Molecular characterization of a cDNA for a cysteine-rich antifungal protein from<Emphasis Type="Italic">Capsicum annuum</Emphasis> |
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Authors: | Yeon?Mi?Lee Hyoung?Suk?Wee Il-Pyung?Ahn Yong-Hwan?Lee Email author" target="_blank">Chung?Sun?AnEmail author |
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Institution: | (1) Department of Biological Sciences, Seoul National University, 151-742 Seoul, Korea;(2) School of Agricultural Biotechnology and Center for Agricultural Biomaterials, Seoul National University, 151-742 Seoul, Korea |
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Abstract: | We have isolated a cDNA clone for the antifungal protein,CaAFP, from hot pepper,Capsicum annuum L. Its open reading frame encodes 85 amino acids, including 8 cysteine residues. CaAFP consists of three domains: a signal
peptide, a chitin-binding domain, and a C-terminal peptide domain. The deduced amino acid sequence of the chitin-binding domain
shows 92% and 85% similarity to the same domain from PnAMPs and hevein, respectively. Southern blot analysis indicated that
CaAFP is present as a single copy, while the northern blots revealed that the clone is highly expressed in the leaves and
flower buds, but not in the roots. However, wounding treatments and chemicals generally known to induce PR proteins did not
stimulate its expression.In situ hybridization also showed that CaAFP is expressed in the parenchyma cells of the floral sepals. As seen in our functional
analysis, this clone was expressed inEscherichia coli, and the fusion protein was purified using nickel-affinity column chromatography. This purified AFP fusion protein inhibited
spore germination and appressoria formation in several plant pathogenic fungi, includingFusarium oxisporum andColletotrichum gloeosporioides. Our results suggest CaAFP is an antifungal protein that defends developing seeds against pathogen invasion while also having
a specific biological role during floral development. |
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Keywords: | Keyword" target="_blank">Keyword antifungal Protein Capsicum annuum chitin-binding domain hevein |
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