrane is now identified.</description><identifier>ISSN: 0028-0836</identifier><identifier>EISSN: 1476-4687</identifier><identifier>DOI: 10.1038/nature08104</identifier><identifier>PMID: 19536257</identifier><identifier>CODEN: NATUAS</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Amino acids ; Analysis ; Animals ; Animals, Genetically Modified ; Biological and medical sciences ; Blood ; Carrier proteins ; Causes of ; Cell adhesion &amp; migration ; Erythrocytes ; General aspects ; Genetic aspects ; Human protozoal diseases ; Humanities and Social Sciences ; Infectious diseases ; Malaria ; Malaria, Falciparum - parasitology ; Medical sciences ; Models, Biological ; Mortality ; multidisciplinary ; Multiprotein Complexes - chemistry ; Multiprotein Complexes - metabolism ; Parasites ; Parasitic diseases ; Physiological aspects ; Plasmodium falciparum ; Plasmodium falciparum - metabolism ; Protein Binding ; Protein Transport ; Proteins ; Protozoal diseases ; Protozoan Proteins - metabolism ; Science ; Translocation (Genetics) ; Vector-borne diseases ; Virulence (Microbiology)</subject><ispartof>Nature (London), 2009-06, Vol.459 (7249), p.945-949</ispartof><rights>Macmillan Publishers Limited. All rights reserved 2009</rights><rights>2009 INIST-CNRS</rights><rights>COPYRIGHT 2009 Nature Publishing Group</rights><rights>Copyright Nature Publishing Group Jun 18, 2009</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c851t-380651b1db3ae88058aa1f9bb5fe147903d1e5d188a73d598dd4a893287fe8a23</citedby><cites>FETCH-LOGICAL-c851t-380651b1db3ae88058aa1f9bb5fe147903d1e5d188a73d598dd4a893287fe8a23</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,2727,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&amp;idt=21549791$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19536257$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lundie, Rachel J</creatorcontrib><creatorcontrib>Rug, Melanie</creatorcontrib><creatorcontrib>Sanders, Paul R</creatorcontrib><creatorcontrib>Boddey, Justin A</creatorcontrib><creatorcontrib>Gilson, Paul R</creatorcontrib><creatorcontrib>Maier, Alexander G</creatorcontrib><creatorcontrib>de Koning-Ward, Tania F</creatorcontrib><creatorcontrib>Smith, Brian J</creatorcontrib><creatorcontrib>Papenfuss, Anthony T</creatorcontrib><creatorcontrib>Cowman, Alan F</creatorcontrib><creatorcontrib>Crabb, Brendan S</creatorcontrib><title>A newly discovered protein export machine in malaria parasites</title><title>Nature (London)</title><addtitle>Nature</addtitle><addtitle>Nature</addtitle><description>Several hundred malaria parasite proteins are exported beyond an encasing vacuole and into the cytosol of the host erythrocyte, a process that is central to the virulence and viability of the causative Plasmodium species. The trafficking machinery responsible for this export is unknown. Here we identify in Plasmodium falciparum a translocon of exported proteins (PTEX), which is located in the vacuole membrane. The PTEX complex is ATP-powered, and comprises heat shock protein 101 (HSP101; a ClpA/B-like ATPase from the AAA+ superfamily, of a type commonly associated with protein translocons), a novel protein termed PTEX150 and a known parasite protein, exported protein 2 (EXP2). EXP2 is the potential channel, as it is the membrane-associated component of the core PTEX complex. Two other proteins, a new protein PTEX88 and thioredoxin 2 (TRX2), were also identified as PTEX components. As a common portal for numerous crucial processes, this translocon offers a new avenue for therapeutic intervention. Malaria parasite virulence During intracellular infection of erythrocytes, malaria parasites reside in vacuoles from where they export many proteins into the host cell. These protein secretions play an important role in the virulence and viability of the Plasmodium parasite. The protein export machinery involved in this process has now been identified. Termed PTEX (for Plasmodium Translocon of EXported proteins), it is an ATP-powered complex located in the vacuole membrane, and may provide a new target for antimalarial drugs. Malaria parasites reside in vacuoles during intracellular infection of erythrocytes and export many proteins into the host cell, a process that is essential for the virulence and viability of Plasmodium . Whereas transport across the parasite membrane is known to rely on the secretory pathway, the transporter responsible for the translocation of proteins across the vacuole membrane is now identified.</description><subject>Amino acids</subject><subject>Analysis</subject><subject>Animals</subject><subject>Animals, Genetically Modified</subject><subject>Biological and medical sciences</subject><subject>Blood</subject><subject>Carrier proteins</subject><subject>Causes of</subject><subject>Cell adhesion &amp; migration</subject><subject>Erythrocytes</subject><subject>General aspects</subject><subject>Genetic aspects</subject><subject>Human protozoal diseases</subject><subject>Humanities and Social Sciences</subject><subject>Infectious diseases</subject><subject>Malaria</subject><subject>Malaria, Falciparum - parasitology</subject><subject>Medical sciences</subject><subject>Models, Biological</subject><subject>Mortality</subject><subject>multidisciplinary</subject><subject>Multiprotein Complexes - chemistry</subject><subject>Multiprotein Complexes - metabolism</subject><subject>Parasites</subject><subject>Parasitic diseases</subject><subject>Physiological aspects</subject><subject>Plasmodium falciparum</subject><subject>Plasmodium falciparum - metabolism</subject><subject>Protein Binding</subject><subject>Protein Transport</subject><subject>Proteins</subject><subject>Protozoal diseases</subject><subject>Protozoan Proteins - metabolism</subject><subject>Science</subject><subject>Translocation (Genetics)</subject><subject>Vector-borne diseases</subject><subject>Virulence (Microbiology)</subject><issn>0028-0836</issn><issn>1476-4687</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqV099r1TAUB_AiirtOn3yXqiiIdiZN0yQvg8vFH4OhoBMfy2l7es1o0y5p3fbfm9HLbq90XKUPhZNPvjmlOUHwlJIjSph8b6AfLBJJSXIvWNBEpFGSSnE_WBASy4hIlh4Ej5w7J4RwKpKHwQFVnKUxF4vgeBkavKyvw1K7ov2NFsuws22P2oR41bW2DxsofmmDoa80UIPVEHZgweke3ePgQQW1wyeb92Hw4-OHs9Xn6PTrp5PV8jQqJKd9xCRJOc1pmTNAKQmXALRSec4r9A0rwkqKvKRSgmAlV7IsE5CKxVJUKCFmh8HrMdf3djGg67PG94t1DQbbwWWpYFJIyvbCmCjGFZcevvgLnreDNf4jvEmSlCmqPHo5ojXUmGlTtb2F4iYxW6aMxCRNuPAqmlFrNGihbg1W2pf_28ck5v4fUb5tdccXnb7IpqF3omnS0QzyT4mNLmZb_acN0xPe7Gzwpserfg2Dc9nJ92-74fvsNPft3XZ59nP1ZTd5v57JLmzrnMUq66xuwF5nlGQ3I5ZNRszrZ5uLM-QNllu7mSkPXm0AuALqyoIptLt1MeWJEop69250zi-ZNdrtDZw_9_nIx-Jt3tT8AcPfPyU</recordid><startdate>20090618</startdate><enddate>20090618</enddate><creator>Lundie, Rachel J</creator><creator>Rug, Melanie</creator><creator>Sanders, Paul R</creator><creator>Boddey, Justin A</creator><creator>Gilson, Paul R</creator><creator>Maier, Alexander G</creator><creator>de Koning-Ward, Tania F</creator><creator>Smith, Brian J</creator><creator>Papenfuss, Anthony T</creator><creator>Cowman, Alan F</creator><creator>Crabb, Brendan S</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</general><scope>IQODW</scope><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>ATWCN</scope><scope>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7ST</scope><scope>7T5</scope><scope>7TG</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88G</scope><scope>88I</scope><scope>8AF</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BEC</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M2M</scope><scope>M2O</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>MBDVC</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PCBAR</scope><scope>PDBOC</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PSYQQ</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>Q9U</scope><scope>R05</scope><scope>RC3</scope><scope>S0X</scope><scope>SOI</scope><scope>F1W</scope><scope>H95</scope><scope>H97</scope><scope>L.G</scope><scope>7X8</scope></search><sort><creationdate>20090618</creationdate><title>A newly discovered protein export machine in malaria parasites</title><author>Lundie, Rachel J ; Rug, Melanie ; Sanders, Paul R ; Boddey, Justin A ; Gilson, Paul R ; Maier, Alexander G ; de Koning-Ward, Tania F ; Smith, Brian J ; Papenfuss, Anthony T ; Cowman, Alan F ; Crabb, Brendan S</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c851t-380651b1db3ae88058aa1f9bb5fe147903d1e5d188a73d598dd4a893287fe8a23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Amino acids</topic><topic>Analysis</topic><topic>Animals</topic><topic>Animals, Genetically Modified</topic><topic>Biological and medical sciences</topic><topic>Blood</topic><topic>Carrier proteins</topic><topic>Causes of</topic><topic>Cell adhesion &amp; migration</topic><topic>Erythrocytes</topic><topic>General aspects</topic><topic>Genetic aspects</topic><topic>Human protozoal diseases</topic><topic>Humanities and Social Sciences</topic><topic>Infectious diseases</topic><topic>Malaria</topic><topic>Malaria, Falciparum - parasitology</topic><topic>Medical sciences</topic><topic>Models, Biological</topic><topic>Mortality</topic><topic>multidisciplinary</topic><topic>Multiprotein Complexes - chemistry</topic><topic>Multiprotein Complexes - metabolism</topic><topic>Parasites</topic><topic>Parasitic diseases</topic><topic>Physiological aspects</topic><topic>Plasmodium falciparum</topic><topic>Plasmodium falciparum - metabolism</topic><topic>Protein Binding</topic><topic>Protein Transport</topic><topic>Proteins</topic><topic>Protozoal diseases</topic><topic>Protozoan Proteins - metabolism</topic><topic>Science</topic><topic>Translocation (Genetics)</topic><topic>Vector-borne diseases</topic><topic>Virulence (Microbiology)</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lundie, Rachel J</creatorcontrib><creatorcontrib>Rug, Melanie</creatorcontrib><creatorcontrib>Sanders, Paul R</creatorcontrib><creatorcontrib>Boddey, Justin A</creatorcontrib><creatorcontrib>Gilson, Paul R</creatorcontrib><creatorcontrib>Maier, Alexander G</creatorcontrib><creatorcontrib>de Koning-Ward, Tania F</creatorcontrib><creatorcontrib>Smith, Brian J</creatorcontrib><creatorcontrib>Papenfuss, Anthony T</creatorcontrib><creatorcontrib>Cowman, Alan F</creatorcontrib><creatorcontrib>Crabb, Brendan S</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Gale In Context: Middle School</collection><collection>ProQuest Central (Corporate)</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium &amp; Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Nursing &amp; Allied Health Database</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Environment Abstracts</collection><collection>Immunology Abstracts</collection><collection>Meteorological &amp; Geoastrophysical Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Agricultural Science Collection</collection><collection>Health &amp; Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Psychology Database (Alumni)</collection><collection>Science Database (Alumni Edition)</collection><collection>STEM Database</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>Materials Science &amp; Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>Advanced Technologies &amp; Aerospace Collection</collection><collection>Agricultural &amp; Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>eLibrary</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>Earth, Atmospheric &amp; Aquatic Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health &amp; Medical Complete (Alumni)</collection><collection>Materials Science Database</collection><collection>Nursing &amp; Allied Health Database (Alumni Edition)</collection><collection>Meteorological &amp; Geoastrophysical Abstracts - Academic</collection><collection>ProQuest Engineering Collection</collection><collection>ProQuest Biological Science Collection</collection><collection>Agricultural Science Database</collection><collection>Health &amp; Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Psychology Database</collection><collection>Research Library</collection><collection>Science Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Engineering Database</collection><collection>Research Library (Corporate)</collection><collection>Nursing &amp; Allied Health Premium</collection><collection>Advanced Technologies &amp; Aerospace Database</collection><collection>ProQuest Advanced Technologies &amp; Aerospace Collection</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Environmental Science Database</collection><collection>Earth, Atmospheric &amp; Aquatic Science Database</collection><collection>Materials Science Collection</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest One Psychology</collection><collection>Engineering Collection</collection><collection>Environmental Science Collection</collection><collection>ProQuest Central Basic</collection><collection>University of Michigan</collection><collection>Genetics Abstracts</collection><collection>SIRS Editorial</collection><collection>Environment Abstracts</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Aquatic Science &amp; Fisheries Abstracts (ASFA) 1: Biological Sciences &amp; Living Resources</collection><collection>Aquatic Science &amp; Fisheries Abstracts (ASFA) 3: Aquatic Pollution &amp; Environmental Quality</collection><collection>Aquatic Science &amp; Fisheries Abstracts (ASFA) Professional</collection><collection>MEDLINE - Academic</collection><jtitle>Nature (London)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lundie, Rachel J</au><au>Rug, Melanie</au><au>Sanders, Paul R</au><au>Boddey, Justin A</au><au>Gilson, Paul R</au><au>Maier, Alexander G</au><au>de Koning-Ward, Tania F</au><au>Smith, Brian J</au><au>Papenfuss, Anthony T</au><au>Cowman, Alan F</au><au>Crabb, Brendan S</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A newly discovered protein export machine in malaria parasites</atitle><jtitle>Nature (London)</jtitle><stitle>Nature</stitle><addtitle>Nature</addtitle><date>2009-06-18</date><risdate>2009</risdate><volume>459</volume><issue>7249</issue><spage>945</spage><epage>949</epage><pages>945-949</pages><issn>0028-0836</issn><eissn>1476-4687</eissn><coden>NATUAS</coden><abstract>Several hundred malaria parasite proteins are exported beyond an encasing vacuole and into the cytosol of the host erythrocyte, a process that is central to the virulence and viability of the causative Plasmodium species. The trafficking machinery responsible for this export is unknown. Here we identify in Plasmodium falciparum a translocon of exported proteins (PTEX), which is located in the vacuole membrane. The PTEX complex is ATP-powered, and comprises heat shock protein 101 (HSP101; a ClpA/B-like ATPase from the AAA+ superfamily, of a type commonly associated with protein translocons), a novel protein termed PTEX150 and a known parasite protein, exported protein 2 (EXP2). EXP2 is the potential channel, as it is the membrane-associated component of the core PTEX complex. Two other proteins, a new protein PTEX88 and thioredoxin 2 (TRX2), were also identified as PTEX components. As a common portal for numerous crucial processes, this translocon offers a new avenue for therapeutic intervention. Malaria parasite virulence During intracellular infection of erythrocytes, malaria parasites reside in vacuoles from where they export many proteins into the host cell. These protein secretions play an important role in the virulence and viability of the Plasmodium parasite. The protein export machinery involved in this process has now been identified. Termed PTEX (for Plasmodium Translocon of EXported proteins), it is an ATP-powered complex located in the vacuole membrane, and may provide a new target for antimalarial drugs. Malaria parasites reside in vacuoles during intracellular infection of erythrocytes and export many proteins into the host cell, a process that is essential for the virulence and viability of Plasmodium . Whereas transport across the parasite membrane is known to rely on the secretory pathway, the transporter responsible for the translocation of proteins across the vacuole membrane is now identified.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>19536257</pmid><doi>10.1038/nature08104</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 0028-0836
ispartof Nature (London), 2009-06, Vol.459 (7249), p.945-949
issn 0028-0836
1476-4687
language eng
recordid cdi_proquest_miscellaneous_67387813
source MEDLINE; Nature Journals Online; Alma/SFX Local Collection
subjects Amino acids
Analysis
Animals
Animals, Genetically Modified
Biological and medical sciences
Blood
Carrier proteins
Causes of
Cell adhesion & migration
Erythrocytes
General aspects
Genetic aspects
Human protozoal diseases
Humanities and Social Sciences
Infectious diseases
Malaria
Malaria, Falciparum - parasitology
Medical sciences
Models, Biological
Mortality
multidisciplinary
Multiprotein Complexes - chemistry
Multiprotein Complexes - metabolism
Parasites
Parasitic diseases
Physiological aspects
Plasmodium falciparum
Plasmodium falciparum - metabolism
Protein Binding
Protein Transport
Proteins
Protozoal diseases
Protozoan Proteins - metabolism
Science
Translocation (Genetics)
Vector-borne diseases
Virulence (Microbiology)
title A newly discovered protein export machine in malaria parasites
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-25T18%3A54%3A41IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_proqu&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=A%20newly%20discovered%20protein%20export%20machine%20in%20malaria%20parasites&rft.jtitle=Nature%20(London)&rft.au=Lundie,%20Rachel%20J&rft.date=2009-06-18&rft.volume=459&rft.issue=7249&rft.spage=945&rft.epage=949&rft.pages=945-949&rft.issn=0028-0836&rft.eissn=1476-4687&rft.coden=NATUAS&rft_id=info:doi/10.1038/nature08104&rft_dat=%3Cgale_proqu%3EA630206457%3C/gale_proqu%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=204463919&rft_id=info:pmid/19536257&rft_galeid=A630206457&rfr_iscdi=true