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Isolation and characterization of a novel class of plant antimicrobial peptides form Mirabilis jalapa L. seeds.

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Cammue, B P, De Bolle, M F, Terras, F R, Proost, P, Van Damme, J, Rees, S B, Vanderleyden, J, Broekaert, W F·1992·Journal of Biological Chemistry

Abstract

We have isolated from seeds of Mirabilis jalapa L. two antimicrobial peptides, designated Mj-AMP1 and Mj-AMP2, respectively. These peptides are highly basic and consist of 37 and 36 residues for Mj-AMP1 and Mj-AMP2, respectively. Both peptides contain three disulfide bridges and differ from one another only by 4 amino acids. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis of the reduced and unreduced peptides suggests that the peptides associate into dimers in their native form. The Mj-AMPs exhibit a broad spectrum of antifungal activity since they are active against all 13 tested plant pathogenic fungi. Concentrations required for 50% inhibition of fungal growth vary from 6 to 300 micrograms/ml for Mj-AMP1 and from 0.5 to 20 micrograms/ml for Mj-AMP2. These peptides were also active on two tested Gram-positive bacteria but were apparently nontoxic for Gram-negative bacteria and cultured human cells. Although the Mj-AMPs show sequence similarity to mu-agatoxins, a class of insecticidal neurotoxic peptides isolated from the venom of spiders, they do not affect pulse transmission in insect nerves.

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Metadata

Authors
Cammue, B. P., De Bolle, M. F., Terras, F. R., Proost, P., Van Damme, J., Rees, S. B., Vanderleyden, J., & Broekaert, W. F.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1992-02
Volume
267
Issue
4
Pages
2228-2233
ISSN
0021-9258 (ISSN-L)
OpenAlex
W2121156875
Cited by
303
References
0
FWCI
9.80
Type
journal article
Language
en
Open access
hybrid

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Cammue, B. P., De Bolle, M. F., Terras, F. R., Proost, P., Van Damme, J., Rees, S. B., Vanderleyden, J., & Broekaert, W. F. (1992). Isolation and characterization of a novel class of plant antimicrobial peptides form Mirabilis jalapa L. seeds. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)45866-8

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