Identification of a cowpea γ‐thionin with bactericidal activity
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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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.”
From Structural insights into <i>Cn</i>‐AMP1, a short disulfide‐free multifunctional peptide from green coconut water (2015) · cites this paper as [33]
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Mandal, S. M., Dey, S., Mandal, M., Sarkar, S., Maria-Neto, S., & Franco, O. L. (2009) · Peptides · doi:10.1016/j.peptides.2008.12.001 · Cited by 136 · see citing works
Self-citationSantana, M. J., de Oliveira, A. L., Queiroz Júnior, L. H. K., Mandal, S. M., Matos, C. O., de O. Dias, R., Franco, O. L., & Lião, L. M. (2015) · FEBS Letters · doi:10.1016/j.febslet.2015.01.029 · Cited by 21 · see citing works
Self-citation
- 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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