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Cryptococcus neoformans

  • Open Access
    IP<sub>7</sub>-SPX Domain Interaction Controls Fungal Virulence by Stabilizing Phosphate Signaling Machinery
    Research Article | Host-Microbe Biology
    IP7-SPX Domain Interaction Controls Fungal Virulence by Stabilizing Phosphate Signaling Machinery

    Invasive fungal diseases pose a serious threat to human health globally with >1.5 million deaths occurring annually, 180,000 of which are attributable to the AIDS-related pathogen, Cryptococcus neoformans. Here, we demonstrate that interaction of the inositol pyrophosphate, IP7, with the CDK inhibitor protein, Pho81, is instrumental in promoting fungal...

    Desmarini Desmarini, Sophie Lev, David Furkert, Ben Crossett, Adolfo Saiardi, Keren Kaufman-Francis, Cecilia Li, Tania C. Sorrell, Lorna Wilkinson-White, Jacqueline Matthews, Dorothea Fiedler, Julianne Teresa Djordjevic
  • Open Access
    Laccase Affects the Rate of <span class="named-content genus-species" id="named-content-1">Cryptococcus neoformans</span> Nonlytic Exocytosis from Macrophages
    Observation | Host-Microbe Biology
    Laccase Affects the Rate of Cryptococcus neoformans Nonlytic Exocytosis from Macrophages

    Cryptococcus neoformans is a yeast that causes severe disease, primarily in immunosuppressed people. It has many attributes that allow it to survive and cause disease, such as a polysaccharide capsule and the dark pigment melanin produced by the laccase enzyme. Upon infection, the yeast is ingested by cells called macrophages, whose function is to kill them. Instead,...

    Stefânia de Oliveira Frazão, Herdson Renney de Sousa, Lenise Gonçalves da Silva, Jéssica dos Santos Folha, Kaio César de Melo Gorgonha, Getúlio Pereira de Oliveira, Maria Sueli Soares Felipe, Ildinete Silva-Pereira, Arturo Casadevall, André Moraes Nicola, Patrícia Albuquerque
  • Open Access
    An Antivirulence Approach for Preventing <span class="named-content genus-species" id="named-content-1">Cryptococcus neoformans</span> from Crossing the Blood-Brain Barrier via Novel Natural Product Inhibitors of a Fungal Metalloprotease
    Research Article | Therapeutics and Prevention
    An Antivirulence Approach for Preventing Cryptococcus neoformans from Crossing the Blood-Brain Barrier via Novel Natural Product Inhibitors of a Fungal Metalloprotease

    Fungal infections like cryptococcal meningitis are difficult to resolve because of the limited therapies available. The small arsenal of antifungal drugs reflect the difficulty in finding available targets in fungi because like mammalian cells, fungi are eukaryotes. The limited efficacy, toxicity, and rising resistance of antifungals contribute to the high morbidity and mortality of fungal infections and further underscore the dire but...

    Phylicia A. Aaron, Kiem Vu, Angie Gelli
  • Open Access
    Sterol-Response Pathways Mediate Alkaline Survival in Diverse Fungi
    Research Article | Host-Microbe Biology
    Sterol-Response Pathways Mediate Alkaline Survival in Diverse Fungi

    The work described here further elucidates how microorganisms sense and adapt to changes in their environment to establish infections in the human host. Specifically, we uncover a novel mechanism by which an opportunistic human fungal pathogen, Cryptococcus neoformans, responds to increases in extracellular pH in order to survive and thrive within the relatively...

    Hannah E. Brown, Calla L. Telzrow, Joseph W. Saelens, Larissa Fernandes, J. Andrew Alspaugh
  • Open Access
    Core <em>N</em>-Glycan Structures Are Critical for the Pathogenicity of <span class="named-content genus-species" id="named-content-1">Cryptococcus neoformans</span> by Modulating Host Cell Death
    Research Article | Host-Microbe Biology
    Core N-Glycan Structures Are Critical for the Pathogenicity of Cryptococcus neoformans by Modulating Host Cell Death

    We previously reported that the outer mannose chains of N-glycans are dispensable for the virulence of C. neoformans, which is in stark contrast to findings for the other human-pathogenic yeast, Candida albicans. Here, we present evidence that an intact core N-glycan structure is...

    Eun Jung Thak, Su-Bin Lee, Shengjie Xu-Vanpala, Dong-Jik Lee, Seung-Yeon Chung, Yong-Sun Bahn, Doo-Byoung Oh, Mari L. Shinohara, Hyun Ah Kang
  • Open Access
    Melanization in <span class="named-content genus-species" id="named-content-1">Cryptococcus neoformans</span> Requires Complex Regulation
    Commentary | Host-Microbe Biology
    Melanization in Cryptococcus neoformans Requires Complex Regulation

    The fungal human pathogen Cryptococcus neoformans undergoes melanization in response to nutrient starvation and exposure to exogenous melanin precursors. Melanization protects the fungus against host defense mechanisms such as oxidative damage and other environmental stressors (e.g., heat/cold stress, antimicrobial compounds, ionizing radiation).

    Radames J. B. Cordero, Emma Camacho, Arturo Casadevall
  • Open Access
    CARD9 Is Required for Classical Macrophage Activation and the Induction of Protective Immunity against Pulmonary Cryptococcosis
    Research Article | Host-Microbe Biology
    CARD9 Is Required for Classical Macrophage Activation and the Induction of Protective Immunity against Pulmonary Cryptococcosis

    Cryptococcus neoformans is a fungal pathogen that is found throughout the environment and can cause life-threatening infections of the lung and central nervous system in severely immunocompromised individuals. Caspase recruitment domain-containing protein 9 (CARD9) is a critical molecule that is activated after interactions of C-type lectin receptors (CLRs) found on...

    Althea Campuzano, Natalia Castro-Lopez, Amanda J. Martinez, Michal A. Olszewski, Anutosh Ganguly, Chrissy Leopold Wager, Chiung-Yu Hung, Floyd L. Wormley
  • Open Access
    Vomocytosis: Too Much Booze, Base, or Calcium?
    Minireview | Host-Microbe Biology
    Vomocytosis: Too Much Booze, Base, or Calcium?

    Macrophages are well known for their phagocytic activity and their role in innate immune responses. Macrophages eat non-self particles, via a variety of mechanisms, and typically break down internalized cargo into small macromolecules. However, some pathogenic agents have the ability to evade this endosomal degradation through a nonlytic exocytosis process termed vomocytosis.

    Melissa Cruz-Acuña, Noah Pacifici, Jamal S. Lewis
  • Open Access
    The Aminoalkylindole BML-190 Negatively Regulates Chitosan Synthesis via the Cyclic AMP/Protein Kinase A1 Pathway in <span class="named-content genus-species" id="named-content-1">Cryptococcus neoformans</span>
    Research Article | Therapeutics and Prevention
    The Aminoalkylindole BML-190 Negatively Regulates Chitosan Synthesis via the Cyclic AMP/Protein Kinase A1 Pathway in Cryptococcus neoformans

    Cryptococcus neoformans is a fungal pathogen that kills ∼200,000 people every year. The cell wall is an essential organelle that protects fungi from the environment. Chitosan, the deacetylated form of chitin, has been shown to be an essential component of the cryptococcal cell wall during infection of a mammalian host. In this study, we screened a set of 480 compounds...

    Brian T. Maybruck, Woei C. Lam, Charles A. Specht, Ma. Xenia G. Ilagan, Maureen J. Donlin, Jennifer K. Lodge
  • Open Access
    A Mechanosensitive Channel Governs Lipid Flippase-Mediated Echinocandin Resistance in <span class="named-content genus-species" id="named-content-1">Cryptococcus neoformans</span>
    Editor's Pick Research Article | Therapeutics and Prevention
    A Mechanosensitive Channel Governs Lipid Flippase-Mediated Echinocandin Resistance in Cryptococcus neoformans

    Cryptococcus neoformans is the leading cause of fungal meningitis, accounting for ∼15% of HIV/AIDS-related deaths, but treatment options for cryptococcosis are limited. Echinocandins are the newest fungicidal drug class introduced but are ineffective in treating cryptococcosis. Our previous study identified the lipid flippase subunit Cdc50 as a contributor to...

    Chengjun Cao, Yina Wang, Seema Husain, Patricia Soteropoulos, Chaoyang Xue

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