Antifungal Plant Defensins: Mechanisms of Action  and Production

Vriens, Kim; Cammue, Bruno P. A.; Thevissen, Karin

doi:10.3390/molecules190812280

Cited by 198 publications

(173 citation statements)

References 137 publications

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“…Similar PI(4,5)P 2 -binding mechanism was also described for the tomato defensin TPP3, which binds specifically to PI(4,5)P 2 and shares the conserved cationic grip binding pocket as NaD1 to mediate cell lysis. 70 It should be noted that the cationic loop region identified as the PA binding site in MtDef4, is conserved among many plant defensins 119,120 and interestingly, the equivalent region (between β2 and β3 strands) was also found to be the PI (4,5)P 2 binding site for both NaD1 and TPP3, 69,70 indicating that this region is functionally conserved to bind phospholipid. Intriguingly, the ability of these plant innate defense molecules to induce membrane permeabilization via binding to inner membrane PI(4,5)P 2 and forming oligomers resembles the aforementioned PI(4,5)P 2 -dependent targeting and oligomerization by MLKL in mammalian cells undergoing necroptosis.…”

Section: Pathogenic Entry Via the Host Extracellular Phospholipid Codementioning

confidence: 96%

The phospholipid code: a key component of dying cell recognition, tumor progression and host–microbe interactions

2015

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A significant effort is made by the cell to maintain certain phospholipids at specific sites. It is well described that proteins involved in intracellular signaling can be targeted to the plasma membrane and organelles through phospholipid-binding domains. Thus, the accumulation of a specific combination of phospholipids, denoted here as the 'phospholipid code', is key in initiating cellular processes. Interestingly, a variety of extracellular proteins and pathogen-derived proteins can also recognize or modify phospholipids to facilitate the recognition of dying cells, tumorigenesis and host-microbe interactions. In this article, we discuss the importance of the phospholipid code in a range of physiological and pathological processes.

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Section: Pathogenic Entry Via the Host Extracellular Phospholipid Codementioning

confidence: 96%

The phospholipid code: a key component of dying cell recognition, tumor progression and host–microbe interactions

2015

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“…Each Cys-rich peptide class has a characteristic number and linear arrangement of Cys residues. The latter form intramolecular disulfide bonds that are essential for proper class-specific secondary folding and activity (Marshall et al, 2011;Haag et al, 2012;Vriens et al, 2014). The majority of known Cys-rich plant peptides are thought to function as AMPs during plant-microbe interactions, and they have been isolated from roots, leaves, stems, flowers, and seeds (Nawrot et al, 2014).…”

Section: Cysteine-rich Peptidesmentioning

confidence: 99%

The Plant Peptidome: An Expanding Repertoire of Structural Features and Biological Functions

et al. 2015

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“…When replacing this motif with AAAARR or RGFRAA, MtDef4 loses its ability to penetrate the interior of the cell [53]. Nevertheless, there is no evidence that this sequence is in other plant defensins penetrating fungal cells [52].…”

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confidence: 99%

“…After interaction with the receptors, the defensins either penetrate the interior of the fungal cell and interact with intracellular targets, or remain on the surface (for example, as MsDef1) and induce cell death by inducing the signal cascade (Fig. 2) [52]. An example of defensin penetrating cell is MtDef4 (see Fig.…”

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confidence: 99%

PLANT DEFENSINS: BIOLOGICAL FUNCTION, MECHANISMS OF ACTION AND METHODS OF ANALYSIS (review)

Kulaeva¹,

Kliukova²,

Повыдыш³

et al. 2017

S-h. biol.

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A b s t r a c tOne of the actual problems of modern agriculture is crop loss due to various biotic and abiotic factors. In plants there is a multicomponent protection system, including the formation of protective barriers, activation the reaction of hypersensitivity and synthesis of antimicrobial peptides, which are low molecular weight compounds showing broad spectrum activity against fungi, bacteria and viruses. This group consists of several groups of peptides, including defensins, which are one of the most common classes of antimicrobial peptides and are detectable in all living organisms. Defensins are small (45-54 amino acids), cysteine-rich peptides involved in a different protective responses (B.P. Thomma et al., 2002). Genes which are coding plant defensins are expressed in different organs of plants, where their products are necessary for biotic and abiotic stresses. Thus, these peptides are extremely important in terms of getting crop lines that are resistant to pathogens and abiotic stresses. Defensins are characterized by a strong sequence variability that seems to correlate with a variety of mechanisms of action of these peptides that can induce pathogen's cell death by penetrating into a cell or by being on its surface (T.M. Shafee et al., 2016). Most of the plant defensins are characterized by the antifungal activity. Some defensins have antibacterial activity, which may be combined with activity against fungi. For a small number of plant defensins their participation in the processes of resistance to heavy metals, cold stress, drought, salinity, and in the development process is indicated. Modern approaches of molecular and computational biology allow an effective search for new forms of defensins activity by studying the wild, non-model plant objects. The development of next-generation sequencing methods («Next Generation Sequencing») make possible the intensive study of the transcriptomes of such objects. However, the correct annotation of the sequences of peptides, characterized by small size and high variability, can be done by usage the special programs, such as SPADA (Small Peptide Alignment Discovery Application) (P. Zhou et al., 2013). SPADA makes multiple sequence alignment of all known paralogous genes within a gene family and builds a predictive model for the search of new members of the same family. Prediction of newly identified active defensins and identification of conserved amino acids can also be performed by computational biology methods. An approach based on a multiple sequence alignment and subsequent cluster analysis allows dividing defensins into groups with similar functional activity (N.L. van der Weerden et al., 2013). Thus, the combination of modern methods of molecular and computational biology allows carrying out the study of this group of protective peptides with high efficiency.

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Antifungal Plant Defensins: Mechanisms of Action and Production

Cited by 198 publications

References 137 publications

The phospholipid code: a key component of dying cell recognition, tumor progression and host–microbe interactions

The phospholipid code: a key component of dying cell recognition, tumor progression and host–microbe interactions

The Plant Peptidome: An Expanding Repertoire of Structural Features and Biological Functions

PLANT DEFENSINS: BIOLOGICAL FUNCTION, MECHANISMS OF ACTION AND METHODS OF ANALYSIS (review)

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