Trafficking of the exported P. falciparum chaperone PfHsp70x.
Identifieur interne : 001629 ( PubMed/Curation ); précédent : 001628; suivant : 001630Trafficking of the exported P. falciparum chaperone PfHsp70x.
Auteurs : Manuel Rhiel [Allemagne] ; Verena Bittl [Allemagne] ; Anke Tribensky [Allemagne] ; Sarah C. Charnaud [Australie] ; Maja Strecker [Allemagne] ; Sebastian Müller [Allemagne] ; Michael Lanzer [Allemagne] ; Cecilia Sanchez [Allemagne] ; Christine Schaeffer-Reiss [France] ; Benoit Westermann [France] ; Brendan S. Crabb [Australie] ; Paul R. Gilson [Australie] ; Simone Külzer [Allemagne] ; Jude M. Przyborski [Allemagne]Source :
- Scientific reports [ 2045-2322 ] ; 2016.
Abstract
Plasmodium falciparum extensively modifies its chosen host cell, the mature human erythrocyte. This remodelling is carried out by parasite-encoded proteins that are exported into the host cell. To gain access to the human red blood cell, these proteins must cross the parasitophorous vacuole, a membrane bound compartment surrounding the parasite that is generated during the invasion process. Many exported proteins carry a so-called PEXEL/HT signal that directs their transport. We recently reported the unexpected finding of a species-restricted parasite-encoded Hsp70, termed PfHsp70x, which is exported into the host erythrocyte cytosol. PfHsp70x lacks a classical PEXEL/HT motif, and its transport appears to be mediated by a 7 amino acid motif directly following the hydrophobic N-terminal secretory signal. In this report, we analyse this short targeting sequence in detail. Surprisingly, both a reversed and scrambled version of the motif retained the capacity to confer protein export. Site directed mutagenesis of glutamate residues within this region leads to a block of protein trafficking within the lumen of the PV. In contrast to PEXEL-containing proteins, the targeting signal is not cleaved, but appears to be acetylated. Furthermore we show that, like other exported proteins, trafficking of PfHsp70x requires the vacuolar translocon, PTEX.
DOI: 10.1038/srep36174
PubMed: 27824087
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Charnaud</name><affiliation wicri:level="1"><nlm:affiliation>Burnet Institute, Melbourne, Vic. 3004, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Burnet Institute, Melbourne, Vic. 3004</wicri:regionArea></affiliation></author><author><name sortKey="Strecker, Maja" sort="Strecker, Maja" uniqKey="Strecker M" first="Maja" last="Strecker">Maja Strecker</name><affiliation wicri:level="1"><nlm:affiliation>Parasitology, FB Biology, Philipps University Marburg, Karl von Frisch Strasse 8, 35043 Marburg, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Parasitology, FB Biology, Philipps University Marburg, Karl von Frisch Strasse 8, 35043 Marburg</wicri:regionArea></affiliation></author><author><name sortKey="Muller, Sebastian" sort="Muller, Sebastian" uniqKey="Muller S" first="Sebastian" last="Müller">Sebastian Müller</name><affiliation wicri:level="1"><nlm:affiliation>Parasitology, FB Biology, Philipps University Marburg, Karl von Frisch Strasse 8, 35043 Marburg, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Parasitology, FB Biology, Philipps University Marburg, Karl von Frisch Strasse 8, 35043 Marburg</wicri:regionArea></affiliation></author><author><name sortKey="Lanzer, Michael" sort="Lanzer, Michael" uniqKey="Lanzer M" first="Michael" last="Lanzer">Michael Lanzer</name><affiliation wicri:level="1"><nlm:affiliation>Zentrum für Infektiologie, Parasitologie, Im Neuenheimer Feld 324, 69120 Heidelberg, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Zentrum für Infektiologie, Parasitologie, Im Neuenheimer Feld 324, 69120 Heidelberg</wicri:regionArea></affiliation></author><author><name sortKey="Sanchez, Cecilia" sort="Sanchez, Cecilia" uniqKey="Sanchez C" first="Cecilia" last="Sanchez">Cecilia Sanchez</name><affiliation wicri:level="1"><nlm:affiliation>Zentrum für Infektiologie, Parasitologie, Im Neuenheimer Feld 324, 69120 Heidelberg, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Zentrum für Infektiologie, Parasitologie, Im Neuenheimer Feld 324, 69120 Heidelberg</wicri:regionArea></affiliation></author><author><name sortKey="Schaeffer Reiss, Christine" sort="Schaeffer Reiss, Christine" uniqKey="Schaeffer Reiss C" first="Christine" last="Schaeffer-Reiss">Christine Schaeffer-Reiss</name><affiliation wicri:level="1"><nlm:affiliation>Laboratoire de Spectrométrie de Masse BioOrganique (LSMBO), IPHC, Université de Strasbourg, CNRS, UMR 7178, Strasbourg, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Laboratoire de Spectrométrie de Masse BioOrganique (LSMBO), IPHC, Université de Strasbourg, CNRS, UMR 7178, Strasbourg</wicri:regionArea></affiliation></author><author><name sortKey="Westermann, Benoit" sort="Westermann, Benoit" uniqKey="Westermann B" first="Benoit" last="Westermann">Benoit Westermann</name><affiliation wicri:level="1"><nlm:affiliation>Laboratoire de Spectrométrie de Masse BioOrganique (LSMBO), IPHC, Université de Strasbourg, CNRS, UMR 7178, Strasbourg, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Laboratoire de Spectrométrie de Masse BioOrganique (LSMBO), IPHC, Université de Strasbourg, CNRS, UMR 7178, Strasbourg</wicri:regionArea></affiliation></author><author><name sortKey="Crabb, Brendan S" sort="Crabb, Brendan S" uniqKey="Crabb B" first="Brendan S" last="Crabb">Brendan S. Crabb</name><affiliation wicri:level="1"><nlm:affiliation>Burnet Institute, Melbourne, Vic. 3004, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Burnet Institute, Melbourne, Vic. 3004</wicri:regionArea></affiliation></author><author><name sortKey="Gilson, Paul R" sort="Gilson, Paul R" uniqKey="Gilson P" first="Paul R" last="Gilson">Paul R. Gilson</name><affiliation wicri:level="1"><nlm:affiliation>Burnet Institute, Melbourne, Vic. 3004, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Burnet Institute, Melbourne, Vic. 3004</wicri:regionArea></affiliation></author><author><name sortKey="Kulzer, Simone" sort="Kulzer, Simone" uniqKey="Kulzer S" first="Simone" last="Külzer">Simone Külzer</name><affiliation wicri:level="1"><nlm:affiliation>Parasitology, FB Biology, Philipps University Marburg, Karl von Frisch Strasse 8, 35043 Marburg, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Parasitology, FB Biology, Philipps University Marburg, Karl von Frisch Strasse 8, 35043 Marburg</wicri:regionArea></affiliation></author><author><name sortKey="Przyborski, Jude M" sort="Przyborski, Jude M" uniqKey="Przyborski J" first="Jude M" last="Przyborski">Jude M. Przyborski</name><affiliation wicri:level="1"><nlm:affiliation>Parasitology, FB Biology, Philipps University Marburg, Karl von Frisch Strasse 8, 35043 Marburg, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Parasitology, FB Biology, Philipps University Marburg, Karl von Frisch Strasse 8, 35043 Marburg</wicri:regionArea></affiliation></author></analytic><series><title level="j">Scientific reports</title><idno type="eISSN">2045-2322</idno><imprint><date when="2016" type="published">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Plasmodium falciparum extensively modifies its chosen host cell, the mature human erythrocyte. This remodelling is carried out by parasite-encoded proteins that are exported into the host cell. To gain access to the human red blood cell, these proteins must cross the parasitophorous vacuole, a membrane bound compartment surrounding the parasite that is generated during the invasion process. Many exported proteins carry a so-called PEXEL/HT signal that directs their transport. We recently reported the unexpected finding of a species-restricted parasite-encoded Hsp70, termed PfHsp70x, which is exported into the host erythrocyte cytosol. PfHsp70x lacks a classical PEXEL/HT motif, and its transport appears to be mediated by a 7 amino acid motif directly following the hydrophobic N-terminal secretory signal. In this report, we analyse this short targeting sequence in detail. Surprisingly, both a reversed and scrambled version of the motif retained the capacity to confer protein export. Site directed mutagenesis of glutamate residues within this region leads to a block of protein trafficking within the lumen of the PV. In contrast to PEXEL-containing proteins, the targeting signal is not cleaved, but appears to be acetylated. Furthermore we show that, like other exported proteins, trafficking of PfHsp70x requires the vacuolar translocon, PTEX.</div></front></TEI><pubmed><MedlineCitation Status="In-Data-Review" Owner="NLM"><PMID Version="1">27824087</PMID><DateCreated><Year>2016</Year><Month>11</Month><Day>08</Day></DateCreated><DateRevised><Year>2017</Year><Month>02</Month><Day>20</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">2045-2322</ISSN><JournalIssue CitedMedium="Internet"><Volume>6</Volume><PubDate><Year>2016</Year><Month>Nov</Month><Day>08</Day></PubDate></JournalIssue><Title>Scientific reports</Title><ISOAbbreviation>Sci Rep</ISOAbbreviation></Journal><ArticleTitle>Trafficking of the exported P. falciparum chaperone PfHsp70x.</ArticleTitle><Pagination><MedlinePgn>36174</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1038/srep36174</ELocationID><Abstract><AbstractText>Plasmodium falciparum extensively modifies its chosen host cell, the mature human erythrocyte. This remodelling is carried out by parasite-encoded proteins that are exported into the host cell. To gain access to the human red blood cell, these proteins must cross the parasitophorous vacuole, a membrane bound compartment surrounding the parasite that is generated during the invasion process. Many exported proteins carry a so-called PEXEL/HT signal that directs their transport. We recently reported the unexpected finding of a species-restricted parasite-encoded Hsp70, termed PfHsp70x, which is exported into the host erythrocyte cytosol. PfHsp70x lacks a classical PEXEL/HT motif, and its transport appears to be mediated by a 7 amino acid motif directly following the hydrophobic N-terminal secretory signal. In this report, we analyse this short targeting sequence in detail. Surprisingly, both a reversed and scrambled version of the motif retained the capacity to confer protein export. Site directed mutagenesis of glutamate residues within this region leads to a block of protein trafficking within the lumen of the PV. In contrast to PEXEL-containing proteins, the targeting signal is not cleaved, but appears to be acetylated. Furthermore we show that, like other exported proteins, trafficking of PfHsp70x requires the vacuolar translocon, PTEX.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Rhiel</LastName><ForeName>Manuel</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Parasitology, FB Biology, Philipps University Marburg, Karl von Frisch Strasse 8, 35043 Marburg, Germany.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Biochemistry Center (BZH), University of Heidelberg, Im Neuenheimer Feld 328, 69120 Heidelberg, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bittl</LastName><ForeName>Verena</ForeName><Initials>V</Initials><AffiliationInfo><Affiliation>Parasitology, FB Biology, Philipps University Marburg, Karl von Frisch Strasse 8, 35043 Marburg, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Tribensky</LastName><ForeName>Anke</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Parasitology, FB Biology, Philipps University Marburg, Karl von Frisch Strasse 8, 35043 Marburg, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Charnaud</LastName><ForeName>Sarah C</ForeName><Initials>SC</Initials><AffiliationInfo><Affiliation>Burnet Institute, Melbourne, Vic. 3004, Australia.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Monash University, Melbourne, Vic. 3800, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Strecker</LastName><ForeName>Maja</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Parasitology, FB Biology, Philipps University Marburg, Karl von Frisch Strasse 8, 35043 Marburg, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Müller</LastName><ForeName>Sebastian</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Parasitology, FB Biology, Philipps University Marburg, Karl von Frisch Strasse 8, 35043 Marburg, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lanzer</LastName><ForeName>Michael</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Zentrum für Infektiologie, Parasitologie, Im Neuenheimer Feld 324, 69120 Heidelberg, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sanchez</LastName><ForeName>Cecilia</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Zentrum für Infektiologie, Parasitologie, Im Neuenheimer Feld 324, 69120 Heidelberg, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Schaeffer-Reiss</LastName><ForeName>Christine</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Laboratoire de Spectrométrie de Masse BioOrganique (LSMBO), IPHC, Université de Strasbourg, CNRS, UMR 7178, Strasbourg, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Westermann</LastName><ForeName>Benoit</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>Laboratoire de Spectrométrie de Masse BioOrganique (LSMBO), IPHC, Université de Strasbourg, CNRS, UMR 7178, Strasbourg, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Crabb</LastName><ForeName>Brendan S</ForeName><Initials>BS</Initials><AffiliationInfo><Affiliation>Burnet Institute, Melbourne, Vic. 3004, Australia.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Monash University, Melbourne, Vic. 3800, Australia.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>University of Melbourne, Melbourne, Vic. 3010, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Gilson</LastName><ForeName>Paul R</ForeName><Initials>PR</Initials><AffiliationInfo><Affiliation>Burnet Institute, Melbourne, Vic. 3004, Australia.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Monash University, Melbourne, Vic. 3800, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Külzer</LastName><ForeName>Simone</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Parasitology, FB Biology, Philipps University Marburg, Karl von Frisch Strasse 8, 35043 Marburg, Germany.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Research School of Biology, ANU, Acton, ACT 2601, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Przyborski</LastName><ForeName>Jude M</ForeName><Initials>JM</Initials><AffiliationInfo><Affiliation>Parasitology, FB Biology, Philipps University Marburg, Karl von Frisch Strasse 8, 35043 Marburg, Germany.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal 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