Exoerythrocytic Plasmodium Parasites Secrete a Cysteine Protease Inhibitor Involved in Sporozoite Invasion and Capable of Blocking Cell Death of Host Hepatocytes
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{"title"=>"Exoerythrocytic Plasmodium parasites secrete a cysteine protease inhibitor involved in sporozoite invasion and capable of blocking cell death of host hepatocytes", "type"=>"journal", "authors"=>[{"first_name"=>"Annika", "last_name"=>"Rennenberg", "scopus_author_id"=>"14421585100"}, {"first_name"=>"Christine", "last_name"=>"Lehmann", "scopus_author_id"=>"57197889836"}, {"first_name"=>"Anna", "last_name"=>"Heitmann", "scopus_author_id"=>"36086221800"}, {"first_name"=>"Tina", "last_name"=>"Witt", "scopus_author_id"=>"26655105500"}, {"first_name"=>"Guido", "last_name"=>"Hansen", "scopus_author_id"=>"22940492900"}, {"first_name"=>"Krishna", "last_name"=>"Nagarajan", "scopus_author_id"=>"14622005000"}, {"first_name"=>"Christina", "last_name"=>"Deschermeier", "scopus_author_id"=>"6506821464"}, {"first_name"=>"Vito", "last_name"=>"Turk", "scopus_author_id"=>"7007025347"}, {"first_name"=>"Rolf", "last_name"=>"Hilgenfeld", "scopus_author_id"=>"7006843618"}, {"first_name"=>"Volker T.", "last_name"=>"Heussler", "scopus_author_id"=>"6701790107"}], "year"=>2010, "source"=>"PLoS Pathogens", "identifiers"=>{"issn"=>"15537366", "isbn"=>"1553-7374 (Electronic)\\n1553-7366 (Linking)", "pui"=>"358569007", "sgr"=>"77950374423", "doi"=>"10.1371/journal.ppat.1000825", "scopus"=>"2-s2.0-77950374423", "pmid"=>"20361051"}, "id"=>"c6eb72f3-0e31-37b3-94b6-b18fdf18c397", "abstract"=>"Plasmodium parasites must control cysteine protease activity that is critical for hepatocyte invasion by sporozoites, liver stage development, host cell survival and merozoite liberation. Here we show that exoerythrocytic P. berghei parasites express a potent cysteine protease inhibitor (PbICP, P. berghei inhibitor of cysteine proteases). We provide evidence that it has an important function in sporozoite invasion and is capable of blocking hepatocyte cell death. Pre-incubation with specific anti-PbICP antiserum significantly decreased the ability of sporozoites to infect hepatocytes and expression of PbICP in mammalian cells protects them against peroxide- and camptothecin-induced cell death. PbICP is secreted by sporozoites prior to and after hepatocyte invasion, localizes to the parasitophorous vacuole as well as to the parasite cytoplasm in the schizont stage and is released into the host cell cytoplasm at the end of the liver stage. Like its homolog falstatin/PfICP in P. falciparum, PbICP consists of a classical N-terminal signal peptide, a long N-terminal extension region and a chagasin-like C-terminal domain. In exoerythrocytic parasites, PbICP is posttranslationally processed, leading to liberation of the C-terminal chagasin-like domain. Biochemical analysis has revealed that both full-length PbICP and the truncated C-terminal domain are very potent inhibitors of cathepsin L-like host and parasite cysteine proteases. The results presented in this study suggest that the inhibitor plays an important role in sporozoite invasion of host cells and in parasite survival during liver stage development by inhibiting host cell proteases involved in programmed cell death.", "link"=>"http://www.mendeley.com/research/exoerythrocytic-plasmodium-parasites-secrete-cysteine-protease-inhibitor-involved-sporozoite-invasio", "reader_count"=>100, "reader_count_by_academic_status"=>{"Unspecified"=>2, "Professor > Associate Professor"=>1, "Researcher"=>27, "Student > Doctoral Student"=>4, "Student > Ph. D. Student"=>27, "Student > Postgraduate"=>5, "Student > Master"=>20, "Other"=>2, "Student > Bachelor"=>8, "Lecturer"=>1, "Professor"=>3}, "reader_count_by_user_role"=>{"Unspecified"=>2, "Professor > Associate Professor"=>1, "Researcher"=>27, "Student > Doctoral Student"=>4, "Student > Ph. D. Student"=>27, "Student > Postgraduate"=>5, "Student > Master"=>20, "Other"=>2, "Student > Bachelor"=>8, "Lecturer"=>1, "Professor"=>3}, "reader_count_by_subject_area"=>{"Unspecified"=>2, "Environmental Science"=>1, "Biochemistry, Genetics and Molecular Biology"=>10, "Agricultural and Biological Sciences"=>70, "Medicine and Dentistry"=>9, "Physics and Astronomy"=>2, "Chemistry"=>4, "Immunology and Microbiology"=>2}, "reader_count_by_subdiscipline"=>{"Medicine and Dentistry"=>{"Medicine and Dentistry"=>9}, "Chemistry"=>{"Chemistry"=>4}, "Physics and Astronomy"=>{"Physics and Astronomy"=>2}, "Immunology and Microbiology"=>{"Immunology and Microbiology"=>2}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>70}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>10}, "Unspecified"=>{"Unspecified"=>2}, "Environmental Science"=>{"Environmental Science"=>1}}, "reader_count_by_country"=>{"Colombia"=>1, "United States"=>2, "Brazil"=>1, "South Africa"=>1, "United Kingdom"=>2, "Kenya"=>1, "Portugal"=>1, "Switzerland"=>1, "Germany"=>2, "India"=>1}, "group_count"=>3}

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  • {"files"=>["https://ndownloader.figshare.com/files/426341", "https://ndownloader.figshare.com/files/426375", "https://ndownloader.figshare.com/files/426423", "https://ndownloader.figshare.com/files/426485", "https://ndownloader.figshare.com/files/426534", "https://ndownloader.figshare.com/files/426561", "https://ndownloader.figshare.com/files/426603", "https://ndownloader.figshare.com/files/426649", "https://ndownloader.figshare.com/files/426685", "https://ndownloader.figshare.com/files/426731", "https://ndownloader.figshare.com/files/426796", "https://ndownloader.figshare.com/files/426861", "https://ndownloader.figshare.com/files/426907", "https://ndownloader.figshare.com/files/426934"], "description"=>"<div><p><em>Plasmodium</em> parasites must control cysteine protease activity that is critical for hepatocyte invasion by sporozoites, liver stage development, host cell survival and merozoite liberation. Here we show that exoerythrocytic <em>P. berghei</em> parasites express a potent cysteine protease inhibitor (PbICP, <em>P. berghei</em> inhibitor of cysteine proteases). We provide evidence that it has an important function in sporozoite invasion and is capable of blocking hepatocyte cell death. Pre-incubation with specific anti-PbICP antiserum significantly decreased the ability of sporozoites to infect hepatocytes and expression of PbICP in mammalian cells protects them against peroxide- and camptothecin-induced cell death. PbICP is secreted by sporozoites prior to and after hepatocyte invasion, localizes to the parasitophorous vacuole as well as to the parasite cytoplasm in the schizont stage and is released into the host cell cytoplasm at the end of the liver stage. Like its homolog falstatin/PfICP in <em>P. falciparum</em>, PbICP consists of a classical N-terminal signal peptide, a long N-terminal extension region and a chagasin-like C-terminal domain. In exoerythrocytic parasites, PbICP is posttranslationally processed, leading to liberation of the C-terminal chagasin-like domain. Biochemical analysis has revealed that both full-length PbICP and the truncated C-terminal domain are very potent inhibitors of cathepsin L-like host and parasite cysteine proteases. The results presented in this study suggest that the inhibitor plays an important role in sporozoite invasion of host cells and in parasite survival during liver stage development by inhibiting host cell proteases involved in programmed cell death.</p></div>", "links"=>[], "tags"=>["exoerythrocytic", "parasites", "secrete", "cysteine", "protease", "inhibitor", "sporozoite", "blocking", "hepatocytes"], "article_id"=>144160, "categories"=>["Physics", "Cell Biology"], "users"=>["Annika Rennenberg", "Christine Lehmann", "Anna Heitmann", "Tina Witt", "Guido Hansen", "Krishna Nagarajan", "Christina Deschermeier", "Vito Turk", "Rolf Hilgenfeld", "Volker T. Heussler"], "doi"=>["https://dx.doi.org/10.1371/journal.ppat.1000825.s001", "https://dx.doi.org/10.1371/journal.ppat.1000825.s002", "https://dx.doi.org/10.1371/journal.ppat.1000825.s003", "https://dx.doi.org/10.1371/journal.ppat.1000825.s004", "https://dx.doi.org/10.1371/journal.ppat.1000825.s005", "https://dx.doi.org/10.1371/journal.ppat.1000825.s006", "https://dx.doi.org/10.1371/journal.ppat.1000825.s007", "https://dx.doi.org/10.1371/journal.ppat.1000825.s008", "https://dx.doi.org/10.1371/journal.ppat.1000825.s009", "https://dx.doi.org/10.1371/journal.ppat.1000825.s010", "https://dx.doi.org/10.1371/journal.ppat.1000825.s011", "https://dx.doi.org/10.1371/journal.ppat.1000825.s012", "https://dx.doi.org/10.1371/journal.ppat.1000825.s013", "https://dx.doi.org/10.1371/journal.ppat.1000825.s014"], "stats"=>{"downloads"=>54, "page_views"=>25, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/Exoerythrocytic_Plasmodium_Parasites_Secrete_a_Cysteine_Protease_Inhibitor_Involved_in_Sporozoite_Invasion_and_Capable_of_Blocking_Cell_Death_of_Host_Hepatocytes/144160", "title"=>"Exoerythrocytic <em>Plasmodium</em> Parasites Secrete a Cysteine Protease Inhibitor Involved in Sporozoite Invasion and Capable of Blocking Cell Death of Host Hepatocytes", "pos_in_sequence"=>0, "defined_type"=>4, "published_date"=>"2010-03-26 01:09:20"}
  • {"files"=>["https://ndownloader.figshare.com/files/857634"], "description"=>"<p>Substrate hydrolysis was measured in the presence of the control protein MBP (1 µM or 100 nM), in the presence of MBP-PbICP-C (1 µM), in the presence of MBP-PbICP-N (1 µM) or in the presence of PbICP-C (100 nM). Protease activity in the presence of 1 µM and 100 nM MBP, respectively was considered as 100% and the percentage of residual protease activity in the presence of the inhibitor was calculated.</p>", "links"=>[], "tags"=>["c-terminal", "n-terminal", "pbicp", "potent", "inhibitor", "cysteine", "proteases", "cathepsin"], "article_id"=>528077, "categories"=>["Physics", "Cell Biology"], "users"=>["Annika Rennenberg", "Christine Lehmann", "Anna Heitmann", "Tina Witt", "Guido Hansen", "Krishna Nagarajan", "Christina Deschermeier", "Vito Turk", "Rolf Hilgenfeld", "Volker T. Heussler"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1000825.t002", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_The_C_terminal_domain_but_not_the_N_terminal_domain_of_PbICP_is_a_potent_inhibitor_of_cysteine_proteases_except_cathepsin_B_/528077", "title"=>"The C-terminal domain but not the N-terminal domain of PbICP is a potent inhibitor of cysteine proteases except cathepsin B.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2010-03-26 02:14:37"}
  • {"files"=>["https://ndownloader.figshare.com/files/857543"], "description"=>"<p><b>1:</b> PbICP (green circles) is secreted by free gliding sporozoites and supports invasion of HepG2 cells. Intracellular sporozoites and trophozoites continue to express and partially secrete PbICP. Thus PbICP can potentially control parasite-derived cysteine proteases as well as host cell cysteine proteases. <b>2+3:</b> During schizogony, PbICP is predominately located in the PV and the parasite cytosol, suggesting that during this developmental phase, parasite cysteine proteases are the main target of the inhibitor. However, it cannot be excluded that small portions of the inhibitor, which are beyond the detection level for IFA, are still exported into the host cell cytoplasm. <b>4:</b> At the end of the liver stage, upon disruption of the PVM, a substantial amount of PbICP is passively released into the host cell cytoplasm. At this stage, the main function of PbICP might be inhibition of host cell cysteine proteases to allow a slow and ordered host cell death and merosome formation.</p>", "links"=>[], "tags"=>["pbicp", "exoerythrocytic", "berghei"], "article_id"=>527995, "categories"=>["Physics", "Cell Biology"], "users"=>["Annika Rennenberg", "Christine Lehmann", "Anna Heitmann", "Tina Witt", "Guido Hansen", "Krishna Nagarajan", "Christina Deschermeier", "Vito Turk", "Rolf Hilgenfeld", "Volker T. Heussler"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1000825.g009", "stats"=>{"downloads"=>0, "page_views"=>1, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Possible_roles_of_PbICP_during_the_exoerythrocytic_development_of_P_berghei_in_vitro_/527995", "title"=>"Possible roles of PbICP during the exoerythrocytic development of <i>P. berghei in vitro</i>.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2010-03-26 02:13:15"}
  • {"files"=>["https://ndownloader.figshare.com/files/857111"], "description"=>"<p>(<b>A</b>) Domain-specific western blot analysis of protein extracts prepared from <i>P. berghei</i> salivary gland sporozoites and blood stage schizonts. Protein extracts of blood stage schizonts (two independent samples: one in lane 2 and a second one in lane 3+4) and sporozoites were separated by SDS-PAGE and blotted on nitrocellulose filters. Filters were then probed with antisera against the chagasin-like domain of PbICP (anti-PbICP-C, rabbit, lane 1–3) or the N-terminal domain (anti-PbICP-N, lane 4). Anti-PbICP-C antiserum detected the full-length inhibitor (55 kDa) as well as the processed form after cleavage of the N-terminal extension domain (23 kDa), whereas anti-PbICP-N antiserum detected only the full-length protein of 55 kDa. (<b>B</b>) IFA of a <i>P. berghei</i>-infected HepG2 cell 48 hpi (widefield deconvolution). Infected cells were fixed and stained with anti-PbICP-N antiserum (mouse, red) and antiserum against PbICP-C (rabbit, green). DNA was stained with DAPI (blue). The images were deconvoluted to remove out-of-focus signals. (<b>C</b>) Schematic illustration of the transfection plasmid pL0017-<i>pbicp-gfp</i> for constitutive strong expression of PbICP. The <i>pbicp-gfpm3</i> coding region (ss, signal sequence of <i>pbicp</i>) is under the control of the strong constitutive <i>pbeef1aa</i> promotor. The vector confers ampicillin resistance (amp+) in <i>E. coli</i> and pyrimethamine resistance (pyr+) in transfected <i>P. berghei</i> parasites. Following transfection, <i>P. berghei</i> parasites constitutively express the fusion protein. The expected <i>in gel</i> sizes of the GFP-tagged full-length PbICP and the GFP-tagged processed form of the inhibitor were calculated and are presented. (<b>D</b>) Anti-GFP western blot analysis of GFP-PbICP-expressing <i>P. berghei</i> blood stage extracts, sporozoite total lysates, infected HepG2 cell total lysates (60 hours after infection) and detached infected HepG2 cells/merosomes. Uninfected HepG2 cells served as a specificity control and reprobing with anti-tubulin antiserum served as a loading control for protein extracts of infected and uninfected HepG2 cells. The anti-GFP antiserum detected proteins that correspond to the size of the full-length GFP-tagged inhibitor (81 kDa) as well as the processed form after cleavage of the N-terminal extension domain (49 kDa).</p>", "links"=>[], "tags"=>["posttranslationally", "processed", "exoerythrocytic"], "article_id"=>527564, "categories"=>["Physics", "Cell Biology"], "users"=>["Annika Rennenberg", "Christine Lehmann", "Anna Heitmann", "Tina Witt", "Guido Hansen", "Krishna Nagarajan", "Christina Deschermeier", "Vito Turk", "Rolf Hilgenfeld", "Volker T. Heussler"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1000825.g005", "stats"=>{"downloads"=>0, "page_views"=>7, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_PbICP_is_posttranslationally_processed_in_the_blood_stage_and_exoerythrocytic_stages_/527564", "title"=>"PbICP is posttranslationally processed in the blood stage and exoerythrocytic stages.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2010-03-26 02:06:04"}
  • {"files"=>["https://ndownloader.figshare.com/files/857333"], "description"=>"<p>(<b>A</b>) <i>Transmigration assay: P. berghei</i> sporozoites were pre-incubated with medium (no serum) preimmune serum (1∶5), anti-PbICP-C antiserum (1∶5) or anti-CSP-antiserum (1∶5) and subsequently added to HepG2 cells in the presence of 1 mM dextran-fluorescein for 1 h to stain wounded cells. Non-infected HepG2 cells (n.i.) cultivated in the presence of 1 mM dextran-fluorescein for 1 h served as a negative control for cell wounding. After this incubation period cells were washed, fixed and the DNA was stained with DAPI to allow visualization of both intact and wounded cells. The total cell number compared to dextran-fluorescein positive cells was determined using an immunofluorescence microscope and the percentage of dextran-fluorescein positive cells was calculated. Presented are the means and standard deviations of three independent experiments. The image presented shows a number of cells, whose nuclei are stained with DAPI. Transmigrated cells are additionally stained with dextran-fluorescein (green). (<b>B</b>) Invasion assay: <i>P. berghei</i> sporozoites expressing mCherry were pre-incubated with preimmune serum (1∶5), anti-PbICP-C antiserum (1∶5) or anti-CSP-antiserum (1∶5) and subsequently added to HepG2 cells. After 1 h, cells were fixed but not permeabilized and stained with an anti-CSP antiserum (inside/outside assay). All sporozoites can be detected by their mCherry expression but only extracellular sporozoites are additionally stained by the anti-CSP antiserum. DNA was stained with DAPI (blue). Free and intracellular sporozoites were counted and the percentage was calculated. Presented are the means and standard deviations of three independent experiments. Typical examples of intracellular and extracellular parasites are presented in the image next to the graph. mCherry expression can be seen in all sporozoites but additional CSP staining (green) is visible only in extracellualr parasites. (<b>C</b>) Parasite development following PbICP neutralization of sporozoites: HepG2 cell infection was performed as described in (B). Serum dilutions (1∶5 to 1∶50) used to pre-incubate sporozoites are indicated. Infected cells were fixed 30 hpi and stained with anti-Exp1 antiserum (chicken, green) and anti-PbICP-C antiserum (rabbit, red) (image shows a typical example of a infected cell 30 hpi stained as described). Infected cells in the individual wells were counted and the percentage of infected cells after treatment was calculated from three independent experiments. The number of infected cells in wells infected with sporozoites that had been exposed to a 1∶10 dilution of the preimmune serum, was considered as 100%. As in the CSP-control, pre-incubation with anti-PbICP-antiserum significantly reduced the infectivity of sporozoites.</p>", "links"=>[], "tags"=>["neutralization", "pbicp", "infectivity", "sporozoites", "inhibit", "traversal"], "article_id"=>527779, "categories"=>["Physics", "Cell Biology"], "users"=>["Annika Rennenberg", "Christine Lehmann", "Anna Heitmann", "Tina Witt", "Guido Hansen", "Krishna Nagarajan", "Christina Deschermeier", "Vito Turk", "Rolf Hilgenfeld", "Volker T. Heussler"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1000825.g007", "stats"=>{"downloads"=>0, "page_views"=>4, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Antibody_mediated_neutralization_of_PbICP_reduces_infectivity_of_sporozoites_in_vitro_but_does_not_inhibit_cell_traversal_of_sporozoites_/527779", "title"=>"Antibody-mediated neutralization of PbICP reduces infectivity of sporozoites <i>in vitro</i> but does not inhibit cell traversal of sporozoites.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2010-03-26 02:09:39"}
  • {"files"=>["https://ndownloader.figshare.com/files/856621"], "description"=>"<p>(<b>A</b>) Recombinant PbICP inhibits papain activity. Recombinant PbICP was produced in <i>E. coli</i> as an MBP-tagged soluble protein and purified from the bacterial lysate by amylose-bead affinity chromatography (insert, lane 1). The MBP tag was cleaved off by factor Xa digestion (insert, lane 2) and PbICP was purified using a MonoQ column (insert, lane 3). Proteins were resolved by SDS-PAGE and stained with Coomassie Blue. Hydrolysis of the substrate Z-Phe-Arg-pNA by papain was measured in the presence of 100 nM of the control protein MBP or 100 nM of MBP-PbICP, factor Xa-cleaved MBP-PbICP or PbICP after tag cleavage and MonoQ purification. Protease activity in presence of 100 nM MBP was considered 100% and the percentage of residual protease activity was calculated from that. MBP: maltose binding protein. (<b>B</b>) Constitutive transcription of the <i>pbicp</i> gene. RNA was isolated from <i>P. berghei</i>-infected mouse blood, mosquito midgut and salivary glands and from infected HepG2 cells. The purified RNA was then used for a duplex RT-PCR with specific primer pairs for the amplification of <i>pbicp</i> cDNA and the <i>tubulin</i> cDNA of <i>P. berghei</i>. In samples with odd numbers, cDNA was used as a template. In samples with even numbers, reverse transcriptase was omitted from the cDNA preparation reaction to control for the presence of genomic DNA.</p>", "links"=>[], "tags"=>["potent", "inhibitor", "c1", "cysteine", "proteases", "constitutively"], "article_id"=>527067, "categories"=>["Physics", "Cell Biology"], "users"=>["Annika Rennenberg", "Christine Lehmann", "Anna Heitmann", "Tina Witt", "Guido Hansen", "Krishna Nagarajan", "Christina Deschermeier", "Vito Turk", "Rolf Hilgenfeld", "Volker T. Heussler"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1000825.g001", "stats"=>{"downloads"=>2, "page_views"=>4, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_PbICP_is_a_potent_inhibitor_of_C1_cysteine_proteases_and_the_pbicp_gene_is_constitutively_transcribed_/527067", "title"=>"PbICP is a potent inhibitor of C1 cysteine proteases and the <i>pbicp</i> gene is constitutively transcribed.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2010-03-26 01:57:47"}
  • {"files"=>["https://ndownloader.figshare.com/files/856865"], "description"=>"<p>(<b>A</b>) Confocal IFA of an extracellular <i>P. berghei</i> sporozoite in the presence of HepG2 cells. HepG2 cells were co-cultivated for 1 h with sporozoites, fixed and stained with an anti-TRAP antiserum (mouse, green) and a polyclonal antiserum against PbICP-C (rabbit, red). DNA was stained with DAPI (blue). (<b>B</b>) Double-stained IEM of a salivary gland sporozoite shows partial co-localization of TRAP and PbICP in vesicles (marked with asterisk). <i>P. berghei</i>-infected <i>A. stephensi</i> salivary glands were fixed 25 days after infection and prepared for IEM. Ultrathin sections were stained with PbICP-C (rabbit, 25 nm gold particles) and anti-TRAP (mouse, 10 nm gold particles). The sections were contrasted with uranyl acetate and lead citrate.</p>", "links"=>[], "tags"=>["colocalizes", "apical", "vesicles"], "article_id"=>527312, "categories"=>["Physics", "Cell Biology"], "users"=>["Annika Rennenberg", "Christine Lehmann", "Anna Heitmann", "Tina Witt", "Guido Hansen", "Krishna Nagarajan", "Christina Deschermeier", "Vito Turk", "Rolf Hilgenfeld", "Volker T. Heussler"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1000825.g003", "stats"=>{"downloads"=>0, "page_views"=>5, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_PbICP_partially_colocalizes_with_TRAP_at_the_apical_pole_and_in_vesicles_of_sporozoites_/527312", "title"=>"PbICP partially colocalizes with TRAP at the apical pole and in vesicles of sporozoites.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2010-03-26 02:01:52"}
  • {"files"=>["https://ndownloader.figshare.com/files/857209"], "description"=>"<p>(<b>A</b>) Purification of recombinant PbICP, PbICP-C and -N. Like the full-length protein, recombinant PbICP-C and -N were expressed in <i>E. coli</i> as MBP-tagged soluble proteins and purified from the bacterial total lysate by amylose-bead affinity chromatography (lane 1, 2, 3). The proteins were resolved by SDS-PAGE and stained with Coomassie Blue. (<b>B</b>) Recombinant PbICP-C inhibits the cysteine protease cathepsin L to a similar extent as full-length PbICP, whereas PbICP-N does not block cathepsin L activity. Hydrolysis of the substrate Z-FR-pNA by cathepsin L was measured in the presence of 1 µM MBP-PbICP-N, MBP-PbICP or MBP-PbICP-C or the control protein MBP.</p>", "links"=>[], "tags"=>["c-terminal", "pbicp", "inhibitor"], "article_id"=>527659, "categories"=>["Physics", "Cell Biology"], "users"=>["Annika Rennenberg", "Christine Lehmann", "Anna Heitmann", "Tina Witt", "Guido Hansen", "Krishna Nagarajan", "Christina Deschermeier", "Vito Turk", "Rolf Hilgenfeld", "Volker T. Heussler"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1000825.g006", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_The_C_terminal_domain_of_PbICP_is_necessary_and_sufficient_for_the_inhibitor_function_/527659", "title"=>"The C-terminal domain of PbICP is necessary and sufficient for the inhibitor function.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2010-03-26 02:07:39"}
  • {"files"=>["https://ndownloader.figshare.com/files/856993"], "description"=>"<p>Wide-field IFA of HepG2 cells infected with <i>P. berghei</i>-expressing mCherry in the cytoplasm (<b>A</b>) or wildtype <i>P. berghei</i> (<b>B-F</b>) at different time points after infection (hpi, hours post infection). Infected cells were fixed, incubated with anti-CSP antiserum (mouse, red) (<b>B</b>) or with anti-ExpI antiserum (chicken, red) (<b>C-F</b>) and antiserum against PbICP-C (rabbit, green) (<b>A-F</b>). DNA was stained with DAPI (blue).</p>", "links"=>[], "tags"=>["localizes"], "article_id"=>527449, "categories"=>["Physics", "Cell Biology"], "users"=>["Annika Rennenberg", "Christine Lehmann", "Anna Heitmann", "Tina Witt", "Guido Hansen", "Krishna Nagarajan", "Christina Deschermeier", "Vito Turk", "Rolf Hilgenfeld", "Volker T. Heussler"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1000825.g004", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_PbICP_is_expressed_throughout_the_liver_stage_and_localizes_to_different_microenvironments_/527449", "title"=>"PbICP is expressed throughout the liver stage and localizes to different microenvironments.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2010-03-26 02:04:09"}
  • {"files"=>["https://ndownloader.figshare.com/files/856744"], "description"=>"<p>(<b>A</b>) Widefield IFA of <i>P. berghei</i> sporozoites that have been allowed to glide on glass coverslips. Sporozoites were fixed after 1 h and subsequently stained with anti-CSP antiserum (mouse, red) and polyclonal antiserum against PbICP-C (rabbit, green). DNA was stained with DAPI (blue). Like the shedded surface protein CSP, PbICP was detected in a patchy pattern in the trails of the circling sporozoites. (<b>B</b>) IEM confirms PbICP localization in vesicles of a midgut sporozoite. <i>P. berghei</i> infected <i>A. stephensi</i> midguts were fixed 20 days after infection and prepared for IEM. Ultrathin sections were stained with polyclonal antiserum directed against PbICP-C (rabbit) and subsequently with gold-labeled Protein A (10 nm gold particles). The sections were contrasted with uranyl acetate and lead citrate.</p>", "links"=>[], "tags"=>["secreted", "salivary", "gland"], "article_id"=>527190, "categories"=>["Physics", "Cell Biology"], "users"=>["Annika Rennenberg", "Christine Lehmann", "Anna Heitmann", "Tina Witt", "Guido Hansen", "Krishna Nagarajan", "Christina Deschermeier", "Vito Turk", "Rolf Hilgenfeld", "Volker T. Heussler"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1000825.g002", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_PbICP_is_secreted_by_salivary_gland_sporozoites_/527190", "title"=>"PbICP is secreted by salivary gland sporozoites.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2010-03-26 01:59:50"}
  • {"files"=>["https://ndownloader.figshare.com/files/857445"], "description"=>"<p>(<b>A</b>) HepG2 cells were transiently transfected with plasmids leading to either cytosolic expression of GFP-tagged PbICP-C or GFP as a control. The transfection efficiency of HepG2 cells with the control plasmid and the GFP-PbICP-C plasmid (absolute numbers of GFP-positive cells/cover) were similar. Host cell death was induced by tBHP treatment for 4 h and analyzed by live imaging using TMRE staining of intact mitochondria (red). DNA condensation was visualized by Hoechst 33258 staining (blue). Dying cells exhibited condensed chromatin in the nucleus and a loss of the mitochondrial membrane potential. (<b>B</b>) Fluorescent cells were counted and the percentage of dead and viable cells was calculated. Presented are the means and standard deviations of three independent experiments. Cells expressing GFP-PbICP-C showed a significantly better survival following tBHP treatment in comparison to GFP-expressing cells.</p>", "links"=>[], "tags"=>["protects", "hepg2", "cells"], "article_id"=>527891, "categories"=>["Physics", "Cell Biology"], "users"=>["Annika Rennenberg", "Christine Lehmann", "Anna Heitmann", "Tina Witt", "Guido Hansen", "Krishna Nagarajan", "Christina Deschermeier", "Vito Turk", "Rolf Hilgenfeld", "Volker T. Heussler"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1000825.g008", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_PbICP_C_expression_protects_HepG2_cells_against_host_cell_death_/527891", "title"=>"PbICP-C expression protects HepG2 cells against host cell death.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2010-03-26 02:11:31"}
  • {"files"=>["https://ndownloader.figshare.com/files/857678"], "description"=>"<p>Substrate hydrolysis was measured in the presence of the control protein MBP (1 µM or 100 nM) or in the presence of MBP-PbICP (1 µM or 100 nM) or PbICP (100 nM). Experiments were performed in triplicate. Protease activity in the presence of 1 µM and 100 nM MBP, respectively was considered as 100% and the percentage of residual protease activity in the presence of the inhibitor was calculated. n.d. not done.</p>", "links"=>[], "tags"=>["pbicp", "potent", "inhibitor", "cysteine", "proteases", "cathepsin"], "article_id"=>528127, "categories"=>["Physics", "Cell Biology"], "users"=>["Annika Rennenberg", "Christine Lehmann", "Anna Heitmann", "Tina Witt", "Guido Hansen", "Krishna Nagarajan", "Christina Deschermeier", "Vito Turk", "Rolf Hilgenfeld", "Volker T. Heussler"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1000825.t001", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Recombinant_PbICP_is_a_potent_inhibitor_of_cysteine_proteases_but_not_of_cathepsin_B_/528127", "title"=>"Recombinant PbICP is a potent inhibitor of cysteine proteases but not of cathepsin B.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2010-03-26 02:15:27"}

PMC Usage Stats | Further Information

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  • {"unique-ip"=>"14", "full-text"=>"15", "pdf"=>"5", "abstract"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"3", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2013", "month"=>"5"}
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Relative Metric

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