A fungal ubiquitin ligase and arrestin binding partner contribute to pathogenesis and survival during cellular stress
Microbial proteins involved in human infectious diseases often need to be modified by specific chemical additions to be fully functional. Here, we explore the role of a particular protein modification, ubiquitination, in infections due to the human fungal pathogen <i>Cryptococcus neoformans</i>. We identified a complex of proteins responsible for adding ubiquitin groups to fungal proteins, and this complex is required for virulence. These proteins are fungal specific and might be targets for novel anti-infection therapy.
Authors
- Natalia Castro-Lopez (ORCID: https://orcid.org/0000-0002-8371-3350)
- Corinna Probst (ORCID: https://orcid.org/0000-0002-1154-5116)
- Connie B. Nichols (ORCID: https://orcid.org/0000-0003-0092-0192)
- J. Andrew Alspaugh (ORCID: https://orcid.org/0000-0003-3009-627X)
- Calla L. Telzrow (ORCID: https://orcid.org/0000-0003-2686-5726)
- Floyd L. Wormley (ORCID: https://orcid.org/0000-0001-9290-3925)
- Lukas M. du Plooy (ORCID: https://orcid.org/0000-0002-5038-4407)
Institutions
- Texas Christian University (US)
- Duke University (US)
- The University of Texas at San Antonio (US)
Publication Details
- Journal
- mBio
- Published
- 2024-09-05
- DOI
- https://doi.org/10.1128/mbio.00981-24
- Citations
- 4
- Primary Topic
- Fungal Infections and Studies
- Type
- article
- Field-Weighted Citation Impact
- 1.55
Funders
- National Research Foundation
- National Institutes of Health
- School of Medicine, Duke University
- National Institute of Allergy and Infectious Diseases
- Duke Cancer Institute