ArticlePlant & cell physiology2004
Pn-AMP1, a plant defense protein, induces actin depolarization in yeasts.
Article in Plant & cell physiology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
18 citing papers in PubMed, 62 citations in OpenAlex.
- Antimicrobial peptides: An important link in the game theory between plants and pathogens.Journal of advanced research · 2026Review
- Production, Delivery, and Regulatory Aspects for Application of Plant-Based Anti-microbial Peptides: a Comprehensive Review.Probiotics and antimicrobial proteins · 2025Review
- Plant Defense Peptides: Exploring the Structure-Function Correlation for Potential Applications in Drug Design and Therapeutics.ACS omega · 2025Review
- Candida albicans and Antifungal Peptides.Infectious diseases and therapy · 2023Article
- Plant Antimicrobial Peptides: Insights into Structure-Function Relationships for Practical Applications.Current issues in molecular biology · 2023Review
- Short Peptides Make a Big Difference: The Role of Botany-Derived AMPs in Disease Control and Protection of Human Health.International journal of molecular sciences · 2021Review
- The interaction Between Carbohydrates and the Antimicrobial Peptide P-113Tri is Involved in the Killing ofMicroorganisms · 2020Article
- The interaction with fungal cell wall polysaccharides determines the salt tolerance of antifungal plant defensins.Cell surface (Amsterdam, Netherlands) · 2019Article
- Potent in vitro and in vivo antifungal activity of a small molecule host defense peptide mimic through a membrane-active mechanism.Scientific reports · 2017Article
- Article
- Plant Defensins NaD1 and NaD2 Induce Different Stress Response Pathways in Fungi.International journal of molecular sciences · 2016Article
- The Penicillium digitatum protein O-mannosyltransferase Pmt2 is required for cell wall integrity, conidiogenesis, virulence and sensitivity to the antifungal peptide PAF26.Molecular plant pathology · 2015Article
- Activation of stress signalling pathways enhances tolerance of fungi to chemical fungicides and antifungal proteins.Cellular and molecular life sciences : CMLS · 2014Review
- FLO11 Gene Is Involved in the Interaction of Flor Strains of Saccharomyces cerevisiae with a Biofilm-Promoting Synthetic Hexapeptide.Applied and environmental microbiology · 2013Article
- Properties and mechanisms of action of naturally occurring antifungal peptides.Cellular and molecular life sciences : CMLS · 2013Review
- Multifunctional cationic host defence peptides and their clinical applications.Cellular and molecular life sciences : CMLS · 2011Review
- 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
- Peptide antimicrobial agents.Clinical microbiology reviews · 2006Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors at 2 institutions in 1 country.
Funding
Abstract
Pn-AMP1, Pharbitis nil antimicrobial peptide 1, is a small cysteine-rich peptide implicated in host-plant defense. We show here that Pn-AMP1 causes depolarization of the actin cytoskeleton in Saccharomyces cerevisiae and Candida albicans. Pn-AMP1 induces rapid depolarization of actin cables and patches within 15 min. Increased osmolarity or temperature induces transient actin depolarization and results in increased sensitivity to Pn-AMP1, while cells conditioned to these stresses show less sensitivity. Mutations in components of a cell wall integrity pathway (Wsc1p, Rom2p, Bck1p and Mpk1p), which regulate actin repolarization, result in increased sensitivity to Pn-AMP1. A genetic screen reveals that mutations in components of the alpha-1,6-mannosyltransferase complex (Mnn10p, Mnn11p and Och1p), which regulate mannosylation of cell wall proteins, confer resistance to Pn-AMP1. FITC-conjugated Pn-AMP1 localizes to the outer surface of the cell with no significant staining observed in spheroplasts. Taken together, these results indicate that cell wall proteins are determinants of resistance to Pn-AMP1, and the ability of a plant defense protein to induce actin depolarization is important for its antifungal activity.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.