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  1. Article ; Online: CDC50 Orthologues in Plasmodium falciparum Have Distinct Roles in Merozoite Egress and Trophozoite Maturation.

    Patel, Avnish / Nofal, Stephanie D / Blackman, Michael J / Baker, David A

    mBio

    2022  Volume 13, Issue 4, Page(s) e0163522

    Abstract: In model organisms, type IV ATPases (P4-ATPases) require cell division control protein 50 (CDC50) chaperones for their phospholipid flipping activity. In the malaria parasite Plasmodium falciparum, guanylyl cyclase alpha (GCα) is an integral membrane ... ...

    Abstract In model organisms, type IV ATPases (P4-ATPases) require cell division control protein 50 (CDC50) chaperones for their phospholipid flipping activity. In the malaria parasite Plasmodium falciparum, guanylyl cyclase alpha (GCα) is an integral membrane protein that is essential for release (egress) of merozoites from their host erythrocytes. GCα is unusual in that it contains both a C-terminal cyclase domain and an N-terminal P4-ATPase domain of unknown function. We sought to investigate whether any of the three CDC50 orthologues (termed A, B, and C) encoded by P. falciparum are required for GCα function. Using gene tagging and conditional gene disruption, we demonstrate that CDC50B and CDC50C but not CDC50A are expressed in the clinically important asexual blood stages and that CDC50B is a binding partner of GCα whereas CDC50C is the binding partner of another putative P4-ATPase, phospholipid-transporting ATPase 2 (ATP2). Our findings indicate that CDC50B has no essential role for intraerythrocytic parasite maturation but modulates the rate of parasite egress by interacting with GCα for optimal cGMP synthesis. In contrast, CDC50C is essential for blood stage trophozoite maturation. Additionally, we find that the CDC50C-ATP2 complex may influence parasite endocytosis of host cell hemoglobin and consequently hemozoin formation.
    MeSH term(s) Adenosine Triphosphatases/genetics ; Animals ; Erythrocytes/parasitology ; Guanylate Cyclase ; Humans ; Malaria ; Malaria, Falciparum/parasitology ; Merozoites/physiology ; Phospholipids ; Plasmodium falciparum/metabolism ; Protozoan Proteins/genetics ; Protozoan Proteins/metabolism ; Trophozoites/metabolism
    Chemical Substances Phospholipids ; Protozoan Proteins ; Adenosine Triphosphatases (EC 3.6.1.-) ; Guanylate Cyclase (EC 4.6.1.2)
    Language English
    Publishing date 2022-07-12
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2557172-2
    ISSN 2150-7511 ; 2161-2129
    ISSN (online) 2150-7511
    ISSN 2161-2129
    DOI 10.1128/mbio.01635-22
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Malaria parasite egress at a glance.

    Tan, Michele S Y / Blackman, Michael J

    Journal of cell science

    2021  Volume 134, Issue 5

    Abstract: All intracellular pathogens must escape (egress) from the confines of their host cell to disseminate and proliferate. The malaria parasite only replicates in an intracellular vacuole or in a cyst, and must undergo egress at four distinct phases during ... ...

    Abstract All intracellular pathogens must escape (egress) from the confines of their host cell to disseminate and proliferate. The malaria parasite only replicates in an intracellular vacuole or in a cyst, and must undergo egress at four distinct phases during its complex life cycle, each time disrupting, in a highly regulated manner, the membranes or cyst wall that entrap the parasites. This Cell Science at a Glance article and accompanying poster summarises our current knowledge of the morphological features of egress across the
    MeSH term(s) Animals ; Erythrocytes ; Life Cycle Stages ; Malaria ; Parasites ; Plasmodium ; Plasmodium falciparum ; Protozoan Proteins
    Chemical Substances Protozoan Proteins
    Language English
    Publishing date 2021-03-08
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2993-2
    ISSN 1477-9137 ; 0021-9533
    ISSN (online) 1477-9137
    ISSN 0021-9533
    DOI 10.1242/jcs.257345
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: The parasitophorous vacuole of the blood-stage malaria parasite.

    Matz, Joachim M / Beck, Josh R / Blackman, Michael J

    Nature reviews. Microbiology

    2020  Volume 18, Issue 7, Page(s) 379–391

    Abstract: The pathology of malaria is caused by infection of red blood cells with unicellular Plasmodium parasites. During blood-stage development, the parasite replicates within a membrane-bound parasitophorous vacuole. A central nexus for host-parasite ... ...

    Abstract The pathology of malaria is caused by infection of red blood cells with unicellular Plasmodium parasites. During blood-stage development, the parasite replicates within a membrane-bound parasitophorous vacuole. A central nexus for host-parasite interactions, this unique parasite shelter functions in nutrient acquisition, subcompartmentalization and the export of virulence factors, making its functional molecules attractive targets for the development of novel intervention strategies to combat the devastating impact of malaria. In this Review, we explore the origin, development, molecular composition and functions of the parasitophorous vacuole of Plasmodium blood stages. We also discuss the relevance of the malaria parasite's intravacuolar lifestyle for successful erythrocyte infection and provide perspectives for future research directions in parasitophorous vacuole biology.
    MeSH term(s) Erythrocytes/parasitology ; Host-Parasite Interactions ; Humans ; Life Cycle Stages ; Malaria, Falciparum/pathology ; Merozoites/growth & development ; Plasmodium falciparum/growth & development ; Vacuoles/parasitology
    Language English
    Publishing date 2020-01-24
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2139054-X
    ISSN 1740-1534 ; 1740-1526
    ISSN (online) 1740-1534
    ISSN 1740-1526
    DOI 10.1038/s41579-019-0321-3
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Subtilisin-like Serine Protease 1 (SUB1) as an Emerging Antimalarial Drug Target: Current Achievements in Inhibitor Discovery.

    Lidumniece, Elina / Withers-Martinez, Chrislaine / Hackett, Fiona / Blackman, Michael J / Jirgensons, Aigars

    Journal of medicinal chemistry

    2022  Volume 65, Issue 19, Page(s) 12535–12545

    Abstract: Widespread resistance to many antimalarial therapies currently in use stresses the need for the discovery of new classes of drugs with new modes of action. The subtilisin-like serine protease SUB1 controls egress of malaria parasites (merozoites) from ... ...

    Abstract Widespread resistance to many antimalarial therapies currently in use stresses the need for the discovery of new classes of drugs with new modes of action. The subtilisin-like serine protease SUB1 controls egress of malaria parasites (merozoites) from the parasite-infected red blood cell. As such, SUB1 is considered a prospective target for drugs designed to interrupt the asexual blood stage life cycle of the malaria parasite. Inhibitors of SUB1 have potential as wide-spectrum antimalarial drugs, as a single orthologue of SUB1 is found in the genomes of all known
    MeSH term(s) Antimalarials/chemistry ; Antimalarials/pharmacology ; Antimalarials/therapeutic use ; Erythrocytes/metabolism ; Humans ; Malaria/drug therapy ; Malaria/parasitology ; Plasmodium ; Plasmodium falciparum/metabolism ; Protozoan Proteins/metabolism ; Serine ; Serine Proteinase Inhibitors ; Subtilisins/chemistry ; Subtilisins/metabolism
    Chemical Substances Antimalarials ; Protozoan Proteins ; Serine Proteinase Inhibitors ; Serine (452VLY9402) ; Subtilisins (EC 3.4.21.-)
    Language English
    Publishing date 2022-09-22
    Publishing country United States
    Document type Journal Article ; Review ; Research Support, Non-U.S. Gov't
    ZDB-ID 218133-2
    ISSN 1520-4804 ; 0022-2623
    ISSN (online) 1520-4804
    ISSN 0022-2623
    DOI 10.1021/acs.jmedchem.2c01093
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: The role of

    Alder, Arne / Sanchez, Cecilia P / Russell, Matthew R G / Collinson, Lucy M / Lanzer, Michael / Blackman, Michael J / Gilberger, Tim-Wolf / Matz, Joachim M

    Proceedings of the National Academy of Sciences of the United States of America

    2023  Volume 120, Issue 30, Page(s) e2306420120

    Abstract: To ensure their survival in the human bloodstream, malaria parasites degrade up to 80% of the host erythrocyte hemoglobin in an acidified digestive vacuole. Here, we combine conditional reverse genetics and quantitative imaging approaches to demonstrate ... ...

    Abstract To ensure their survival in the human bloodstream, malaria parasites degrade up to 80% of the host erythrocyte hemoglobin in an acidified digestive vacuole. Here, we combine conditional reverse genetics and quantitative imaging approaches to demonstrate that the human malaria pathogen
    MeSH term(s) Animals ; Humans ; Antimalarials/pharmacology ; Antimalarials/metabolism ; Adenosine Triphosphatases/metabolism ; Vacuoles ; Malaria, Falciparum/parasitology ; Plasmodium falciparum/metabolism ; Parasites
    Chemical Substances Antimalarials ; Adenosine Triphosphatases (EC 3.6.1.-)
    Language English
    Publishing date 2023-07-18
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.2306420120
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  6. Article ; Online: Simultaneous multiple allelic replacement in the malaria parasite enables dissection of PKG function.

    Koussis, Konstantinos / Withers-Martinez, Chrislaine / Baker, David A / Blackman, Michael J

    Life science alliance

    2020  Volume 3, Issue 4

    Abstract: Over recent years, a plethora of new genetic tools has transformed conditional engineering of the malaria parasite genome, allowing functional dissection of essential genes in the asexual and sexual blood stages that cause pathology or are required for ... ...

    Abstract Over recent years, a plethora of new genetic tools has transformed conditional engineering of the malaria parasite genome, allowing functional dissection of essential genes in the asexual and sexual blood stages that cause pathology or are required for disease transmission, respectively. Important challenges remain, including the desirability to complement conditional mutants with a correctly regulated second gene copy to confirm that observed phenotypes are due solely to loss of gene function and to analyse structure-function relationships. To meet this challenge, here we combine the dimerisable Cre (DiCre) system with the use of multiple
    MeSH term(s) Alleles ; Animals ; Cyclic GMP-Dependent Protein Kinases/genetics ; Cyclic GMP-Dependent Protein Kinases/metabolism ; Erythrocytes/metabolism ; Gene Deletion ; Malaria/genetics ; Parasites/metabolism ; Phenotype ; Phosphorylation ; Plasmodium falciparum/genetics ; Protozoan Proteins/genetics
    Chemical Substances Protozoan Proteins ; Cyclic GMP-Dependent Protein Kinases (EC 2.7.11.12)
    Language English
    Publishing date 2020-03-16
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 2575-1077
    ISSN (online) 2575-1077
    DOI 10.26508/lsa.201900626
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: Plasmodium falciparum

    Nofal, Stephanie D / Patel, Avnish / Blackman, Michael J / Flueck, Christian / Baker, David A

    mBio

    2021  Volume 12, Issue 1

    Abstract: Guanylyl cyclases (GCs) synthesize cyclic GMP (cGMP) and, together with cyclic nucleotide phosphodiesterases, are responsible for regulating levels of this intracellular messenger which mediates myriad functions across eukaryotes. In malaria parasites ( ...

    Abstract Guanylyl cyclases (GCs) synthesize cyclic GMP (cGMP) and, together with cyclic nucleotide phosphodiesterases, are responsible for regulating levels of this intracellular messenger which mediates myriad functions across eukaryotes. In malaria parasites (
    MeSH term(s) Adenosine Triphosphatases/classification ; Adenosine Triphosphatases/genetics ; Adenosine Triphosphatases/metabolism ; Cyclic GMP/biosynthesis ; Cyclic GMP/genetics ; Erythrocytes/parasitology ; Guanylate Cyclase/genetics ; Guanylate Cyclase/metabolism ; Humans ; Malaria/parasitology ; Merozoites/physiology ; Plasmodium falciparum/enzymology ; Plasmodium falciparum/genetics ; Protein Domains ; Protozoan Proteins/genetics ; Protozoan Proteins/metabolism ; Signal Transduction
    Chemical Substances Protozoan Proteins ; Adenosine Triphosphatases (EC 3.6.1.-) ; Guanylate Cyclase (EC 4.6.1.2) ; Cyclic GMP (H2D2X058MU)
    Language English
    Publishing date 2021-01-26
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2557172-2
    ISSN 2150-7511 ; 2161-2129
    ISSN (online) 2150-7511
    ISSN 2161-2129
    DOI 10.1128/mBio.02694-20
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article: cAMP signalling and its role in host cell invasion by malaria parasites

    Perrin, Abigail J / Patel, Avnish / Flueck, Christian / Blackman, Michael J / Baker, David A

    Current opinion in microbiology. 2020 Dec., v. 58

    2020  

    Abstract: Cyclic adenosine monophosphate (cAMP) is an important signalling molecule across evolution, but until recently there was little information on its role in malaria parasites. Advances in gene editing – in particular conditional genetic approaches and mass ...

    Abstract Cyclic adenosine monophosphate (cAMP) is an important signalling molecule across evolution, but until recently there was little information on its role in malaria parasites. Advances in gene editing – in particular conditional genetic approaches and mass spectrometry have paved the way for characterisation of the key components of the cAMP signalling pathway in malaria parasites. This has revealed that cAMP signalling plays a critical role in invasion of host red blood cells by Plasmodium falciparum merozoites through regulating the phosphorylation of key parasite proteins by the cAMP-dependent protein kinase (PKA). These insights will help us to investigate parasite cAMP signalling as a target for novel antimalarial drugs.
    Keywords Plasmodium falciparum ; antimalarials ; cAMP-dependent protein kinase ; cyclic AMP ; evolution ; genes ; host cell invasion ; malaria ; mass spectrometry ; merozoites ; microbiology ; parasites ; phosphorylation
    Language English
    Dates of publication 2020-12
    Size p. 69-74.
    Publishing place Elsevier Ltd
    Document type Article
    Note NAL-AP-2-clean
    ZDB-ID 1418474-6
    ISSN 1879-0364 ; 1369-5274
    ISSN (online) 1879-0364
    ISSN 1369-5274
    DOI 10.1016/j.mib.2020.09.003
    Database NAL-Catalogue (AGRICOLA)

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  9. Article: Mixed Alkyl/Aryl Phosphonates Identify Metabolic Serine Hydrolases as Antimalarial Targets.

    Bennett, John M / Narwal, Sunil K / Kabeche, Stephanie / Abegg, Daniel / Hackett, Fiona / Yeo, Tomas / Li, Veronica L / Muir, Ryan K / Faucher, Franco F / Lovell, Scott / Blackman, Michael J / Adibekian, Alexander / Yeh, Ellen / Fidock, David A / Bogyo, Matthew

    bioRxiv : the preprint server for biology

    2024  

    Abstract: Malaria, caused ... ...

    Abstract Malaria, caused by
    Language English
    Publishing date 2024-01-11
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2024.01.11.575224
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  10. Article ; Online: Global analysis of putative phospholipases in

    Burda, Paul-Christian / Ramaprasad, Abhinay / Bielfeld, Sabrina / Pietsch, Emma / Woitalla, Anna / Söhnchen, Christoph / Singh, Mehar Nihal / Strauss, Jan / Sait, Aaron / Collinson, Lucy M / Schwudke, Dominik / Blackman, Michael J / Gilberger, Tim-Wolf

    mBio

    2023  Volume 14, Issue 4, Page(s) e0141323

    Abstract: For its replication within red blood cells, the malaria parasite depends on a highly active and regulated lipid metabolism. Enzymes involved in lipid metabolic processes such as phospholipases are, therefore, potential drug targets. Here, using reverse ... ...

    Abstract For its replication within red blood cells, the malaria parasite depends on a highly active and regulated lipid metabolism. Enzymes involved in lipid metabolic processes such as phospholipases are, therefore, potential drug targets. Here, using reverse genetics approaches, we show that only 1 out of the 19 putative phospholipases expressed in asexual blood stages of
    MeSH term(s) Animals ; Humans ; Plasmodium falciparum/metabolism ; Parasites/metabolism ; Phosphoinositide Phospholipase C/metabolism ; Phospholipases/genetics ; Phospholipases/metabolism ; Protozoan Proteins/genetics ; Protozoan Proteins/metabolism ; Malaria/metabolism ; Phospholipids/metabolism ; Phosphatidylinositols/metabolism ; Erythrocytes/parasitology ; Malaria, Falciparum/parasitology
    Chemical Substances Phosphoinositide Phospholipase C (EC 3.1.4.11) ; Phospholipases (EC 3.1.-) ; Protozoan Proteins ; Phospholipids ; Phosphatidylinositols
    Language English
    Publishing date 2023-07-25
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2557172-2
    ISSN 2150-7511 ; 2161-2129
    ISSN (online) 2150-7511
    ISSN 2161-2129
    DOI 10.1128/mbio.01413-23
    Database MEDical Literature Analysis and Retrieval System OnLINE

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