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Thaumatin-like Proteins in Legumes: Functions and Potential Applications—A Review

Feng, Lanlan, Wei, Shaowei, Li, Yin·2024·Plants
DOI 10.3390/plants13081124PMC PMC11055134
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Abstract

Thaumatin-like proteins (TLPs) comprise a complex and evolutionarily conserved protein family that participates in host defense and several developmental processes in plants, fungi, and animals. Importantly, TLPs are plant host defense proteins that belong to pathogenesis-related family 5 (PR-5), and growing evidence has demonstrated that they are involved in resistance to a variety of fungal diseases in many crop plants, particularly legumes. Nonetheless, the roles and underlying mechanisms of the TLP family in legumes remain unclear. The present review summarizes recent advances related to the classification, structure, and host resistance of legume TLPs to biotic and abiotic stresses; analyzes and predicts possible protein–protein interactions; and presents their roles in phytohormone response, root nodule formation, and symbiosis. The characteristics of TLPs provide them with broad prospects for plant breeding and other uses. Searching for legume TLP genetic resources and functional genes, and further research on their precise function mechanisms are necessary.

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Figure 1 The protein structure of AhTLP1. (A) The protein structure and eight disulfide bonds of AhTLP (http://www.ebi.ac.uk./interpro/, accessed on 28 March 2024; http://prosite.expasy.org/, accessed on 28 March 2024). TM: transmembrane helix; SP: signal peptide; N: N-terminal; C: C-terminal; c: conserved cysteine involved in a disulfide bond. (B) Three-dimensional structure of AhTLP1 and thaumatin. The TLP protein family contains three conserved domains: domain I, containing 11 stranded β-sheets organized as a β-barrel, forming the protein core; domain II, containing an α-helix and a set of disulfide-rich loops (green balls); and domain III, containing a β-hairpin and a coil motif, both maintained by a disulfide bond. This image was generated with PyMOL Molecular Graphics System version 2.2.0 (Schrödinger, LLC, https://pymol.org).
Figure 1 The protein structure of AhTLP1. (A) The protein structure and eight disulfide bonds of AhTLP (http://www.ebi.ac.uk./interpro/, accessed on 28 March 2024; http://prosite.expasy.org/, accessed on 28 March 2024). TM: transmembrane helix; SP: signal peptide; N: N-terminal; C: C-terminal; c: conserved cysteine involved in a disulfide bond. (B) Three-dimensional structure of AhTLP1 and thaumatin. The TLP protein family contains three conserved domains: domain I, containing 11 stranded β-sheets organized as a β-barrel, forming the protein core; domain II, containing an α-helix and a set of disulfide-rich loops (green balls); and domain III, containing a β-hairpin and a coil motif, both maintained by a disulfide bond. This image was generated with PyMOL Molecular Graphics System version 2.2.0 (Schrödinger, LLC, https://pymol.org).CC BY · PubMed Central
Figure 2 Plant defense mechanisms of TLPs. Plants respond to biotic and abiotic stresses through several pathways. Under stress conditions, metabolic changes and systemic acquired resistance (SAR) are quickly stimulated and initiate the expression of PR proteins, including PR5. TLPs are PR5 members, multifunctional proteins that exhibit antifungal activity, glucan-binding activity, glucanase activity, xylanase inhibitor abilities, cytokinin-binding abilities, and actin-binding abilities. TLPs contain three domains: I, II, and III. N: N-terminal, C: C-terminal.
Figure 2 Plant defense mechanisms of TLPs. Plants respond to biotic and abiotic stresses through several pathways. Under stress conditions, metabolic changes and systemic acquired resistance (SAR) are quickly stimulated and initiate the expression of PR proteins, including PR5. TLPs are PR5 members, multifunctional proteins that exhibit antifungal activity, glucan-binding activity, glucanase activity, xylanase inhibitor abilities, cytokinin-binding abilities, and actin-binding abilities. TLPs contain three domains: I, II, and III. N: N-terminal, C: C-terminal.CC BY · PubMed Central
Figure 3 Protein–protein interaction predictions for Arachis hypogaea TLP1 analyzed using STRING. A0A444WUM6: AhTLP1, Arachis hypogaea TLP1; KEGG: Kyoto Encyclopedia of Genes and Genomes. The thickness of the line indicates the degree of confidence prediction of the interaction.
Figure 3 Protein–protein interaction predictions for Arachis hypogaea TLP1 analyzed using STRING. A0A444WUM6: AhTLP1, Arachis hypogaea TLP1; KEGG: Kyoto Encyclopedia of Genes and Genomes. The thickness of the line indicates the degree of confidence prediction of the interaction.CC BY · PubMed Central
Figure 4 Protein–protein interaction predictions for Glycine max GmOLPa and GmOLPb analyzed using STRING. (A) STRING analysis of GmOLPa; (B) STRING analysis of GmOLPb. The thickness of the line indicates the degree of confidence prediction of the interaction.
Figure 4 Protein–protein interaction predictions for Glycine max GmOLPa and GmOLPb analyzed using STRING. (A) STRING analysis of GmOLPa; (B) STRING analysis of GmOLPb. The thickness of the line indicates the degree of confidence prediction of the interaction.CC BY · PubMed Central

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Metadata

Authors
Feng, L., Wei, S., & Li, Y.
Venue
Plants
Publisher
MDPI AG
Published
2024-04-17
Volume
13
Issue
8
Pages
1124
ISSN
2223-7747
DOI
10.3390/plants13081124
PMC
PMC11055134
Cited by
37
References
1
Language
en
Licence
creativecommons.org/licenses/by/4.0/ (vor)
Funders
  • National Natural Science Foundation of China (31171625, 2020A1414040005, 2021A1515110341)
  • Science and Technology Planning Project of Guangdong Province, China (31171625, 2020A1414040005, 2021A1515110341)
  • Guangdong Basic and Applied Basic Research Foundation, China (31171625, 2020A1414040005, 2021A1515110341)

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This page
CoChat. (2026). Citation check: Thaumatin-like Proteins in Legumes: Functions and Potential Applications—A Review. https://app.cochat.ai/papers/10.3390/plants13081124
The paper
Feng, L., Wei, S., & Li, Y. (2024). Thaumatin-like Proteins in Legumes: Functions and Potential Applications—A Review. Plants. https://doi.org/10.3390/plants13081124