Cited by 103Antimicrobial Peptides and ActivitiesPlant-Microbe Interactions and ImmunityAntimicrobial agents and applications

Identification of a cowpea γ‐thionin with bactericidal activity

Franco, Octávio L., Murad, Andre M., Leite, José R., Mendes, Paulo A. M., Prates, Maura V., Bloch, Carlos·2006·The FEBS Journal

Abstract

Antimicrobial peptides are an abundant group of proteinaceous compounds widely produced in the plant kingdom. Among them, the γ‐thionin family, also known as plant defensins, represents one typical family and comprises low molecular mass cysteine‐rich proteins, usually cationic and distributed in different plant tissues. Here, we report the purification and characterization of a novel γ‐thionin from cowpea seeds (Vigna unguiculata), named Cp‐thionin II, with bactericidal activity against Gram‐positive and Gram‐negative bacteria. Once the primary structure was elucidated, molecular modelling experiments were used to investigate the multimerization and mechanism of action of plant γ‐thionins. Furthermore, Cp‐thionin II was also localized in different tissues in cowpea seedlings during germination in contrasting conditions, to better understand the plant protection processes. The use of plant defensins in the construction of transgenic plants and also in the production of novel drugs with activity against human pathogens is discussed.

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Crossref · 10.1111/j.1742-4658.2006.05349.x

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  • Some antimicrobial peptide classes, such as human alpha-defensins and plant gamma-defensins, need arginines exposed on the peptide surface, and their removal or substitution reduced bacterial killing activity.

    “It has been demonstrated that some antimicrobial peptide classes, such as human a-defensins [32] and plant c-defensins [33], need arginines exposed on the peptide surface and their removal or substitution reduced bacterial killing activity.”

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Authors
Franco, O. L., Murad, A. M., Leite, J. R., Mendes, P. A. M., Prates, M. V., & Bloch, C.
Affiliations
  • Universidade Católica de Brasília (BR)
  • Embrapa (BR)
Venue
The FEBS Journal
Publisher
Wiley
Published
2006-07-17
Volume
273
Issue
15
Pages
3489-3497
ISSN
  • 1742-464X (ISSN-L)
  • 1742-4658
OpenAlex
W2079637435
Cited by
103
References
0
Citations by year
2026: 2 · 2025: 6 · 2024: 4 · 2023: 4 · 2022: 3 · 2021: 4 · 2020: 5 · 2019: 8 · 2018: 6 · 2017: 5 · 2016: 2 · 2015: 7 · 2014: 9 · 2013: 5 · 2012: 5
FWCI
3.54
Type
journal article
Language
en
Open access
closed
Locations
  • FEBS Journal (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
  • Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant-Microbe Interactions and Immunity
  • Physical Sciences › Chemistry › Organic Chemistry › Antimicrobial agents and applications
Keywords
plant defensins, antimicrobial peptides, cowpea, bactericidal activity, cysteine-rich proteins, protein oligomerization, seed germination, transgenic plants
MeSH terms
Amino Acid Sequence, Anti-Bacterial Agents, Gram-Negative Bacteria, Gram-Positive Bacteria, Microbial Sensitivity Tests, Molecular Sequence Data, Sequence Homology, Amino Acid, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Antimicrobial Cationic Peptides, Phaseolus

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