ArticleVirulence2019
A unique aspartyl protease gene expansion in Talaromyces marneffei plays a role in growth inside host phagocytes.
Article in Virulence, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 14 citations in OpenAlex.
- Glutathione Peroxidase fromInternational journal of molecular sciences · 2026Article
- Aspartic Proteases Drive Stress Response, Morphogenesis, and Macrophage Interaction in Sporothrix brasiliensis.Mycopathologia · 2025Article
- Disseminated Talaromyces marneffei infection mimicking tuberculosis in an HIV-negative adult with anti-IFN-γ autoantibodies: a case report.BMC infectious diseases · 2025Article
- The dimorphic fungus Talaromyces marneffei: An opportunistic killer in Southeast Asia.PLoS pathogens · 2025Article
- Unraveling the dynamic transcriptomic changes during the dimorphic transition ofFrontiers in microbiology · 2024Article
- An Overview of Diagnostic and Management Strategies for Talaromycosis, an Underrated Disease.Journal of fungi (Basel, Switzerland) · 2023Review
- An Overlooked and Underrated Endemic Mycosis-Talaromycosis and the Pathogenic Fungus Talaromyces marneffei.Clinical microbiology reviews · 2023Review
- Characterization of Aspartic Proteases fromJournal of fungi (Basel, Switzerland) · 2023Article
- Extracellular vesicles derived fromFrontiers in immunology · 2023Article
- The Effect ofInfection and drug resistance · 2021Article
- Bioinformatic analysis of the pathogenic mechanism of talaromyces marneffei infection.Medicine · 2020Article
- Sixty Years from Segretain's Description: What Have We Learned and Should Learn About the Basic Mycology of Talaromyces marneffei?Mycopathologia · 2019Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aspartyl proteases are a widely represented class of proteolytic enzymes found in eukaryotes and retroviruses. They have been associated with pathogenicity in a range of disease-causing microorganisms. The dimorphic human-pathogenic fungus Talaromyces marneffei has a large expansion of these proteases identified through genomic analyses. Here we characterize the expansion of these genes (pop - paralogue of pep) and their role in T. marneffei using computational and molecular approaches. Many of the genes in this monophyletic family show copy number variation and positive selection despite the preservation of functional regions and possible redundancy. We show that the expression profile of these genes differs and some are expressed during intracellular growth in the host. Several of these proteins have distinctive localization as well as both additive and epistatic effects on the formation of yeast cells during macrophage infections. The data suggest that this is a recently evolved aspartyl protease gene family which affects intracellular growth and contributes to the pathogenicity of T. marneffei.
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