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Antifungal activity of C3a and C3a-derived peptides against Candida
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Pharmacy.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Pharmacy.
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2007 (English)In: Biochimica et Biophysica Acta - Biomembranes, ISSN 0005-2736, E-ISSN 1879-2642, Vol. 1768, no 2, 346-353 p.Article in journal (Refereed) Published
Abstract [en]

Antimicrobial peptides are generated during activation of the complement system [Nordahl et al. Proc. Natl. Acad. Sci. U. S. A. 2004, 101:16879-16884]. Here we show that the anaphylatoxin C3a exerts antimicrobial effects against the yeast Candida. Fluorescence microscopy and electron microscopy analysis demonstrated that C3a-derived peptides bound to the cell surface of Candida, and induced membrane perturbations and release of extracellular material. Various Candida isolates were found to induce complement degradation, leading to generation of C3a. Arginine residues were found to be critical for the antifungal and membrane breaking activity of a C3a-derived antimicrobial peptide, CNY21 (C3a; Cys57–Arg77). A CNY21 variant with increased positive net charge displayed enhanced antifungal activity. Thus, C3a-derived peptides can be utilized as templates in the development of peptide-based antifungal therapies.

Place, publisher, year, edition, pages
2007. Vol. 1768, no 2, 346-353 p.
Keyword [en]
Amino Acid Sequence, Antifungal Agents/*pharmacology, Antimicrobial Cationic Peptides/*pharmacology, Candida albicans/*drug effects, Complement C3a/*pharmacology, Humans, Liposomes, Microbial Sensitivity Tests, Molecular Sequence Data
National Category
Pharmaceutical Sciences Medical and Health Sciences Biological Sciences
URN: urn:nbn:se:uu:diva-10438DOI: 10.1016/j.bbamem.2006.10.017ISI: 000244384600017PubMedID: 17169328OAI: oai:DiVA.org:uu-10438DiVA: diva2:38206
Available from: 2007-03-23 Created: 2007-03-23 Last updated: 2011-02-15Bibliographically approved

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Ringstad, LovisaMalmsten, Martin
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