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  1. 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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  2. 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
    Database NAL-Catalogue (AGRICOLA)

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  3. 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
    Database MEDical Literature Analysis and Retrieval System OnLINE

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