Biotechnological applications of versatile plant lipid transfer proteins (LTPs)
- PMID: 33746031
- DOI: 10.1016/j.peptides.2021.170531
Biotechnological applications of versatile plant lipid transfer proteins (LTPs)
Abstract
Plant AMPs are usually cysteine-rich, and can be classified in several classes, including lipid transfer proteins (LTPs). LTPs are small plant cationic peptides, and can be classified in two subclasses, LTP1 (9-10 kDa) and LTP2 (7 kDa). They have been identified and isolated from various plant species and can be involved in a number of processes, including responses against several phytopathogens. LTP1 presents 4 parallel α- helices and a 310-helix fragment. These structures form a tunnel with large and small entrances. LTP2 presents 3 parallel α- helices, which form a cavity with triangular structure. Both LTP subclasses present a hydrophobic cavity, which makes interaction with different lipids and general hydrophobic molecules possible. Several studies report a broad spectrum of activity of plant LTPs, including antibacterial, antifungal, antiviral, antitumoral, and insecticidal activity. Thus, these molecules can be employed in human and animal health as an alternative to the conventional treatment of disease, well as providing the source of novel drugs. However, employing peptides in human health can present challenges, such as the toxicity of peptides, the difference between the results found in in vitro assays and in pre-clinical or clinical tests and their low efficiency against Gram-negative bacteria. In this context, plant LTPs can be an interesting alternative means by which to bypass such challenges. This review addresses the versatility of plant LTPs, their broad spectrum of activities and their potential applications in human and animal health and in agricultural production, and examines challenges in their biotechnological application.
Keywords: Antifungal activity; Antimicrobial activity; Antitumoral activity; Antiviral activity; Inhibitor of digestive enzymes; Lipid transfer proteins; Plant antimicrobial peptide.
Copyright © 2021 Elsevier Inc. All rights reserved.
Similar articles
-
A novel lipid transfer protein from the pea Pisum sativum: isolation, recombinant expression, solution structure, antifungal activity, lipid binding, and allergenic properties.BMC Plant Biol. 2016 Apr 30;16:107. doi: 10.1186/s12870-016-0792-6. BMC Plant Biol. 2016. PMID: 27137920 Free PMC article.
-
A multifaceted study of stigma/style cysteine-rich adhesin (SCA)-like Arabidopsis lipid transfer proteins (LTPs) suggests diversified roles for these LTPs in plant growth and reproduction.J Exp Bot. 2010 Oct;61(15):4277-90. doi: 10.1093/jxb/erq228. Epub 2010 Jul 28. J Exp Bot. 2010. PMID: 20667964 Free PMC article.
-
Homology modelling of an antimicrobial protein, Ace-AMP1, from lipid transfer protein structures.Fold Des. 1997;2(3):183-92. doi: 10.1016/s1359-0278(97)00025-4. Fold Des. 1997. PMID: 9218956
-
Plant lipid transfer proteins: are we finally closing in on the roles of these enigmatic proteins?J Lipid Res. 2018 Aug;59(8):1374-1382. doi: 10.1194/jlr.R083139. Epub 2018 Mar 19. J Lipid Res. 2018. PMID: 29555656 Free PMC article. Review.
-
The biochemistry and biology of extracellular plant lipid-transfer proteins (LTPs).Protein Sci. 2008 Feb;17(2):191-8. doi: 10.1110/ps.073300108. Epub 2007 Dec 20. Protein Sci. 2008. PMID: 18096636 Free PMC article. Review.
Cited by
-
Identification of potato Lipid transfer protein gene family and expression verification of drought genes StLTP1 and StLTP7.Plant Direct. 2023 Mar 27;7(3):e491. doi: 10.1002/pld3.491. eCollection 2023 Mar. Plant Direct. 2023. PMID: 36993902 Free PMC article.
-
Plant-Derived Antimicrobial Peptides as Potential Antiviral Agents in Systemic Viral Infections.Pharmaceuticals (Basel). 2021 Aug 6;14(8):774. doi: 10.3390/ph14080774. Pharmaceuticals (Basel). 2021. PMID: 34451871 Free PMC article. Review.
-
Antifungal Action of Arabidopsis thaliana TCP21 via Induction of Oxidative Stress and Apoptosis.Antioxidants (Basel). 2023 Sep 15;12(9):1767. doi: 10.3390/antiox12091767. Antioxidants (Basel). 2023. PMID: 37760070 Free PMC article.
-
Plant Antimicrobial Peptides and Their Main Families and Roles: A Review of the Literature.Curr Issues Mol Biol. 2024 Dec 24;47(1):1. doi: 10.3390/cimb47010001. Curr Issues Mol Biol. 2024. PMID: 39852116 Free PMC article. Review.
-
Potent Antifungal Functions of a Living Modified Organism Protein, CP4-EPSPS, against Pathogenic Fungal Cells.Molecules. 2023 May 24;28(11):4289. doi: 10.3390/molecules28114289. Molecules. 2023. PMID: 37298765 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources