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  1. Article ; Online: Dissecting EXP2 sequence requirements for protein export in malaria parasites.

    Pitman, Ethan L / Counihan, Natalie A / Modak, Joyanta K / Chowdury, Mrittika / Gilson, Paul R / Webb, Chaille T / de Koning-Ward, Tania F

    Frontiers in cellular and infection microbiology

    2024  Volume 13, Page(s) 1332146

    Abstract: Apicomplexan parasites that reside within a parasitophorous vacuole harbor a conserved pore-forming protein that enables small-molecule transfer across the parasitophorous vacuole membrane (PVM). ... ...

    Abstract Apicomplexan parasites that reside within a parasitophorous vacuole harbor a conserved pore-forming protein that enables small-molecule transfer across the parasitophorous vacuole membrane (PVM). In
    MeSH term(s) Erythrocytes/parasitology ; Malaria, Falciparum/parasitology ; Plasmodium falciparum/genetics ; Protein Transport ; Protozoan Proteins/genetics ; Protozoan Proteins/metabolism ; Vacuoles/metabolism
    Chemical Substances Protozoan Proteins
    Language English
    Publishing date 2024-01-12
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2619676-1
    ISSN 2235-2988 ; 2235-2988
    ISSN (online) 2235-2988
    ISSN 2235-2988
    DOI 10.3389/fcimb.2023.1332146
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  2. Article ; Online: Post-translational lipid modifications in Plasmodium parasites.

    Counihan, Natalie A / Chernih, Hope C / de Koning-Ward, Tania F

    Current opinion in microbiology

    2022  Volume 69, Page(s) 102196

    Abstract: Most eukaryotic proteins undergo post-translational modifications (PTMs) that significantly alter protein properties, regulate diverse cellular processes and increase proteome complexity. Among these PTMs, lipidation plays a unique and key role in ... ...

    Abstract Most eukaryotic proteins undergo post-translational modifications (PTMs) that significantly alter protein properties, regulate diverse cellular processes and increase proteome complexity. Among these PTMs, lipidation plays a unique and key role in subcellular trafficking, signalling and membrane association of proteins through altering substrate function, and hydrophobicity via the addition and removal of lipid groups. Three prevalent classes of lipid modifications in Plasmodium parasites include prenylation, myristoylation, and palmitoylation that are important for regulating parasite-specific molecular processes. The enzymes that catalyse these lipid attachments have also been explored as potential drug targets for antimalarial development. In this review, we discuss these lipidation processes in Plasmodium spp. and the methodologies that have been used to identify these modifications in the deadliest species of malaria parasite, Plasmodium falciparum. We also discuss the development status of inhibitors that block these pathways.
    MeSH term(s) Animals ; Lipids ; Parasites ; Plasmodium/genetics ; Plasmodium/metabolism ; Plasmodium falciparum/genetics ; Plasmodium falciparum/metabolism ; Protein Processing, Post-Translational ; Protozoan Proteins/metabolism
    Chemical Substances Lipids ; Protozoan Proteins
    Language English
    Publishing date 2022-08-26
    Publishing country England
    Document type Journal Article ; Review ; Research Support, Non-U.S. Gov't
    ZDB-ID 1418474-6
    ISSN 1879-0364 ; 1369-5274
    ISSN (online) 1879-0364
    ISSN 1369-5274
    DOI 10.1016/j.mib.2022.102196
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article: How Malaria Parasites Acquire Nutrients From Their Host.

    Counihan, Natalie A / Modak, Joyanta K / de Koning-Ward, Tania F

    Frontiers in cell and developmental biology

    2021  Volume 9, Page(s) 649184

    Abstract: ... ...

    Abstract Plasmodium
    Language English
    Publishing date 2021-03-25
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2737824-X
    ISSN 2296-634X
    ISSN 2296-634X
    DOI 10.3389/fcell.2021.649184
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  4. Article ; Online: Methods Used to Investigate the

    Edgar, Rebecca C S / Counihan, Natalie A / McGowan, Sheena / de Koning-Ward, Tania F

    Frontiers in cellular and infection microbiology

    2022  Volume 11, Page(s) 829823

    Abstract: Plasmodium ... ...

    Abstract Plasmodium falciparum
    MeSH term(s) Antimalarials/pharmacology ; Antimalarials/therapeutic use ; Chloroquine/therapeutic use ; Humans ; Malaria, Falciparum/parasitology ; Plasmodium falciparum/genetics ; Vacuoles
    Chemical Substances Antimalarials ; Chloroquine (886U3H6UFF)
    Language English
    Publishing date 2022-01-13
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2619676-1
    ISSN 2235-2988 ; 2235-2988
    ISSN (online) 2235-2988
    ISSN 2235-2988
    DOI 10.3389/fcimb.2021.829823
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  5. Article: Post-translational lipid modifications in Plasmodium parasites

    Counihan, Natalie A / Chernih, Hope C / de Koning-Ward, Tania F

    Current opinion in microbiology. 2022 Oct., v. 69

    2022  

    Abstract: Most eukaryotic proteins undergo post-translational modifications (PTMs) that significantly alter protein properties, regulate diverse cellular processes and increase proteome complexity. Among these PTMs, lipidation plays a unique and key role in ... ...

    Abstract Most eukaryotic proteins undergo post-translational modifications (PTMs) that significantly alter protein properties, regulate diverse cellular processes and increase proteome complexity. Among these PTMs, lipidation plays a unique and key role in subcellular trafficking, signalling and membrane association of proteins through altering substrate function, and hydrophobicity via the addition and removal of lipid groups. Three prevalent classes of lipid modifications in Plasmodium parasites include prenylation, myristoylation, and palmitoylation that are important for regulating parasite-specific molecular processes. The enzymes that catalyse these lipid attachments have also been explored as potential drug targets for antimalarial development. In this review, we discuss these lipidation processes in Plasmodium spp. and the methodologies that have been used to identify these modifications in the deadliest species of malaria parasite, Plasmodium falciparum. We also discuss the development status of inhibitors that block these pathways.
    Keywords Plasmodium falciparum ; antimalarials ; hydrophobicity ; lipids ; malaria ; microbiology ; myristoylation ; palmitoylation ; parasites ; proteome
    Language English
    Dates of publication 2022-10
    Publishing place Elsevier Ltd
    Document type Article
    ZDB-ID 1418474-6
    ISSN 1879-0364 ; 1369-5274
    ISSN (online) 1879-0364
    ISSN 1369-5274
    DOI 10.1016/j.mib.2022.102196
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  6. Article ; Online: Specific IgA Enhances the Transcytosis and Excretion of Hepatitis A Virus.

    Counihan, Natalie A / Anderson, David A

    Scientific reports

    2016  Volume 6, Page(s) 21855

    Abstract: Hepatitis A virus (HAV) replicates in the liver, and is excreted from the body in feces. However, the mechanisms of HAV transport from hepatocytes to the gastrointestinal tract are poorly understood, mainly due to lack of suitable in vitro models. Here, ... ...

    Abstract Hepatitis A virus (HAV) replicates in the liver, and is excreted from the body in feces. However, the mechanisms of HAV transport from hepatocytes to the gastrointestinal tract are poorly understood, mainly due to lack of suitable in vitro models. Here, we use a polarized hepatic cell line and in vivo models to demonstrate vectorial transport of HAV from hepatocytes into bile via the apical cell membrane. Although this transport is specific for HAV, the rate of fecal excretion in inefficient, accounting for less than 1% of input virus from the bloodstream per hour. However, we also found that the rate of HAV excretion was enhanced in the presence of HAV-specific IgA. Using mice lacking the polymeric IgA receptor (pIgR(-/-)), we show that a proportion of HAV:IgA complexes are transported via the pIgR demonstrating a role for specific antibody in pathogen excretion.
    MeSH term(s) Animals ; Blotting, Western ; Caco-2 Cells ; Calicivirus, Feline/immunology ; Calicivirus, Feline/metabolism ; Calicivirus, Feline/physiology ; Cell Polarity ; Cells, Cultured ; Feces/virology ; Hepatitis A virus/immunology ; Hepatitis A virus/isolation & purification ; Hepatitis A virus/physiology ; Hepatocytes/cytology ; Hepatocytes/metabolism ; Hepatocytes/virology ; Humans ; Immunoglobulin A/immunology ; Immunoglobulin A/metabolism ; Liver/virology ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Microscopy, Electron, Scanning ; Rabbits ; Receptors, Fc/deficiency ; Receptors, Fc/genetics ; Receptors, Fc/metabolism ; Recombinant Proteins/biosynthesis ; Recombinant Proteins/immunology ; Recombinant Proteins/isolation & purification ; Transcytosis
    Chemical Substances IgA receptor ; Immunoglobulin A ; Receptors, Fc ; Recombinant Proteins
    Language English
    Publishing date 2016-02-25
    Publishing country England
    Document type Journal Article
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/srep21855
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  7. Article ; Online: Genetic and chemical validation of

    Edgar, Rebecca C S / Siddiqui, Ghizal / Hjerrild, Katheryn / Malcolm, Tess R / Vinh, Natalie B / Webb, Chaille T / Holmes, Clare / MacRaild, Christopher A / Chernih, Hope C / Suen, Willy W / Counihan, Natalie A / Creek, Darren J / Scammells, Peter J / McGowan, Sheena / de Koning-Ward, Tania F

    eLife

    2022  Volume 11

    Abstract: Plasmodium falciparum, ...

    Abstract Plasmodium falciparum,
    MeSH term(s) Aminopeptidases/chemistry ; Aminopeptidases/genetics ; Digestion ; Hemoglobins ; Humans ; Malaria, Falciparum ; Plasmodium falciparum/genetics ; Plasmodium falciparum/metabolism ; Protease Inhibitors ; Protozoan Proteins/chemistry ; Protozoan Proteins/genetics
    Chemical Substances Hemoglobins ; Protease Inhibitors ; Protozoan Proteins ; Aminopeptidases (EC 3.4.11.-)
    Language English
    Publishing date 2022-09-13
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2687154-3
    ISSN 2050-084X ; 2050-084X
    ISSN (online) 2050-084X
    ISSN 2050-084X
    DOI 10.7554/eLife.80813
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  8. Article ; Online: The malaria parasite Plasmodium falciparum Sortilin is essential for merozoite formation and apical complex biogenesis.

    Hallée, Stéphanie / Counihan, Natalie A / Matthews, Kathryn / de Koning-Ward, Tania F / Richard, Dave

    Cellular microbiology

    2018  Volume 20, Issue 8, Page(s) e12844

    Abstract: The inner membrane complex and the apical secretory organelles are defining features of apicomplexan parasites. Despite their critical roles, the mechanisms behind the biogenesis of these structures in the malaria parasite Plasmodium falciparum are still ...

    Abstract The inner membrane complex and the apical secretory organelles are defining features of apicomplexan parasites. Despite their critical roles, the mechanisms behind the biogenesis of these structures in the malaria parasite Plasmodium falciparum are still poorly defined. We here show that decreasing expression of the P. falciparum homologue of the conserved endolysomal escorter Sortilin-VPS10 prevents the formation of the inner membrane complex and abrogates the generation of new merozoites. Moreover, protein trafficking to the rhoptries, the micronemes, and the dense granules is disrupted, which leads to the accumulation of apical complex proteins in the endoplasmic reticulum and the parasitophorous vacuole. We further show that protein export to the erythrocyte and transport through the constitutive secretory pathway are functional. Taken together, our results suggest that the malaria parasite P. falciparum Sortilin has potentially broader functions than most of its other eukaryotic counterparts.
    MeSH term(s) Adaptor Proteins, Vesicular Transport/genetics ; Adaptor Proteins, Vesicular Transport/metabolism ; Gene Knockdown Techniques ; Merozoites/growth & development ; Organelle Biogenesis ; Plasmodium falciparum/growth & development ; Protein Transport
    Chemical Substances Adaptor Proteins, Vesicular Transport ; sortilin (Z020Y8WIJ4)
    Language English
    Publishing date 2018-04-30
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1468320-9
    ISSN 1462-5822 ; 1462-5814
    ISSN (online) 1462-5822
    ISSN 1462-5814
    DOI 10.1111/cmi.12844
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  9. Article ; Online: Characterisation of complexes formed by parasite proteins exported into the host cell compartment of Plasmodium falciparum infected red blood cells.

    Jonsdottir, Thorey K / Counihan, Natalie A / Modak, Joyanta K / Kouskousis, Betty / Sanders, Paul R / Gabriela, Mikha / Bullen, Hayley E / Crabb, Brendan S / de Koning-Ward, Tania F / Gilson, Paul R

    Cellular microbiology

    2021  Volume 23, Issue 8, Page(s) e13332

    Abstract: During its intraerythrocytic life cycle, the human malaria parasite Plasmodium falciparum supplements its nutritional requirements by scavenging substrates from the plasma through the new permeability pathways (NPPs) installed in the red blood cell (RBC) ...

    Abstract During its intraerythrocytic life cycle, the human malaria parasite Plasmodium falciparum supplements its nutritional requirements by scavenging substrates from the plasma through the new permeability pathways (NPPs) installed in the red blood cell (RBC) membrane. Parasite proteins of the RhopH complex: CLAG3, RhopH2, RhopH3, have been implicated in NPP activity. Here, we studied 13 exported proteins previously hypothesised to interact with RhopH2, to study their potential contribution to the function of NPPs. NPP activity assays revealed that the 13 proteins do not appear to be individually important for NPP function, as conditional knockdown of these proteins had no effect on sorbitol uptake. Intriguingly, reciprocal immunoprecipitation assays showed that five of the 13 proteins interact with all members of the RhopH complex, with PF3D7_1401200 showing the strongest association. Mass spectrometry-based proteomics further identified new protein complexes; a cytoskeletal complex and a Maurer's clefts/J-dot complex, which overall helps clarify protein-protein interactions within the infected RBC (iRBC) and is suggestive of the potential trafficking route of the RhopH complex itself to the RBC membrane.
    MeSH term(s) Animals ; Erythrocyte Membrane/metabolism ; Erythrocytes/metabolism ; Humans ; Parasites/metabolism ; Plasmodium falciparum/metabolism ; Protein Transport ; Protozoan Proteins/metabolism
    Chemical Substances Protozoan Proteins
    Language English
    Publishing date 2021-05-03
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1468320-9
    ISSN 1462-5822 ; 1462-5814
    ISSN (online) 1462-5822
    ISSN 1462-5814
    DOI 10.1111/cmi.13332
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Gumming up the works: DNA polymers as HCV entry inhibitors.

    Counihan, Natalie A / Lindenbach, Brett D

    Gastroenterology

    2009  Volume 137, Issue 2, Page(s) 427–430

    MeSH term(s) Antigens, CD/metabolism ; Antiviral Agents/pharmacology ; DNA/pharmacology ; DNA, Viral/genetics ; Drug Delivery Systems ; Hepacivirus/drug effects ; Hepacivirus/genetics ; Hepatitis C/genetics ; Hepatitis C/prevention & control ; Humans ; Hydrophobic and Hydrophilic Interactions ; Infection Control ; Polymers/pharmacology ; Primary Prevention/methods ; Virus Internalization/drug effects
    Chemical Substances Antigens, CD ; Antiviral Agents ; DNA, Viral ; Polymers ; DNA (9007-49-2)
    Language English
    Publishing date 2009-06-27
    Publishing country United States
    Document type Comment ; Editorial
    ZDB-ID 80112-4
    ISSN 1528-0012 ; 0016-5085
    ISSN (online) 1528-0012
    ISSN 0016-5085
    DOI 10.1053/j.gastro.2009.06.018
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    Zs.MO 572: Show issues

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