Two hevein homologs isolated from the seed of Pharbitis nil L. exhibit potent antifungal activity

Ja Choon Koo, So Young Lee, Hyun Jin Chun, Yong Hwa Cheong, Jae Su Choi, Shun Ichiro Kawabata, Masaru Miyagi, Susumu Tsunasawa, Kwon Soo Ha, Dong Won Bae, Chang Deok Han, Bok Luel Lee, Moo Je Cho

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Abstract

Two antifungal peptides (Pn-AMP1 and Pn-AMP2) have been purified to homogeneity from seeds of Pharbitis nil. The amino acid sequences of Pn- AMP11 (41 amino acid0 residues) and Pn-AMP2 (40 amino acid residues) were identical except that Pn-AMP1 has an additional serine residue at the carboxyl-terminus. The molecular masses of Pn-AMP1 and Pn-AMP2 were confirmed as 4299.7 and 4213.2 Da, respectively. Both the Pn-AMPs were highly basic (pI 12.02) and had characteristics of cysteine/glycine rich chitin-binding domain. Pn-AMPs exhibited potent antifungal activity against both chitin- containing and non-chitin-containing fungi in the cell wall. Concentrations required for 50% inhibition of fungal growth were ranged from 3 to 26 μg/ml for Pn-AMP1 and from 0.6 to 75 μg/ml for Pn-AMP2. The Pn-AMPs penetrated very rapidly into fungal hyphae and localized at septum and hyphal tips of fungi, which caused burst of hyphal tips. Burst of hyphae resulted in disruption of the fungal membrane and leakage of the cytoplasmic materials to our knowledge, Pn-AMPs are the first herein-like proteins that show similar fungicidal effects as thionins do.

Original languageEnglish
Pages (from-to)80-90
Number of pages11
JournalBiochimica et Biophysica Acta - Protein Structure and Molecular Enzymology
Volume1382
Issue number1
DOIs
Publication statusPublished - Jan 15 1998

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology

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    Koo, J. C., Lee, S. Y., Chun, H. J., Cheong, Y. H., Choi, J. S., Kawabata, S. I., Miyagi, M., Tsunasawa, S., Ha, K. S., Bae, D. W., Han, C. D., Lee, B. L., & Cho, M. J. (1998). Two hevein homologs isolated from the seed of Pharbitis nil L. exhibit potent antifungal activity. Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology, 1382(1), 80-90. https://doi.org/10.1016/S0167-4838(97)00148-9