ArticleAntimicrobial agents and chemotherapy2007
Global phenotype screening and transcript analysis outlines the inhibitory mode(s) of action of two amphibian-derived, alpha-helical, cationic peptides on Saccharomyces cerevisiae.
Article in Antimicrobial agents and chemotherapy, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 33 citations in OpenAlex.
- Anti-Cariogenic Effects ofPharmaceutics · 2024Article
- Membrane-Interacting Antifungal Peptides.Frontiers in cell and developmental biology · 2021Review
- Antimicrobial peptides - Advances in development of therapeutic applications.Life sciences · 2020Review
- Benzoquinone alters the lipid homeostasis inToxicology research · 2019Article
- Antimicrobial Peptide Potency is Facilitated by Greater Conformational Flexibility when Binding to Gram-negative Bacterial Inner Membranes.Scientific reports · 2016Article
- Synthetically modified L-histidine-rich peptidomimetics exhibit potent activity against Cryptococcus neoformans.Bioorganic & medicinal chemistry letters · 2014Article
- Combined systems approaches reveal highly plastic responses to antimicrobial peptide challenge in Escherichia coli.PLoS pathogens · 2014Article
- Defensins: antifungal lessons from eukaryotes.Frontiers in microbiology · 2014Review
- Endocytosis-mediated vacuolar accumulation of the human ApoE apolipoprotein-derived ApoEdpL-W antimicrobial peptide contributes to its antifungal activity in Candida albicans.Antimicrobial agents and chemotherapy · 2011Article
- A genomic approach highlights common and diverse effects and determinants of susceptibility on the yeast Saccharomyces cerevisiae exposed to distinct antimicrobial peptides.BMC microbiology · 2010Article
- Antimicrobial peptide MUC7 12-mer activates the calcium/calcineurin pathway in Candida albicans.FEMS yeast research · 2010Article
- Peptide-based Antifungal Therapies against Emerging Infections.Drugs of the future · 2010Article
- Soft X-ray tomography of phenotypic switching and the cellular response to antifungal peptoids in Candida albicans.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Exploring the mode of action of antimicrobial peptide MUC7 12-mer by fitness profiling of Saccharomyces cerevisiae genomewide mutant collection.Antimicrobial agents and chemotherapy · 2009Article
- The antimalarial drug quinine disrupts Tat2p-mediated tryptophan transport and causes tryptophan starvation.The Journal of biological chemistry · 2009Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Dermaseptin S3(1-16) [DsS3(1-16)] and magainin 2 (Mag 2) are two unrelated, amphibian-derived cationic peptides that adopt an alpha-helical structure within microbial membranes and have been proposed to kill target organisms via membrane disruption. Using a combination of global deletion mutant library phenotypic screening, expression profiling, and physical techniques, we have carried out a comprehensive in vitro analysis of the inhibitory action of these two peptides on the model fungus Saccharomyces cerevisiae. Gene ontology profiling (of biological processes) was used to identify both common and unique effects of each peptide. Resistance to both peptides was conferred by genes involved in telomere maintenance, chromosome organization, and double-strand break repair, implicating a common inhibitory action of DNA damage. Crucially, each peptide also required unique genes for maintaining resistance; for example, DsS3(1-16) required genes involved in protein targeting to the vacuole, and Mag 2 required genes involved in DNA-dependent DNA replication and DNA repair. Thus, DsS3(1-16) and Mag 2 have both common and unique antifungal actions that are not simply due to membrane disruption. Physical techniques revealed that both peptides interacted with DNA in vitro but in subtly different ways, and this observation was supported by the functional genomics experiments that provided evidence that both peptides also interfered with DNA integrity differently in vivo. This implies that both peptides are able to pass through the cytoplasmic membrane of yeast cells and damage DNA, an inhibitory action that has not been previously attributed to either of these peptides.
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