The chitin‐binding capability of Cy‐AMP1 from cycad is essential to antifungal activity |
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| Authors: | Seiya Yokoyama Yuto Iida Yousuke Kawasaki Yuji Minami Keiichi Watanabe Fumio Yagi |
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| Affiliation: | 1. Department of Applied Biological Chemistry, The United Graduate School of Agricultural Sciences, Kagoshima University, 1‐21‐24, Korimoto, Kagoshima, 890‐0065, Japan;2. Department of Biochemical Science and Technology, Faculty of Agriculture, Kagoshima University, 1‐21‐24, Korimoto, Kagoshima, 890‐0065, Japan;3. Department of Applied Biological Sciences, Faculty of Agriculture, Saga University, Honjo‐machi, Saga 840‐8502, Japan |
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| Abstract: | Antimicrobial peptides are important components of the host innate immune responses by exerting broad‐spectrum microbicidal activity against pathogenic microbes. Cy‐AMP1 found in the cycad (Cycas revoluta) seeds has chitin‐binding ability, and the chitin‐binding domain was conserved in knottin‐type and hevein‐type antimicrobial peptides. The recombinant Cy‐AMP1 was expressed in Escherichia coli and purified to study the role of chitin‐binding domain. The mutants of Cy‐AMP1 lost chitin‐binding ability completely, and its antifungal activity was markedly decreased in comparison with native Cy‐AMP1. However, the antimicrobial activities of the mutant peptides are nearly identical to that of native one. It was suggested that the chitin‐binding domain plays an essential role in antifungal, but not antimicrobial, activity of Cy‐AMP1. Copyright © 2009 European Peptide Society and John Wiley & Sons, Ltd. |
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| Keywords: | cycad antimicrobial peptide chitin‐binding capability pGEX‐4T1 vector CD spectrum antimicrobial activity antifungal activity |
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