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

研究成果: ジャーナルへの寄稿記事

106 引用 (Scopus)

抄録

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.

元の言語英語
ページ(範囲)80-90
ページ数11
ジャーナルBiochimica et Biophysica Acta - Protein Structure and Molecular Enzymology
1382
発行部数1
DOI
出版物ステータス出版済み - 1 15 1998

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Ipomoea nil
Adenosine Monophosphate
Seed
Seeds
Chitin
Hyphae
Fungi
Thionins
Amino Acids
Molecular mass
Glycine
Cell Wall
Serine
Cysteine
Amino Acid Sequence
Cells
Cell Membrane
Membranes
Peptides
hevein

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Biophysics
  • Biochemistry
  • Molecular Biology

これを引用

Two hevein homologs isolated from the seed of Pharbitis nil L. exhibit potent antifungal activity. / Koo, Ja Choon; Lee, So Young; Chun, Hyun Jin; Cheong, Yong Hwa; Choi, Jae Su; Kawabata, Shun-Ichiro; Miyagi, Masaru; Tsunasawa, Susumu; Ha, Kwon Soo; Bae, Dong Won; Han, Chang Deok; Lee, Bok Luel; Cho, Moo Je.

:: Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology, 巻 1382, 番号 1, 15.01.1998, p. 80-90.

研究成果: ジャーナルへの寄稿記事

Koo, JC, Lee, SY, Chun, HJ, Cheong, YH, Choi, JS, Kawabata, S-I, Miyagi, M, Tsunasawa, S, Ha, KS, Bae, DW, Han, CD, Lee, BL & Cho, MJ 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, 巻. 1382, 番号 1, pp. 80-90. https://doi.org/10.1016/S0167-4838(97)00148-9
Koo, Ja Choon ; Lee, So Young ; Chun, Hyun Jin ; Cheong, Yong Hwa ; Choi, Jae Su ; Kawabata, Shun-Ichiro ; Miyagi, Masaru ; Tsunasawa, Susumu ; Ha, Kwon Soo ; Bae, Dong Won ; Han, Chang Deok ; Lee, Bok Luel ; Cho, Moo Je. / Two hevein homologs isolated from the seed of Pharbitis nil L. exhibit potent antifungal activity. :: Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology. 1998 ; 巻 1382, 番号 1. pp. 80-90.
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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.",
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