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  1. Article ; Online: mSphere of Influence: Tweaking Organellar Purification Approaches.

    Huet, Diego

    mSphere

    2020  Volume 5, Issue 5

    Abstract: Diego Huet studies the organelles involved in the metabolic adaptations of the apicomplexan ... ...

    Abstract Diego Huet studies the organelles involved in the metabolic adaptations of the apicomplexan parasite
    MeSH term(s) Cytological Techniques ; Humans ; Metabolome ; Mitochondria/metabolism ; Toxoplasma/metabolism
    Language English
    Publishing date 2020-09-09
    Publishing country United States
    Document type Journal Article
    ISSN 2379-5042
    ISSN (online) 2379-5042
    DOI 10.1128/mSphere.00690-20
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Interorganellar Communication Through Membrane Contact Sites in

    Huet, Diego / Moreno, Silvia N J

    Contact (Thousand Oaks (Ventura County, Calif.))

    2023  Volume 6, Page(s) 25152564231189064

    Abstract: Apicomplexan parasites are a group of protists that cause disease in humans and include pathogens ... ...

    Abstract Apicomplexan parasites are a group of protists that cause disease in humans and include pathogens like
    Language English
    Publishing date 2023-08-06
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 2964312-0
    ISSN 2515-2564 ; 2515-2564
    ISSN (online) 2515-2564
    ISSN 2515-2564
    DOI 10.1177/25152564231189064
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: ATP synthase-associated coiled-coil-helix-coiled-coil-helix (CHCH) domain-containing proteins are critical for mitochondrial function in

    Usey, Madelaine M / Huet, Diego

    mBio

    2023  Volume 14, Issue 5, Page(s) e0176923

    Abstract: Importance: Members of the coiled-coil-helix-coiled-coil-helix (CHCH) domain protein family are transported into the mitochondrial intermembrane space, where they play important roles in the biogenesis and function of the organelle. Unexpectedly, the ... ...

    Abstract Importance: Members of the coiled-coil-helix-coiled-coil-helix (CHCH) domain protein family are transported into the mitochondrial intermembrane space, where they play important roles in the biogenesis and function of the organelle. Unexpectedly, the ATP synthase of the apicomplexan
    MeSH term(s) Animals ; Toxoplasma/genetics ; Toxoplasma/metabolism ; Mitochondria/metabolism ; Proteins/metabolism ; Parasites/metabolism ; Nitric Oxide Synthase/metabolism ; Adenosine Triphosphate/metabolism ; Protozoan Proteins/genetics ; Protozoan Proteins/metabolism ; Mitochondrial Proteins/metabolism
    Chemical Substances Proteins ; Nitric Oxide Synthase (EC 1.14.13.39) ; Adenosine Triphosphate (8L70Q75FXE) ; Protozoan Proteins ; Mitochondrial Proteins
    Language English
    Publishing date 2023-10-05
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2557172-2
    ISSN 2150-7511 ; 2161-2129
    ISSN (online) 2150-7511
    ISSN 2161-2129
    DOI 10.1128/mbio.01769-23
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Parasite powerhouse: A review of the Toxoplasma gondii mitochondrion.

    Usey, Madelaine M / Huet, Diego

    The Journal of eukaryotic microbiology

    2022  Volume 69, Issue 6, Page(s) e12906

    Abstract: Toxoplasma gondii is a member of the apicomplexan phylum, a group of single-celled eukaryotic parasites that cause significant human morbidity and mortality around the world. T. gondii harbors two organelles of endosymbiotic origin: a non-photosynthetic ... ...

    Abstract Toxoplasma gondii is a member of the apicomplexan phylum, a group of single-celled eukaryotic parasites that cause significant human morbidity and mortality around the world. T. gondii harbors two organelles of endosymbiotic origin: a non-photosynthetic plastid, known as the apicoplast, and a single mitochondrion derived from the ancient engulfment of an α-proteobacterium. Due to excitement surrounding the novelty of the apicoplast, the T. gondii mitochondrion was, to a certain extent, overlooked for about two decades. However, recent work has illustrated that the mitochondrion is an essential hub of apicomplexan-specific biology. Development of novel techniques, such as cryo-electron microscopy, complexome profiling, and next-generation sequencing have led to a renaissance in mitochondrial studies. This review will cover what is currently known about key features of the T. gondii mitochondrion, ranging from its genome to protein import machinery and biochemical pathways. Particular focus will be given to mitochondrial features that diverge significantly from the mammalian host, along with discussion of this important organelle as a drug target.
    MeSH term(s) Animals ; Humans ; Toxoplasma/metabolism ; Parasites ; Cryoelectron Microscopy ; Apicoplasts/metabolism ; Mitochondria/metabolism ; Mammals
    Language English
    Publishing date 2022-05-04
    Publishing country United States
    Document type Journal Article ; Review ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 1147218-2
    ISSN 1550-7408 ; 1066-5234
    ISSN (online) 1550-7408
    ISSN 1066-5234
    DOI 10.1111/jeu.12906
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Editorial: Disruptive technologies for the study of host-pathogen interactions.

    Quintana, Juan F / Harding, Clare / Huet, Diego / Sateriale, Adam / Bernabeu, Maria

    Frontiers in cellular and infection microbiology

    2022  Volume 12, Page(s) 1048342

    MeSH term(s) Disruptive Technology ; Host-Pathogen Interactions ; Host-Parasite Interactions
    Language English
    Publishing date 2022-10-13
    Publishing country Switzerland
    Document type Editorial ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
    ZDB-ID 2619676-1
    ISSN 2235-2988 ; 2235-2988
    ISSN (online) 2235-2988
    ISSN 2235-2988
    DOI 10.3389/fcimb.2022.1048342
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: The mystery of massive mitochondrial complexes: the apicomplexan respiratory chain.

    Maclean, Andrew E / Hayward, Jenni A / Huet, Diego / van Dooren, Giel G / Sheiner, Lilach

    Trends in parasitology

    2022  Volume 38, Issue 12, Page(s) 1041–1052

    Abstract: The mitochondrial respiratory chain is an essential pathway in most studied eukaryotes due to its roles in respiration and other pathways that depend on mitochondrial membrane potential. Apicomplexans are unicellular eukaryotes whose members have an ... ...

    Abstract The mitochondrial respiratory chain is an essential pathway in most studied eukaryotes due to its roles in respiration and other pathways that depend on mitochondrial membrane potential. Apicomplexans are unicellular eukaryotes whose members have an impact on global health. The respiratory chain is a drug target for some members of this group, notably the malaria-causing Plasmodium spp. This has motivated studies of the respiratory chain in apicomplexan parasites, primarily Toxoplasma gondii and Plasmodium spp. for which experimental tools are most advanced. Studies of the respiratory complexes in these organisms revealed numerous novel features, including expansion of complex size. The divergence of apicomplexan mitochondria from commonly studied models highlights the diversity of mitochondrial form and function across eukaryotic life.
    MeSH term(s) Humans ; Electron Transport ; Mitochondria/metabolism ; Toxoplasma ; Plasmodium/metabolism ; Malaria/parasitology ; Apicomplexa/metabolism
    Language English
    Publishing date 2022-10-24
    Publishing country England
    Document type Journal Article ; Review ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
    ZDB-ID 2036227-4
    ISSN 1471-5007 ; 1471-4922
    ISSN (online) 1471-5007
    ISSN 1471-4922
    DOI 10.1016/j.pt.2022.09.008
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: IFT25 is required for the construction of the trypanosome flagellum.

    Huet, Diego / Blisnick, Thierry / Perrot, Sylvie / Bastin, Philippe

    Journal of cell science

    2019  Volume 132, Issue 5

    Abstract: Intraflagellar transport (IFT), the movement of protein complexes responsible for the assembly of cilia and flagella, is remarkably conserved from protists to humans. However, two IFT components (IFT25 and IFT27) are missing from multiple unrelated ... ...

    Abstract Intraflagellar transport (IFT), the movement of protein complexes responsible for the assembly of cilia and flagella, is remarkably conserved from protists to humans. However, two IFT components (IFT25 and IFT27) are missing from multiple unrelated eukaryotic species. In mouse, IFT25 (also known as HSPB11) and IFT27 are not required for assembly of several cilia with the noticeable exception of the flagellum of spermatozoa. Here, we show that the
    MeSH term(s) Animals ; Cilia/metabolism ; Flagella/genetics ; Flagella/metabolism ; Intracellular Signaling Peptides and Proteins/genetics ; Intracellular Signaling Peptides and Proteins/metabolism ; Male ; Mice ; Molecular Chaperones/genetics ; Molecular Chaperones/metabolism ; Protein Transport ; Protozoan Proteins/genetics ; Protozoan Proteins/metabolism ; Spermatozoa/metabolism ; Trypanosoma brucei brucei/physiology ; rab GTP-Binding Proteins/genetics ; rab GTP-Binding Proteins/metabolism
    Chemical Substances IFT25 protein, mouse ; Intracellular Signaling Peptides and Proteins ; Molecular Chaperones ; Protozoan Proteins ; intraflagellar transport 27 protein, mouse ; rab GTP-Binding Proteins (EC 3.6.5.2)
    Language English
    Publishing date 2019-02-22
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2993-2
    ISSN 1477-9137 ; 0021-9533
    ISSN (online) 1477-9137
    ISSN 0021-9533
    DOI 10.1242/jcs.228296
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: CRISPR-Cas9-based genome-wide screening of Toxoplasma gondii.

    Sidik, Saima M / Huet, Diego / Lourido, Sebastian

    Nature protocols

    2018  Volume 13, Issue 1, Page(s) 307–323

    Abstract: Apicomplexan parasites, such as Toxoplasma gondii, cause extensive morbidity and mortality in humans and livestock, highlighting the need for a deeper understanding of their molecular biology. Although techniques for the generation of targeted gene ... ...

    Abstract Apicomplexan parasites, such as Toxoplasma gondii, cause extensive morbidity and mortality in humans and livestock, highlighting the need for a deeper understanding of their molecular biology. Although techniques for the generation of targeted gene disruptions have long been available for apicomplexans, such methods are not readily scalable to the entire genome. We recently used CRISPR-Cas9 to disrupt all nuclear protein-coding genes in T. gondii using a pooled format. The method relies on transfection of a guide RNA library into parasites constitutively expressing Cas9. Here, we present the complete workflow of such a screen, including preparation of the guide RNA library, growth and testing of the recipient strain, generation of the mutant population, culture conditions for the screen, preparation of genomic DNA libraries, next-generation sequencing of the guide RNA loci, and analysis to detect fitness-conferring genes. This method can be deployed to study how culture conditions affect the repertoire of genes needed by parasites, which will enable studies of their metabolic needs, host specificity, and drug-resistance mechanisms. In addition, by manipulating the background in which the screen is performed, researchers will be able to investigate genetic interactions, which may help uncover redundancy or epistasis in the parasite genome. Using this method, a genome-wide screen and its analysis can be completed in 3 weeks, after ∼1 month of preparation to generate the library and grow the cells needed, making it a powerful tool for uncovering functionally important genes in apicomplexan parasites.
    MeSH term(s) CRISPR-Cas Systems/physiology ; Chromosome Mapping/methods ; Clustered Regularly Interspaced Short Palindromic Repeats ; Gene Knockout Techniques/methods ; Genome, Protozoan ; Genomic Library ; Humans ; Nuclear Proteins/genetics ; Nuclear Proteins/physiology ; RNA, Guide, CRISPR-Cas Systems ; Toxoplasma/genetics ; Transfection
    Chemical Substances Nuclear Proteins ; RNA, Guide, CRISPR-Cas Systems
    Language English
    Publishing date 2018-01-11
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2244966-8
    ISSN 1750-2799 ; 1754-2189
    ISSN (online) 1750-2799
    ISSN 1754-2189
    DOI 10.1038/nprot.2017.131
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  9. Article ; Online: Review of basal-plus insulin regimen options for simpler insulin intensification in people with Type 2 diabetes mellitus.

    Raccah, D / Huet, D / Dib, A / Joseph, F / Landers, B / Escalada, J / Schmitt, H

    Diabetic medicine : a journal of the British Diabetic Association

    2017  Volume 34, Issue 9, Page(s) 1193–1204

    Abstract: Aims: To identify simple insulin regimens for people with Type 2 diabetes mellitus that can be accepted and implemented earlier in primary and specialist care, taking into consideration each individual's needs and capabilities.: Methods: Using ... ...

    Abstract Aims: To identify simple insulin regimens for people with Type 2 diabetes mellitus that can be accepted and implemented earlier in primary and specialist care, taking into consideration each individual's needs and capabilities.
    Methods: Using randomized clinical trials identified by a search of the PubMed database, as well as systematic reviews, meta-analyses and proof-of-concept studies, this review addresses topics of interest related to the progressive intensification of a basal insulin regimen to a basal-plus regimen (one basal insulin injection plus stepwise addition of one to three preprandial short-acting insulin injections/day) vs a basal-bolus regimen (basal insulin plus three short-acting insulin injections per day) in people with Type 2 diabetes. The review explores approaches that can be used to define the meal for first prandial injection with basal-plus regimens, differences among insulin titration algorithms, and the importance of self-motivation and autonomy in achieving optimum glycaemic control.
    Results: A basal-plus regimen can provide glycaemic control equivalent to that obtained with a full basal-bolus regimen, with fewer injections of prandial insulin. The first critical step is to optimize basal insulin dosing to reach a fasting glucose concentration of ~6.7 mmol/l; this allows ~40% of patients with baseline HbA
    Conclusions: Compared with a basal-bolus regimen, a basal-plus insulin regimen is as effective but more practical, and has the best chance of acceptance and success in the real world.
    MeSH term(s) Blood Glucose/analysis ; Blood Glucose/drug effects ; Blood Glucose/metabolism ; Diabetes Mellitus, Type 2/blood ; Diabetes Mellitus, Type 2/drug therapy ; Diabetes Mellitus, Type 2/epidemiology ; Dose-Response Relationship, Drug ; Drug Administration Schedule ; Drug Therapy, Combination/methods ; Glycated Hemoglobin A/analysis ; Glycated Hemoglobin A/metabolism ; Humans ; Hypoglycemic Agents/administration & dosage ; Hypoglycemic Agents/adverse effects ; Insulin/administration & dosage ; Insulin/adverse effects
    Chemical Substances Blood Glucose ; Glycated Hemoglobin A ; Hypoglycemic Agents ; Insulin
    Language English
    Publishing date 2017-07-09
    Publishing country England
    Document type Journal Article ; Review ; Research Support, Non-U.S. Gov't
    ZDB-ID 605769-x
    ISSN 1464-5491 ; 0742-3071 ; 1466-5468
    ISSN (online) 1464-5491
    ISSN 0742-3071 ; 1466-5468
    DOI 10.1111/dme.13390
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  10. Article ; Online: Infection pulmonaire à Mycobacterium malmoense. Difficultés diagnostiques et de thérapeutiques.

    Huet, D / Godbert, B / Hermann, J / Zordan, J-M / Chabot, F / Andréjak, C

    Revue des maladies respiratoires

    2017  Volume 34, Issue 3, Page(s) 257–261

    Abstract: Introduction: Pulmonary infection due to Mycobacterium malmoense can be difficult to diagnose. These difficulties can be responsible for a delay in the implementation of optimal treatment. Moreover, the treatment is not standardized.: Observation: We ...

    Title translation Pulmonary infection with Mycobacterium malmoense. Difficulties in diagnosis and treatment.
    Abstract Introduction: Pulmonary infection due to Mycobacterium malmoense can be difficult to diagnose. These difficulties can be responsible for a delay in the implementation of optimal treatment. Moreover, the treatment is not standardized.
    Observation: We report the case of a 56-year-old patient who developed a Mycobacterium malmoense pulmonary infection whose diagnosis was delayed due to initial suspicion of pulmonary Mycobacterium tuberculosis infection. Once the diagnosis was confirmed, the patient was treated empirically with rifampicin, ethambutol, and clarithromycin for 12 months after culture conversion, giving a total of 15 months. The clinical and radiological outcomes were favorable.
    Discussion: This clinical case highlights the difficulties of diagnosing pulmonary atypical mycobacterial infection according to the American Thoracic Society criteria, particularly Mycobacterium malmoense, a non-tuberculous mycobacterium (NTM) quite uncommon in France. Currently, there are new diagnostic techniques such as GenoType Mycobacteria Direct
    Conclusion: A more systematic reporting strategy could allow cohort studies and therefore provide us with data on the most efficient drugs in the treatment of the rarest NTM infections.
    MeSH term(s) Clarithromycin/administration & dosage ; Diagnosis, Differential ; Ethambutol/administration & dosage ; Humans ; Lung Diseases/diagnosis ; Lung Diseases/drug therapy ; Lung Diseases/microbiology ; Male ; Middle Aged ; Mycobacterium Infections, Nontuberculous/diagnosis ; Mycobacterium Infections, Nontuberculous/drug therapy ; Mycobacterium Infections, Nontuberculous/microbiology ; Nontuberculous Mycobacteria/isolation & purification ; Respiratory Tract Infections/diagnosis ; Respiratory Tract Infections/drug therapy ; Rifampin/administration & dosage ; Tuberculosis, Pulmonary/diagnosis
    Chemical Substances Ethambutol (8G167061QZ) ; Clarithromycin (H1250JIK0A) ; Rifampin (VJT6J7R4TR)
    Language French
    Publishing date 2017-03
    Publishing country France
    Document type Case Reports ; Journal Article
    ZDB-ID 605743-3
    ISSN 1776-2588 ; 0301-0279 ; 0761-8425
    ISSN (online) 1776-2588
    ISSN 0301-0279 ; 0761-8425
    DOI 10.1016/j.rmr.2016.05.012
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