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A Comprehensive Structural and Functional Analysis of Saccharomyces Killer Toxins

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Creagh, Jack W., Givens, Lily L., Reetz, David C., Coss, Sarah A., Bizarria, Rodolfo, Alias, Siti Aisyah, Rizman-Idid, Mohammed, Patel, Jagdish S., Rodrigues, Andre, Ytreberg, F. Marty, Rowley, Paul A.·2026·Toxins
DOI 10.3390/toxins18050235PMC PMC12637454

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Abstract

Antifungal killer toxins are cytotoxic proteins that have the potential to combat the growing threat of fungi to human health and agriculture. A lack of empirical tertiary structures has limited understanding of their mechanisms of action and their ability to target pathogens. In this study, AlphaFold and molecular dynamics simulations were used to generate tertiary structure models of all canonical Saccharomyces killer toxins and to place them in the context of historical empirical data. These models enabled the prediction of functional domains and posttranslational modifications, including proteolytic cleavage sites and disulfide bonds. They also revealed unexpected homology between Saccharomyces killer toxins, suggesting that all but K28 are likely ionophores. Structural homology to the well-studied killer toxins K1 and K2 enabled the prediction of the antifungal and immunity mechanisms of K1L, K21, K45, K74, and KHS. The understudied killer toxins Klus, KHR, and K62 were found to have homology to bacterial and plant toxins, including members of the aerolysin family and antifungal lectins. These structural similarities provide clues for the mechanisms of killer toxin carbohydrate binding, oligomerization, and membrane attack. This modeling approach will help guide the continued use of the model yeast S. cerevisiae to study killer toxins in the context of the wealth of functional data gathered in the decades since their first discovery.

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200 of 251 shown

Metadata

Authors
Creagh, J. W., Givens, L. L., Reetz, D. C., Coss, S. A., Bizarria, R., Alias, S. A., Rizman-Idid, M., Patel, J. S., Rodrigues, A., Ytreberg, F. M., & Rowley, P. A.
Affiliations
  • University of Idaho (US)
  • Universidade de São Paulo (BR)
  • Institute of Ocean and Earth Sciences, C308, Institute of Advanced Studies Building, Universiti Malaya, Kuala Lumpur 50603, Malaysia
  • Department of General and Applied Biology, Institute of Biosciences, São Paulo State University (UNESP), Rio Claro 13506, Brazil
ORCID
Venue
Toxins
Publisher
MDPI AG
Published
2026-05-20
Volume
18
Issue
5
Pages
235
ISSN
2072-6651 (ISSN-L)
DOI
10.3390/toxins18050235
PMC
PMC12637454
OpenAlex
W4415946291
Cited by
0
References
2
FWCI
0.00
Type
journal article
Language
en
Open access
Licence
Locations
  • Toxins (publishedVersion, cc-by)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nd)
  • PubMed (publishedVersion)
  • PubMed Central (publishedVersion, cc-by)
  • Europe PMC (PubMed Central) (submittedVersion, cc-by-nd)
Funders
  • National Science Foundation CAREER Award (2143405)
  • Hypothesis Fund
  • Fundação de Amparo à Pesquisa do Estado de São Paulo (2019/24412–2, 2021/09980–4, 2019/03746–0)
  • Conselho Nacional de Desenvolvimento Científico e Tecnológico (305269/2018–6, 142396/2019–2)
  • University of Idaho
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
  • Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
Keywords
antifungal proteins, ionophores, disulfide bond prediction, proteolytic cleavage sites, toxin oligomerization, carbohydrate binding, fungal pathogen control, Saccharomyces cerevisiae

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