Hydrophobin-based capsules with target-sensitive release mechanism, compositions comprising thereof, and related methods

Abstract

The present invention relates to hydrophobin (HFB) fusion polypeptides, HFB-based capsules comprising said HFB fusion polypeptides and having a target-sensitive opening mechanism, and compositions comprising the HFB-based capsules. The invention further relates to the use of said HFB capsules as a platform for the delivery of a variety of compounds for agronomical, gastronomical and / or pharmaceutical purposes and its use for the detection of pathogens and / or microbes.

Description

[0001]HYDROPHOBIN-BASED CAPSULES WITH TARGET-SENSITIVE RELEASE MECHANISM, COMPOSITIONS COMPRISING THEREOF, AND RELATED METHODS TECHNICAL FIELD OF THE INVENTION The present invention relates to hydrophobin (HFB) fusion polypeptides, HFB-based capsules comprising said HFB fusion polypeptides and having a target-sensitive opening mechanism, and compositions comprising the HFB-based capsules. The invention further relates to the use of said HFB capsules as a platform for the delivery of a variety of compounds for agronomical, gastronomical and / or pharmaceutical purposes, and its use for the detection of pathogens and / or microbes. BACKGROUND Hydrophobins (HFB) are a group of small (~100 amino acids) cysteine-rich proteins that were discovered in filamentous fungi that are lichenized or not. Later similar proteins were also found in Bacteria. HFB are known for their ability to form hydrophobic capsules and coatings on the surface of an object. They were first discovered and separated in Schizophyllum commune in 1991. Based on differences in hydropathy patterns and biophysical properties, they can be divided into two categories: class I and class II. Hydrophobins can self-assemble into a monolayer on hydrophilic:hydrophobic interfaces such as a water:air interface. Thanks to this property, there have been disclosed, both in patent and non-patent literature, methods for encapsulating and delivering a variety of compounds via HFB-based capsules, as follows: Reuter LJ et al. (2017) study and characterize fusion proteins comprising different variants of hydrophobin (HFB) and transferrin (Tf). The study evaluates the formation of particles resulting from this fusion and their ability to encapsulate PSi, a drug used against cancer cells. The internalization of these particles into cancer cells is mediated via transferrin and its binding to the transferrin receptor, thus the Tf protein directs the capsule and its contents towards a specific target, i.e., towards cancer cells. Xiao Y et al. (2018) study the possibility of improving the introduction of NIR fluorescent probes. A hydrophobin-RGD peptide fusion protein (RGD-HFBI) was used as the delivery mechanism. In the work it was demonstrated that the RGD-HFBI protein is capable of producing capsules that envelop the probes in "nano-cages" and that the RGD peptide retains its binding capacity to the αvβ3 integrin. The work further demonstrates that these constructs are selectively incorporated into cells expressing αvβ3 integrin. Maiolo D et al. (2017) study the use of hydrophobin (HFBII) capsules for the solubilization of particles composed of gold nanoparticles stabilized with dodecanethiol. They report the use of hydrophobin for the formation of capsules that allow the solubilization of the hydrophobic drug and its incorporation into cancer cells. They also evaluated their ability to be incorporated in vivo. The work finds that the contents of the hydrophobin capsules are released after incorporation into cells and subsequent reduction of the complex by glutathione reduction. U.S. Patent No. 10,188,136 relates to hydrophobin mimic compounds capable of forming nanoparticle or nanocontainer structures, and their potential use in bio-nanotechnology. The compound is described as comprising a protein head, a hydrophilic linker and a hydrophobic tail. The mimic is described exhibiting hydrophobin II (HFBII)-like properties. U.S. Patent No. 11,447,794 relates to a method of increasing resistance against fungal pathogens of the family Phacosporaceae in plants and / or plant cells. This is achieved for instance by increasing the expression of a hydrophobin protein or fragment thereof in a plant, plant part and / or plant cell in comparison to wild type plants, wild type plant parts and / or wild type plant cells. In the transgenic plants hydrophobin can be expressed as a fusion protein to facilitate and / or enhance expression. Furthermore, the hydrophobin protein can be expressed including a secretion signal sequence which mediates secretion of the protein into the apoplast and / or into the cuticle. Chinese patent 201945514 is directed to a fusion protein comprising a GLP-1 and at least one other protein, wherein said other protein is hydrophobin. It is also directed to a pharmacological composition comprising said chimera protein and to a method of delivering said chimera protein for treatment of type 2 diabetes. Patent application CN110669140A discloses a chimeric protein resulting from the fusion of hydrophobin and a fluorescent protein, as well as a method for obtaining the same. The fusion protein is used for the detection of thrombin in a sample. Although the use of hydrophobin capsules as a compound delivery system has been described in the prior art, even noting the possibility of using receptors for directing such capsules, the potential targets described in the state of the art are quite limited, and there is no particular approach to the problem of how to achieve the opening of the capsules for the effective delivery of their contents. Reuter et al. (2017), e.g., describe that hydrophobin capsules are incorporated into a target cell, but do not provide any description regarding the opening mechanism. Meanwhile Maiolo et al. (2018), describe that hydrophobin capsules are incorporated into cells, wherein the reducing action of glutathione reductase (GSH) promotes capsule rupture and the release of the contents. BRIEF DESCRIPTION OF THE INVENTION In this context, a hydrophobin-based capsule is provided, comprising an opening mechanism that initiates content release upon binding to a receptor of a target molecule. This mechanism operates independently of cellular incorporation or external factors, such as reduction by endogenous enzymes including glutathione reductase (GSH). In view of the limitations of the prior art, it is a first aspect of the present invention to provide an HFB-based capsule comprising a) at least one non-fusion hydrophobin, and b) at least one HFB fusion polypeptide, having a hydrophobin bound to a receptor, wherein the binding of the receptor to its target is sufficient to destabilize the HFB-based capsule, leading to its opening. In an embodiment, the binding of the receptor to its target results in the spatial fixing of the receptor to its target molecule. In an embodiment, the HFB-based capsule comprises an HFB fusion polypeptide comprising a hydrophobin selected from an HFBI, HFBII, HFB7, or which is a polypeptide of SEQ ID NO: 1-36, or a variant thereof with at least at least 85% sequence identity to any one of SEQ ID NO: 1-36. In an embodiment, the HFB-based capsule comprises at least one HFB fusion polypeptide comprising a receptor selected from a) a Leucine Rich Repeat – Receptor Kinase (LRR-RK), b) a Leucine Rich Repeat – Receptor Protein (LRR-RP), c) a Lysin motif – Receptor Kinase (LysM-RK) or a Lysin motif – Receptor protein (LysM-RP), d) a receptor of SEQ ID NO: 56-63, e) AtLORE, AtWAK1, AtLecRK-I.8, AtDORN1, AtLecRK-I.9, AtLLG1-3, AtFER, o f) a FLS2 comprising amino acid residues R294, H316 and N674, and g) a BAK1 comprising amino acid residues T52, L53 and V54. In an embodiment, the HFB-based capsule comprises at least one HFB fusion polypeptide comprising a receptor capable of binding to a pathogen or microbe having a Pathogen-Associated Molecular Pattern (PAMP) or a Microbe-Associated Molecular Pattern (MAMP). In an embodiment, the HFB-based capsule comprises at least one HFB fusion polypeptide comprising a receptor capable of binding a target molecule from a pathogen or microbe selected from a) a bacterium selected from Escherichia spp., Salmonella spp., Staphylococcus spp., Xanthomonas spp., and Pseudomonas spp.; b) a fungus, selected from Cercospora spp., Exserohilum spp., Fusarium spp., Botrytis spp., Phytophthora spp., Candida spp., Aspergillus spp., and Spiroplasma spp.; c) a nematode selected from Meloidogyne spp., and Ascaris spp; d) a virus selected from Tomato mosaic virus, Tomato yellow curl virus, Influenza virus, and Herpes simplex virus; and e) a parasite, selected from Plasmodium spp., Trypanozoma spp. In an embodiment, the HFB-based capsule comprises a non-fusion hydrophobin selected from an HFBI, HFBII, HFB7, or which is a polypeptide of SEQ ID NO: 1-36, or a variant thereof with at least 85% sequence identity to any one of SEQ ID NO: 1-36. In an embodiment, the HFB-based capsule comprises at least two HFB fusion polypeptides, each having a hydrophobin bound to a receptor, wherein each receptor is a dimerizable receptor, and the dimerization of each receptor with the target is sufficient to destabilize the HFB-based capsule, leading to its opening. The binding of the dimerizable receptor to its target molecule induces the formation of a dimer- target complex, and reduces the interaction of the dimer-target complex, and the at least one non- fusion hydrophobin, destabilizing the HFB-based capsule, leading to its opening. In an embodiment, the HFB-based capsule encapsulates a compound selected from an antibacterial, an antifungal, an antinematode, an antiviral, an antiparasitic, an analgesic, a nutraceutical, an essential oil, an industrial chemical, and a cosmetic ingredient. It is a second aspect of the invention to provide a hydrophobin (HFB) fusion polypeptide comprising a hydrophobin, and a dimerizable receptor bound to said HFB, wherein the HFB fusion polypeptide binds to its target molecule by forming a dimer. In an embodiment, the hydrophobin fusion polypeptide comprises a hydrophobin is selected from an HFBI, HFBII, HFB7, or which is a polypeptide of SEQ ID NO: 1-36, or a variant thereof with at least 85% sequence identity to any one of SEQ ID NO: 1-36. In an embodiment, the hydrophobin fusion polypeptide comprises a dimerizable receptor selected from a) a Leucine Rich Repeat – Receptor Kinase (LRR-RK), b) a Leucine Rich Repeat – Receptor Protein (LRR-RP), c) a Lysin motif – Receptor Kinase (LysM-RK) or a Lysin motif – Receptor protein (LysM-RP), d) a receptor of SEQ ID NO: 56-63, e) AtLORE, AtWAK1, AtLecRK-I.8, AtDORN1, AtLecRK-I.9, AtLLG1-3, AtFER, or f) a FLS2 comprising amino acid residues R294, H316 and N674, or g) a BAK1 comprising amino acid residues T52, L53 and V54; In an embodiment, the hydrophobin fusion polypeptide comprises a dimerizable receptor that binds to a target selected from a Pathogen-Associated Molecular Pattern (PAMP) and a Microbe- Associated Molecular Pattern (MAMP) It is a third aspect of the invention to provide a composition comprising a) an HFB-based capsule in any one of its embodiments, b) at least one suitable excipient, and c) a compound of interest, wherein said compound of interest is encapsulated by the HFB-based capsule. In an embodiment, the compound of interest is an agronomical compound selected from an antibacterial, an antifungal, an antinematode, or an antiviral compound. In an embodiment, the composition is applied to a plant selected from main row crops, fruits and vegetables. In an embodiment, the plant is affected by a pathogen or microbe selected from a) a bacterium selected from Xanthomonas spp., Pseudomonas spp.; b) a fungus selected from Cercospora spp., Exserohilum spp., Fusarium spp., Botrytis spp., Phytophthora spp.; c) a nematode selected from Meloidogyne spp.; and d) a virus, selected from Tobacco mosaic virus, and Tomato yellow curl virus. In an embodiment, the compound of interest is a gastronomical compound selected from an antibacterial, an antifungal, an antinematode, an antiviral, an antiparasitic, an analgesic, a nutraceutical, or a colorant compound. In an embodiment, the composition is applied to a food product selected from dairy products, bakery products, and meat-based products. In an embodiment, the food product comprises a pathogen or microbe selected from e) a bacterium selected from Escherichia spp., Salmonella spp., Staphylococcus spp., Pseudomonas spp; f) a fungus selected from Fusarium spp., Candida spp., Aspergillus spp. Spiroplasma spp.; g) a nematode selected from Ascaris spp.; h) a virus selected from Influenza virus, or Herpes simplex virus; and i) a parasite selected from Plasmodium spp., Trypanozoma spp. In an embodiment, the compound of interest is a pharmaceutical compound selected from an antibacterial, an antifungal, an antinematode, an antiviral, an antiparasitic, an analgesic, a nutraceutical, or a colorant compound. In an embodiment, the pharmaceutical composition is applied to an organism in need selected from humans and other primates (e.g. apes and monkeys), farm animals (e.g. cattle, sheep, pigs, goats, horses), pets and other domestic animals (e.g. dogs, cats), laboratory animals (e.g. mice, rats, guinea pigs, rabbits), birds and poultry (chickens, turkeys, ducks, geese) for the treatment of a condition caused by a pathogen or microbe. More preferably, for the treatment of a condition caused by a pathogen or microbe selected from a) a bacterium selected from Escherichia spp., Salmonella spp., Staphylococcus spp., Pseudomonas spp; b) a fungus selected from Fusarium spp., Candida spp., Aspergillus spp. Spiroplasma spp.; c) a nematode selected from Ascaris spp.; d) a virus selected from Influenza virus, or Herpes simplex virus; and e) a parasite selected from Plasmodium spp., Trypanozoma spp. It is a fourth aspect of the invention to provide a method for applying a compound of interest, comprising the steps of a) providing the composition of the third aspect, b) applying an effective amount of the composition to an organism in need, c) contacting the HFB-based capsule with a target molecule. It is a fifth aspect of the invention to provide a method for detecting a pathogen or microbe of interest, comprising the steps of a) providing an HFB-based capsule of the first aspect and a reporter compound encapsulated by the HFB-based capsule, b) contacting the HFB-based capsule of step a) with the pathogen or microbe of interest, c) revealing the contacting of step b) by measuring the release of the reporter compound. BRIEF DESCRIPTION OF THE FIGURES Figure 1. Extracellular domains of FLS2-BAK1 bound to flg22 (4MN8). N-terminal residues are indicated in red and C-terminal in black. Figure 2. Distance between the Acs of the C-terminal residues of FLS2 and BAK1, calculated with Visual Molecular Dynamics (VMD) software. Figure 3. Interactions between flg22 and FLS2-BAK1. A) Interaction of the N-terminal (Left, residues 1 to 7) and C-terminal (Right, residues 8 to 21) portion of flg22 with FLS2. Residue Gly318 of FLS2 is indicated in red. B) Detail of the interaction between FLS2 and BAK1. C) BAK1 recognizes the C-terminal end of flg22 bound to FLS2. Figure 4. Matrices generated with the PSSM command of FoldX. For selected FLS2 residues, the △△G values obtained for each pair of chains of the complex (kcal mol -1 ) are plotted. Residues R294-H316 and N674, relevant in the interaction of FLS2 with flg22 and BAK1, respectively, are highlighted. Figure 5. Matrices generated with the PSSM command of FoldX. For the selected residues of BAK1, the △△G values obtained for each pair of chains of the complex are plotted (kcal mol-1). Residues F60 and F144, responsible for its interaction with FLS2, are highlighted. Similarly, residues T52 Similarly, residues T52, L53 and V54, whose change affects the interaction with flg22, are indicated. Figure 6. Matrices generated with the PSSM command of FoldX. For the selected residues of flg22, the △△G values obtained for each pair of chains of the complex (kcal mol-1) are plotted. Residues L3, D14 and D15, relevant in the interaction with FLS2, are highlighted. G18, which participates in the binding to BAK1, is also highlighted. Figure 7. MSA of the Pfam family seed PF00669, “flagellin N-terminal”. The first sequence, highlighted in black, corresponds to the flg22 peptide of P. aeruginosa, highlighted in black, corresponds to the P. aeruginosa peptide flg22, with which fls2-bak1 (4mn8) is co-crystallized. FLS2-BAK1 (4MN8). Visualization was performed in Jalview, coloring for hydrophobicity (red: hydrophobic residues) and conservation. Figure 8. Specific recognition of a chitin oligomer by AtCERK1. A) The chitin binds to a surface depression on the surface of AtCERK1. B) Detail of the interactions between AtCERK1 and NAG. Figure 9. Superposition of crystals of AtCERK1 free and chitin-bound state: 4EBY and 4EBZ. The crystallographic waters are shown at are represented in orange crystallographic waters and in green the NAG chain. In the protein (blue) the amino acids involved in the interactions observed in Figure 8 are highlighted in light blue. Figure 10. Matrix generated with the PositionScan command of FoldX. For the selected 4EBY residues, the △△G values obtained (kcal mol-1) are plotted. Figure 11. Structural overlap of free FLS2 (4MNA, LRR7-17 repeats) with FLS2-flg22-BAK1 (4MN8). A) Detail of LRRs 7 to 17. B) FLS2 in complex with flg22 and BAK1 (4MN8) is shown in cyan. Complex with flg22 and BAK1 (black). Free FLS2 is depicted in orange. Figure 12. A) Structural overlay of free and chitin-bound AtCERK1. B) Structural overlay of free and chitin-bound OsCEBiP, residues 29-223 I Comparison of the LysM2 domain of CERK1 from Arabidopsis and rice. Figure 13. A) Model of the homodimer formed by the extracellular domain of OsCERK induced by chitin. B) Model of the homodimer formed by the extracellular domain of OsCEBiP induced by chitin. Figure 14. Schematic of the FLS2 / BAK1 heterodimerization that occurs upon recognition of flg22. This process triggers Pattern-Triggered Immunity. The 4MN8 structures of FLS2 and BAK1 were used. Figure 15. A) Crystal of hydrophobin 1 from T. reesei, 2FZ6. The hydrophobic loops and the N- and C-terminal N- and C-terminal ends are highlighted. B) Structural alignment of the 2FZ6 crystal with the model obtained by Alphafold for HFB7. Alphafold for HFB7 (RMSD 2.66 Å). C) Alignment of hydrophobins 1 and 2 of T. reesei. Disulfide bridges (magenta) and hydrophobic loops (orange) have been highlighted, forming the characteristic pattern of class II hydrophobin. Figure 16. Schematic representation of the HFB-based capsule opening mechanism. In the presence of flg22 the BAK1-FLS2 dimer-target complex forms, causing a lower stability of the interaction between the HFB fusion polypeptide and surrounding HFBs, leading to the opening of the HFB-based capsule. Figure 17. Alphafold models for the BAK1-HFB7 and FLS2-HFB7 fusion proteins. Structural alignment of the 2FZ6 hydrophobin crystal with the BAK1-HFB7 model (RMSD 2.09 Å). Right. Structural alignment of the 2FZ6 hydrophobin crystal with the FLS2-HFB7 model (RMSD 3,09 Å). Figure 18. Example of images observed in TEM of nanocapsule formation. Each suspension was deposited on a 400 mesh nickel grid covered with a carbon film. The samples were observed at a voltage of 120 kV in the transmission electron microscope. Figure 19. Particles averaging around 100 nm are observed with and without the addition of SNA, but particles in the micron range are also detected following the addition of SNA probably due to the precipitation of SNA Figure 20. A) Shows an SDS PAGE depicting the purification of PDI as a fusion protein to Trx. P: total fraction of culture, FT: flowtrough after Ni-NTA, W 1-5 belong to column wash procedure E1-2 belong to the elution process. B) Shows the digestion process, Lanes 1 and 3 correspond to the protein weight marker in the second lane the purified protein can be observed after the procedure depicted in the previous image. In lanes 4,5 and 7 is obtained PDI after the digestion, and lane 6 belongs to the Trx obtained after the digestion of fusion protein. It is only detected after elution with imidazole because it contains a his tag. Figure 21. Results of nanocapsule recovery from different ultracentrifugation procedure. The highest amount of nanocapsules were obtained from the ultracentrifugation procedure. However, the mild centrifugation also yields nanocapsule formation. Thus, for routine nanocapsule preparation the inventors follow with mild centrifugation step. Figure 22. Scheme of the interaction between a particular embodiment of the HFB fusion polypeptide and the Ni-NTA resin, with consequent release of the fluorescein from the interior of the capsule. The HFB fusion polypeptide from the cover of the nanocapsule contains a hydrophilic and hydrophobic portion that allows nanocapsule formation. It should be noted that the receptor portion of the HFB fusion polypeptide is located in the outer of the nanocapsule and anchored via the HFB portion to the nanocapsule itself.. Figure 23. Alpha fold prediction of three-dimensional structure of the HFB fusion polypeptide PDI- Trx is shown. The His-tag is located at the C-terminal of Trx. Figure 24. Example of images observed in TEM of nanocapsule formation. A) PFI:FI in a 1:14 ratio; B) PDI: PDI-Trx (sensor-like): FI in a 1:0.1:114 ratio; PDI-Trx:PDI in a ratio 1:10. Figure 25. Fluorescence intensity (emission) as a function of temperature of the tubes containing the nanocapsules. Nanocapsules + sensor 1 refers to the molar ratio 1 (0.05:1:14), Nanocapsules + sensor 2 refers to the molar ratio 2 (0.2:1:14), Nanocapsules + sensor 3 refers to the molar ratio 3 (0.5:1:14), nanocapsules PDI refers to the nanocapsules without the HFB fusion polypeptide and control Fl refers to the control of fluorescein free. Figure 26. Fluorescence intensity (emission) as a function of temperature of the tubes containing A) Supernatant 1 (SN1) after interaction with the Ni-NTA resin, and B) the Supernatant 2 (SN2), after elution with imidazole. Nanocapsules + sensor 1 refers to the molar ratio 1 (0.05:1:14), Nanocapsules + sensor 2 refers to the molar ratio 2 (0.2:1:14), Nanocapsules + sensor 3 refers to the molar ratio 3 (0.5:1:14), nanocapsules PDI refers to the nanocapsules without the sensor- like protein and control Fl refers to the control of fluorescein free. For the tubes with the SN2 the inventors evidence fluorescence intensities of around 0.8-1.4 x106. Figure 27. Alpha fold prediction of the three-dimensional folding of the HFB fusion polypeptide PDI-MBP is shown, with the PDI protein highlighted as P, MBP highlighted as M, and the linker as L. The sensor-like affinity is determined by the MBP's interaction with the maltodextrin resin. B) predicted interaction between hydrophobic patches of PDI. Figure 28. Fluorescence intensity (emission) as a function of temperature of the tubes containing the nanocapsules previous to the resin interaction assay. Fl refers to the control of fluorescein free. Figure 29. Fluorescence intensity (emission) as a function of temperature of the tubes containing the nanocapsules before and after the incubation with the maltose resin. Fl refers to the control of fluorescein free. DETAILED DESCRIPTION OF THE INVENTION The invention will be described in further detail below, with reference to the accompanying figures and exemplary embodiments below. Any technical terminology used herein shall be understood by the common definition utilized in the art and / or by those skilled in the art, unless otherwise explicitly stated or inferred by context. As used herein, the terms “hydrophobin” and “HFB” are used interchangeably and refer to a polypeptide of any one of the sequences of SEQ ID NO: 1-36, homologous variants and / or mutant variants thereof capable of forming amphipathic structures, such as capsules capable of encapsulating compounds such that they promote their solubility. As used herein, the term “HFB-based capsule” refers to a three-dimensional amphipathic structure in the form of capsule capable of encapsulating compounds such that they promote their solubility in a polar solvent, e.g., water, wherein said structure comprises a non-fusion hydrophobin and / or an HFB fusion polypeptide, preferably both non-fusion hydrophobin and an HFB fusion polypeptide. The capsule may be complete or incomplete and have any shape necessary to carry out the intended function. The term may also refer to the incorporation of the compound into the structure of the HFB-based capsule. As used herein, the term “fusion polypeptide” refers to a polypeptide sequence that’s covalently linked, i.e. fused, to another molecule by one of its ends. The fusion polypeptide is preferably bound to a receptor. Said link maybe through an N-terminal or C-terminal of the polypeptide sequence. Accordingly, "HFB fusion polypeptide" refers to a fusion polypeptide comprising a hydrophobin in any embodiment disclosed herein. More specifically, an HFB fusion polypeptide comprises a hydrophobin (HFB), and a receptor, Optionally, an HFB fusion polypeptide can comprise a linker sequence. In contrast, the term “non-fusion hydrophobin” and variants thereof refer to a hydrophobin in any of its embodiments that is not fused to any other protein or fragment thereof. As used herein, the term “receptor” refers to a polypeptide, or fragment thereof such that it allows an HFB fusion polypeptide comprising it to recognize and / or bind to a specific target molecule, preferably by its direct interaction. More particularly, the term “dimerizable receptor” refers to a polypeptide, or fragment thereof such that it allows an HFB fusion polypeptide comprising it to recognize and / or bind to a specific target molecule by forming a dimer, i.e., the receptor is in the form of a dimer. In this sense, a dimer formed by a pair of HFB fusion proteins may comprise each a different dimerizable receptor, thus forming an heterodimer, or the same dimerizable receptor, thus forming a homodimer. Whenever said receptor (dimerizable or not) is used to determine the presence of a particular target molecule, the term “sensor” may be used instead. In that case, the terms may be used interchangeably. Throughout the present description, the term “dimer” refers to a quaternary protein structure resulting from the interaction of two dimerizable receptors between each other, preferably triggered by the binding to its target. The formation of the dimer can be mediated by environmental factors, such as salinity or pH, as well as by the presence of specific molecules, e.g. biomolecules such as proteins, lipids, saccharides, or combinations thereof and of different composition. Consequently, the term "dimer-target complex" refers to a quaternary protein structure comprising the dimer, as previously described, and its target molecule. This complex results from the interaction of the dimer and its target molecule. As an example, and without intent to limit the scope of the present invention, a fusion polypeptide of the present invention can result from the linking of an HFB and a receptor through the covalent bonding between these such that these form a single polypeptide sequence in any of the following conformations: N-terminus - H–B - receptor– C-terminus N- terminus – receptor – HFB – C-terminus In an embodiment, the fusion polypeptide may further comprise a linker sequence linking an HFB and a receptor through the covalent bonding between these such that these form a single polypeptide sequence in any of the following conformations: N-terminus - HFB - linker – receptor – C-terminus N- terminus – receptor – linker – HFB – C-terminus As used herein, the term “opening”, when referring to a capsule, refers to the action by which the capsule alters its structure in such a way as to allow the release of the contents encapsulated by said capsule, if it has one. Such opening may take place by the generation of pores, breaks, gaps, ruptures, or any other similar topological phenomenon. Typically, according to the invention, said pores, breaks, gaps, ruptures, or any other similar topological phenomenon are the result of a reduction in the stability of the HFB-based capsule. The opening of the capsule can be an irreversible process. As used herein, the term “destabilize”, “destabilizing”, and similar expressions, refers to a process by which the structural integrity of a capsule is altered in a way that can lead to its opening. Said destabilization may be caused by physical causes, e.g. an increase in the tensile stress that the capsule is exposed to, by biological causes, e.g. a lower interaction between the molecules that forms the capsule itself, or chemical causes, e.g. a change in the salinity or pH of the media surrounding the capsule. As used herein, the expression “"to recognize and / or bind" and variants of said expression, when referring to an HFB-based capsule, an HFB fusion polypeptide or a receptor, shall be understood as the physical and direct association between said HFB-based capsule, HFB fusion polypeptide or receptor and their target molecule, preferably as a result of a specific recognition resulting from the interaction between the receptor and its target molecule by means of intermolecular forces such as Van der Waals, dipole, H-bond and / or ionic forces. This association may occur in vivo and / or in vitro and includes a contact between a molecule and another molecule, although it may also include contact between a molecule and another element significantly larger and / or more complex than a molecule, for example a cell, or a microorganism, or a specific cell structure. In some cases the recognition and / or binding of the receptor and its target may trigger a process of dimerization of said receptor. As used herein, the expression “to reduce the interaction” when referring to hydrophobins, either non-fusion hydrophobins or part of an HFB fusion polypeptide in any embodiment of the present invention, means a reduction in any kind of molecular interaction such that increases the probability of opening of a capsule comprising said hydrophobins. The molecular interaction comprises intermolecular forces such as Van der Waals, dipole, H-bond and / or ionic forces. It is a first aspect of the present invention to provide an HFB-based capsule comprising a) at least one non-fusion hydrophobin, and b) at least one HFB fusion polypeptide, having a hydrophobin bound to a receptor, wherein the recognition and / or binding of the receptor to its target is sufficient to destabilize the HFB-based capsule, leading to its opening. As a person skilled in the art will understand from the Examples provided herein, the opening mechanism of the capsule is due to the fact that the recognition and / or binding between the receptor and its target molecule results in spatial fixing of the receptors to a fixed target, leading to a higher tensile stress in the hydrophobin membrane that forms the capsule, destabilizing said membrane and eventually leading to the opening of the capsule by its rupture, releasing the content to the external medium. As described in the Background section herein, said mechanism has not been described nor suggested in the prior art, resulting in an HFB-based capsule that can be directed against specific targets and that opens by its own means without the intervention of additional enzymes or the action of a cell. It is a first aspect of the present invention to provide an HFB-based capsule comprising a) at least one non-fusion hydrophobin, and b) at least one HFB fusion polypeptide, having a hydrophobin bound to a receptor, wherein the recognition and / or binding of the receptor to its target is sufficient to destabilize the HFB-based capsule, leading to its opening. In an embodiment, the HFB-based capsule comprises a) at least one non-fusion hydrophobin, and b) at least one HFB fusion polypeptide, having a hydrophobin bound to a receptor, wherein the recognition and / or binding of the receptor to its target results in the spatial fixing of the receptor to its target, which is sufficient to destabilize the HFB-based capsule, leading to its opening. More specifically, wherein the target is a fixed target. In a particular embodiment, the spatial fixing of the receptor to its target is due to the intermolecular forces such as Van der Waals, dipole, H-bond and / or ionic forces that mediate the recognition and / or binding of the receptor to its target, more specifically, wherein the target is a fixed target. In an embodiment, the HFB-based capsule comprises at least one HFB fusion polypeptide having a hydrophobin that is naturally occurring, e.g., an HFBI, HFBII, or HFB7, or any other wild-type hydrophobin of any species, e.g. a Trichoderma reesei hydrophobin, or a non-naturally occurring or modified hydrophobin, e.g. a recombinant or mutant hydrophobin that results from the application of a biotechnological technique. In a preferred embodiment, the HFB-based capsule comprises at least one HFB fusion polypeptide having a hydrophobin selected from an HFBI, HFBII, HFB7, or which is a polypeptide of SEQ ID NO: 1-36, preferably the HFB is a polypeptide of SEQ ID NO: 19. In an embodiment, the HFB-based capsule comprises at least one HFB fusion polypeptide having a hydrophobin selected from any one of SEQ ID NO: 1-36, or a polypeptide with at least 60% sequence identity to any one of SEQ ID NO: 1-36. Preferably, a polypeptide with at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity to any one sequence of SEQ ID NO: 1-36. More preferably, a polypeptide with at least 85%, at least 86%, with at least 87%, with at least 88%, with at least 89%, with at least 90%, with at least 91%, with at least 92%, with at least 93%, with at least 94%, with at least 95%, with at least 96%, with at least 97%, with at least 98%, or with at least 99% sequence identity to any one sequence of SEQ ID NO: 1-36. In an embodiment, the HFB-based capsule comprises a) at least one non-fusion hydrophobin, and b) at least one HFB fusion polypeptide, having a hydrophobin bound to a receptor, wherein the recognition and / or binding of the receptor to its target results in the spatial fixing of the receptor to its target, which is sufficient to destabilize the HFB-based capsule, leading to its opening, more specifically, wherein the target is a fixed target, and the HFB-based capsule comprises at least one HFB fusion polypeptide having a hydrophobin selected from any one of SEQ ID NO: 1-36, or a polypeptide with at least 60% sequence identity to any one of SEQ ID NO: 1-36; preferably, a polypeptide with at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity to any one sequence of SEQ ID NO: 1-36. As used herein, the terms “fixing”, “fixed”, “spatial fixing”, “spatially fixed” and similar expressions, when referring to a target molecule, a receptor molecule, a HFB fusion polypeptide, and the like, refers to a reduction or lack of mobility of said molecule. This reduction or lack of mobility can be due to the nature of the molecule itself or the result of an intermolecular interaction. As a non- limiting example, a “fixed target” may be a molecule that may be bond to a substrate, or that is on itself too large to move freely. As a non-limiting example, a “spatially fixed receptor” may be a receptor molecule that has its mobility reduced or nullified by its binding or recognition to a fixed target. In an embodiment, the HFB-based capsule comprises at least one HFB fusion polypeptide having a receptor selected from a Pattern Recognition Receptor (PRR), more specifically, - a Leucine Rich Repeat – Receptor Kinase (LRR-RK), - a Leucine Rich Repeat – Receptor Protein (LRR-RP), - a Lysin motif – Receptor Kinase (LysM-RK) or a Lysin motif – Receptor protein (LysM- RP), - a receptor of SEQ ID NO: 56-63, - AtLORE, AtWAK1, AtLecRK-I.8, AtDORN1, AtLecRK-I.9, AtLLG1-3, AtFER, o - a FLS2 comprising amino acid residues R294, H316 and N674, and - a BAK1 comprising amino acid residues T52, L53 and V54. In a preferred embodiment, the HFB-based capsule comprises at least one HFB fusion polypeptide comprising a receptor selected from a Pattern Recognition Receptor (PRR), more specifically, - a Leucine Rich Repeat – Receptor Kinase (LRR-RK) selected from o FLS2, BAK1, AtFLS2, AtBAK1, SlFLS3, AtEFR, SlCORE, SlSERK3a, AtXPS1, OsXA21, OsSERK2, AtMIK2, OsRLK1, AtNIL31, SlSYR1, SlSYR2, SlPORK1, AtRLK7, atPEPR1, and AtPEPR2, - a Leucine Rich Repeat – Receptor Protein (LRR-RP) selected from o NbCSPR, NbSOBIR1, NbBAK1, AtRLP1, AtSOBIR1, AtBAJ1, AtRLP23, AtSERKs, AtRLP30, AtRLP42, SICf2, SlCf4, SlCf5, SlCf9, SlSOBI1m, SlSOBIR1, SlSERK1 / 3a, SlEIX1, SlEIX2, SlVe1, SmELR, NbRXEG1, BnLepR3, BnRLM2, BnSOBIR1, VuINR, and sLcUrE1, and - a Lysin motif – Receptor Kinase (LysM-RK) or a Lysin motif – Receptor protein (LysM- RP) selected from o OsCEBiP, OsCERK1, AtLYK4, AtLYK5, AtLYM2, LjLYS6, MtLYK9, MtLYR3, MtLYR4, PsLYK9, VvLYK1-1, VvLYK1-2, MdCERK1, AtCERK1, OsLYP4, OsLYP6, OsCERK1, AtLYM1, AtLYM3, AtCERK1, LjEPR3, LjNFR1, LjNFR5, MtLYK3, MtNFP, PsSYM37, PsK, and PsLYR3. - a receptor of SEQ ID NO: 56-63, - AtLORE, AtWAK1, AtLecRK-I.8, AtDORN1, AtLecRK-I.9, AtLLG1-3, AtFER, - a FLS2 comprising amino acid residues R294, H316 and N674, and - a BAK1 comprising amino acid residues T52, L53 and V54; In an embodiment, the HFB-based capsule comprises at least one HFB fusion polypeptide having a linker sequence linking the HFB and the receptor. In a preferred embodiment, said linker sequence is a (GGGGS)X sequence, wherein X is 1, 2, 3 or 4; more preferably wherein X is 2. In an embodiment, the HFB-based capsule comprises at least one HFB fusion polypeptide having a receptor capable of recognizing and / or binding to a target molecule, wherein said target molecule selected from a Pathogen-Associated Molecular Pattern (PAMP) and a Microbe- Associated Molecular Pattern (MAMP); preferably wherein said PAMP or MAMP is - a molecule that elicits an LRR-RK response, - a molecule that elicits an LRR-RP response, - a molecule that elicits a LysM-RK or LysM-RP response, - mc-3-OH fatty acid, pectin, oligogalacturonides, egg extract, NAD+, extracellular ATP, or an alkalinization factor, e.g., RALF1 or RALF2. In a preferred embodiment, the HFB-based capsule comprises at least two HFB fusion polypeptides comprising a dimerizable receptor capable of recognizing and / or binding to a target molecule selected from - a molecule that elicits a LRR-RK response selected from o flagellin, e.g., flg22, flgll-28 or a fLg22 of SEQ ID NO: 37-55; or a flg22 comprising amino acids L3, D14, D15 and G18, Elongation factor-Tu, e.g. elf18, cold shock proteins, e.g., csp22, xanthine uracil permease, e.g., xup25, proRaxX, e.g., RaxX21, RaxX16, enriched Fusarium oxysporum elicitor EnFOE, nematode proteins, prosystemin, AtprePAMP-induced peptides (AtPIP1-11), and AtproPep 1-8; - a molecule that elicits LRR-RP responses, selected from o Cold shock protein, e.g., csp22, Enigmatic MAMP of Xanthomonas, e.g., eMax, NEP-1 like protein, e.g., nlp20, Sclerotinia culture filtrate elicitor, e.g., SCFE1, polygalacturonase, AVRs, e.g., AVR2, AVR4, AVR5, AVR9, SIRcr-1, SiRcr-2, Ethylene-inducing xylanase, e.g., EIX, Ave1, Elicitin Pre-INF1, XEG1, AvrLm1, AvrLm2, Chloroplastic ATP synthase, e.g., inceptin, and Cuscuta factor CuF, - a molecule that elicits a LysM-RK or LysM-RP response selected from o chitin, e.g., a CO6 chitin, CO7 chitin or CO8 chitin, 1,3-β-D-glucan(Glc)6, peptidoglycan, chitooligosaccharide, a Nod factor, e.g., lipo- chitooligosaccharides (LCO), exopolysaccharide (EPS), and lipopolysaccharides (LPS), or - mc-3-OH fatty acid, pectin, oligogalacturonides, egg extract, NAD+, extracellular ATP, or an alkalinization factors, e.g., RALF1 or RALF2. In another embodiment, the HFB-based capsule comprises at least one HFB fusion polypeptide having a receptor capable of recognizing and / or binding a target molecule from a pathogen or microbe selected from a) a bacterium, e.g., Escherichia spp., Salmonella spp., Staphylococcus spp., Xanthomonas spp., Pseudomonas spp., more preferably, Escherichia coli, Salmonella typhimurium, Staphylococcus aureus, Xanthomonas campestris, Pseudomonas syringae, and Pseudomonas aureginosa; b) a fungus, e.g., Cercospora spp., Exserohilum spp., Fusarium spp., Botrytis spp., Phytophthora spp., Candida spp., Aspergillus spp., Spiroplasma spp., more preferably, Cercospora sojinia, Exserohilum turcicum, Fusarium graminearum, Fusarium solani, Botrytis cinerea, Phytophthora sojae, Candida albicans, Aspergillus fumigatus; and Spiroplasma kunkelii; c) a nematode, e.g., Meloidogyne spp., and Ascaris spp., more preferably, Meloidogyne exigua, and Ascaris lumbricoides; d) a virus, e.g., Tomato mosaic virus, Tomato yellow curl virus, Influenza virus, and Herpes simplex virus; e) a parasite, e.g., Plasmodium spp., and Trypanozoma spp., more preferably, Plasmodium falciparum, and Trypanozoma cruzi. In another embodiment, the HFB-based capsule comprises at least one HFB fusion polypeptide having a receptor capable of recognizing and / or binding a target molecule from a pathogen or microbe selected from a) a bacterium, e.g., Escherichia spp., Salmonella spp., Staphylococcus spp., Xanthomonas spp., Pseudomonas spp., more preferably, Escherichia coli, Salmonella typhimurium, Staphylococcus aureus, Xanthomonas campestris, Pseudomonas syringae, and Pseudomonas aureginosa; b) a fungus, e.g., Cercospora spp., Exserohilum spp., Fusarium spp., Botrytis spp., Phytophthora spp., Candida spp., Aspergillus spp., Spiroplasma spp., more preferably, Cercospora sojinia, Exserohilum turcicum, Fusarium graminearum, Fusarium solani, Botrytis cinerea, Phytophthora sojae, Candida albicans, Aspergillus fumigatus; and Spiroplasma kunkelii; c) a nematode, e.g., Meloidogyne spp., Ascaris spp., more preferably, Meloidogyne exigua, and Ascaris lumbricoides; d) a virus, e.g., Tomato mosaic virus, Tomato yellow curl virus, Influenza virus, and Herpes simplex virus; and e) a parasite, e.g., Plasmodium spp., Trypanozoma spp., more preferably, Plasmodium falciparum, Trypanozoma cruzi. As the person skilled in the art can appreciate from the teachings provided herein, the ability of the HFB fusion polypeptide of the present invention to be part of an HFB-based capsule is the result of the incorporation of a hydrophobin to said HFB fusion polypeptide. This allows the HFB fusion polypeptide to interact with other hydrophobins, thus being part of the hydrophobin capsule. In this regard, the fusion polypeptide of the present invention can be modified by the person skilled in the art to incorporate any other hydrophobin, either naturally occurring or artificial, according to their specific needs. Any embodiment resulting from such modification is to be considered as falling within the scope of the present invention. In an embodiment, the HFB-based capsule can be used for encapsulating a compound commonly used in agronomical, gastronomical, or pharmaceutical industry, i.e., an agronomical, gastronomical, or pharmaceutical compound. Preferably, the agronomical, gastronomical, or pharmaceutical compound is one for which is sought to reduce its use or that can increase its shelf life, or that needs protection from degradation. In another embodiment, the agronomical, gastronomical, or pharmaceutical compound is one that has to be applied several times due to the run-off, those that need to add additives to improve the penetration and those that can be applied together with biological inputs. In a preferred embodiment, the agronomical, gastronomical, or pharmaceutical compound is selected from an antibacterial, an antifungal, an antinematode, an antiviral, an antiparasitic, an analgesic, and a nutraceutical compound. Thanks to the teachings and examples provided herein, a person skilled in the art would be capable of generating HFB-based capsules having a target-sensitive opening mechanism capable of encapsulating a wide variety of compounds for their selective delivery upon detection of the corresponding target molecule. The example provided herein of the encapsulation of molecules of antibiotic antifungal colorant obtained from solid extracts of Trichoderma spp. metabolites should be understood only as an exemplary embodiment of the corresponding aspects of the present invention and is not meant to limit the scope of the invention. It should be noted that it is within the knowledge of a person skilled in the art, in combination with the teachings provided herein, to be capable of determining the exact laboratory or experimental conditions that allow for the proper encapsulation of a compound of interest. These laboratory or experimental conditions will depend on several factors, like the compound three-dimensional structure, its size, chemical composition, isotonic properties, among others. Thus, the encapsulation of said compound might be dependent on pH, temperature, salinity, etc. Through development and testing, the inventors of the present invention have developed several mechanisms that lead to the reduction of the stability of the HFB-based capsule which can be the result of physical elements, e.g. superficial tensions, of biological elements, e.g. changes in interactions induced by alterations in the structure of proteins, or chemical elements, e.g. changes in pH or ionic strength of the media. More specifically, the inventors have developed an HFB-based capsule comprising an HFB fusion polypeptide having a dimerizable receptor that dimerize upon recognition and / or binding to its target, forming a dimer-target complex. As the person skilled in the art would understand from the Examples provided herein, the opening of this particular embodiment of the HFB-based capsule incorporates an additional factor that contributes to the destabilization of the HFB-based capsule. In this case, there’s a reduction of the interaction between the non-fusion hydrophobin(s) and dimer-target complex, more specifically, the HFB fusion polypeptides that are part of the dimer- target complex, and that form said capsule. This reduction in the interaction is the result of a conformational change that triggers when the HFB fusion polypeptides of the capsule form the dimer-target complex when they recognize and / or bind to a target molecule. The fact that the HFB fusion polypeptide modifies its level of interaction with other hydrophobins is a technical feature that has not been described or suggested in the prior art and is not easily deducible from the primary structure of the protein, thus it would not be obvious to a person skilled in the art that such mechanism would be available for the production of an HFB-based capsule that’s target-sensitive. Thus, In an embodiment of the HFB-based capsule of the first aspect, the HFB-based capsule comprises a) at least one non-fusion hydrophobin, and b) at least two HFB fusion polypeptides, each having a hydrophobin bound to a receptor, wherein the receptor comprises a dimerizable receptor, and the recognition and / or binding of the dimerizable receptor to its target molecule is sufficient to destabilize the HFB-based capsule, leading to its opening. More specifically, wherein the recognition and / or binding of the dimerizable receptor to its target molecule a) induces the formation of a dimer-target complex, and b) reduces the interaction of the dimer-target complex, and the at least one non-fusion hydrophobin, destabilizing the HFB-based capsule, leading to its opening. The at least two HFB fusion polypeptides may be the same or different, preferably the at least two HFB fusion polypeptides are different. When the at least two HFB fusion polypeptides are different, they may differ in their HFB, or their receptor, or any combination thereof. Optionally, the at least two HFB fusion polypeptides may differ in their linker sequence. For example, they may differ in the presence or absence of a linker sequence, or in the specific sequence thereof. In a particular preferred embodiment, the at least two HFB fusion polypeptides differ in their dimerizable receptor. As used herein, the term “at least two HFB fusion polypeptides”, refers to the presence of at least two separate molecules of HFB fusion polypeptide, in any embodiment disclosed in the present application. In this sense, when describing that “at least two HFB fusion polypeptides” comprise a certain feature, characteristic or element, this description may also apply to at least one of the at least two HFB fusion polypeptides. In an embodiment, the HFB-based capsule comprises at least two HFB fusion polypeptide having a hydrophobin that is naturally occurring, e.g., an HFBI, HFBII, or HFB7, or any other wild-type hydrophobin of any species, e.g. a Trichoderma reesei hydrophobin, or a non-naturally occurring or modified hydrophobin, e.g. a recombinant or mutant hydrophobin that results from the application of a biotechnological technique. In a preferred embodiment, the HFB-based capsule comprises at least two HFB fusion polypeptide having a hydrophobin selected from an HFBI, HFBII, HFB7, or which is a polypeptide of SEQ ID NO: 1-36, preferably the HFB is a polypeptide of SEQ ID NO: 19. In an embodiment, the HFB-based capsule comprises at least two HFB fusion polypeptides having a hydrophobin selected from any one of SEQ ID NO: 1-36, or a polypeptide with at least 60% sequence identity to any one of SEQ ID NO: 1-36. Preferably, a polypeptide with at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity to any one sequence of SEQ ID NO: 1-36.More preferably, a polypeptide with at least 85%, at least 86%, with at least 87%, with at least 88%, with at least 89%, with at least 90%, with at least 91%, with at least 92%, with at least 93%, with at least 94%, with at least 95%, with at least 96%, with at least 97%, with at least 98%, or with at least 99% sequence identity to any one sequence of SEQ ID NO: 1-36. In an embodiment, the HFB-based capsule comprises at least two HFB fusion polypeptides having a receptor selected from a Pattern Recognition Receptor (PRR), more specifically, - a Leucine Rich Repeat – Receptor Kinase (LRR-RK), - a Leucine Rich Repeat – Receptor Protein (LRR-RP), - a Lysin motif – Receptor Kinase (LysM-RK) or a Lysin motif – Receptor protein (LysM- RP), - a receptor of SEQ ID NO: 56-63, - AtLORE, AtWAK1, AtLecRK-I.8, AtDORN1, AtLecRK-I.9, AtLLG1-3, AtFER, o - a FLS2 comprising amino acid residues R294, H316 and N674, and - a BAK1 comprising amino acid residues T52, L53 and V54. In a preferred embodiment, the HFB-based capsule comprises at least two HFB fusion polypeptides comprising a dimerizable receptor selected from a Pattern Recognition Receptor (PRR), more specifically, - a Leucine Rich Repeat – Receptor Kinase (LRR-RK) selected from o FLS2, BAK1, AtFLS2, AtBAK1, SlFLS3, AtEFR, SlCORE, SlSERK3a, AtXPS1, OsXA21, OsSERK2, AtMIK2, OsRLK1, AtNIL31, SlSYR1, SlSYR2, SlPORK1, AtRLK7, atPEPR1, and AtPEPR2, - a Leucine Rich Repeat – Receptor Protein (LRR-RP) selected from o NbCSPR, NbSOBIR1, NbBAK1, AtRLP1, AtSOBIR1, AtBAJ1, AtRLP23, AtSERKs, AtRLP30, AtRLP42, SICf2, SlCf4, SlCf5, SlCf9, SlSOBI1m, SlSOBIR1, SlSERK1 / 3a, SlEIX1, SlEIX2, SlVe1, SmELR, NbRXEG1, BnLepR3, BnRLM2, BnSOBIR1, VuINR, and sLcUrE1, and - a Lysin motif – Receptor Kinase (LysM-RK) or a Lysin motif – Receptor protein (LysM- RP) selected from o OsCEBiP, OsCERK1, AtLYK4, AtLYK5, AtLYM2, LjLYS6, MtLYK9, MtLYR3, MtLYR4, PsLYK9, VvLYK1-1, VvLYK1-2, MdCERK1, AtCERK1, OsLYP4, OsLYP6, OsCERK1, AtLYM1, AtLYM3, AtCERK1, LjEPR3, LjNFR1, LjNFR5, MtLYK3, MtNFP, PsSYM37, PsK, and PsLYR3. - a receptor of SEQ ID NO: 56-63, - AtLORE, AtWAK1, AtLecRK-I.8, AtDORN1, AtLecRK-I.9, AtLLG1-3, AtFER, or - a FLS2 comprising amino acid residues R294, H316 and N674, and - a BAK1 comprising amino acid residues T52, L53 and V54; In an embodiment, the HFB-based capsule comprises at least two HFB fusion polypeptides having a linker sequence linking the HFB and the receptor. In a preferred embodiment, said linker sequence is a (GGGGS)X sequence, wherein X is 1, 2, 3 or 4; more preferably wherein X is 2. In an embodiment, the HFB-based capsule comprises at least two HFB fusion polypeptides having a receptor capable of recognizing and / or binding to a target molecule, wherein said target molecule is selected from a Pathogen-Associated Molecular Pattern (PAMP) and a Microbe- Associated Molecular Pattern (MAMP); preferably wherein said PAMP or MAMP is - a molecule that elicits an LRR-RK response, - a molecule that elicits an LRR-RP response, - a molecule that elicits a LysM-RK or LysM-RP response, - mc-3-OH fatty acid, pectin, oligogalacturonides, egg extract, NAD+, extracellular ATP, or an alkalinization factor, e.g., RALF1 or RALF2. In a preferred embodiment, the HFB-based capsule comprises at least two HFB fusion polypeptides having a receptor capable of recognizing and / or binding to a target molecule selected from - a molecule that elicits a LRR-RK response selected from o flagellin, e.g., flg22, flgll-28 or a fLg22 of SEQ ID NO: 37-55; or a flg22 comprising amino acids L3, D14, D15 and G18, Elongation factor-Tu, e.g. elf18, cold shock proteins, e.g., csp22, xanthine uracil permease, e.g., xup25, proRaxX, e.g., RaxX21, RaxX16, enriched Fusarium oxysporum elicitor EnFOE, nematode proteins, prosystemin, AtprePAMP-induced peptides (AtPIP1-11), and AtproPep 1-8; - a molecule that elicits LRR-RP responses, selected from o Cold shock protein, e.g., csp22, Enigmatic MAMP of Xanthomonas, e.g., eMax, NEP-1 like protein, e.g., nlp20, Sclerotinia culture filtrate elicitor, e.g., SCFE1, polygalacturonase, AVRs, e.g., AVR2, AVR4, AVR5, AVR9, SIRcr-1, SiRcr-2, Ethylene-inducing xylanase, e.g., EIX, Ave1, Elicitin Pre-INF1, XEG1, AvrLm1, AvrLm2, and Chloroplastic ATP synthase, e.g., inceptin, and Cuscuta factor CuF, - a molecule that elicits a LysM-RK or LysM-RP response selected from o chitin, e.g., a CO6 chitin, CO7 chitin or CO8 chitin, 1,3-β-D-glucan(Glc)6, peptidoglycan, chitooligosaccharide, a Nod factor, e.g., lipo- chitooligosaccharides (LCO), exopolysaccharide (EPS), or lipopolysaccharides (LPS), and - mc-3-OH fatty acid, pectin, oligogalacturonides, egg extract, NAD+, extracellular ATP, and an alkalinization factors, e.g., RALF1 and RALF2. In another embodiment, the HFB-based capsule comprises at least two HFB fusion polypeptides having a receptor capable of recognizing and / or binding a target molecule from a pathogen or microbe selected from f) a bacterium, e.g., Escherichia spp., Salmonella spp., Staphylococcus spp., Xanthomonas spp., Pseudomonas spp., more preferably, Escherichia coli, Salmonella typhimurium, Staphylococcus aureus, Xanthomonas campestris, Pseudomonas syringae, and Pseudomonas aureginosa; g) a fungus, e.g., Cercospora spp., Exserohilum spp., Fusarium spp., Botrytis spp., Phytophthora spp., Candida spp., Aspergillus spp., Spiroplasma spp., more preferably, Cercospora sojinia, Exserohilum turcicum, Fusarium graminearum, Fusarium solani, Botrytis cinerea, Phytophthora sojae, Candida albicans, Aspergillus fumigatus; and Spiroplasma kunkelii; h) a nematode, e.g., Meloidogyne spp., Ascaris spp., more preferably, Meloidogyne exigua, and Ascaris lumbricoides; i) a virus, e.g., Tomato mosaic virus, Tomato yellow curl virus, Influenza virus, and Herpes simplex virus; and j) a parasite, e.g., Plasmodium spp., and Trypanozoma spp., more preferably, Plasmodium falciparum, and Trypanozoma cruzi. It should be understood that the HFB-based capsule comprises not only at least two HFB fusion polypeptides, but also other non-fusion hydrophobins such as forming a proper capsule capable of encapsulating a compound. Accordingly, in an embodiment, the HFB-based capsule comprises a non-fusion hydrophobin - that’s naturally occurring, e.g., an HFBI, HFBII, or HFB7, or any other wild-type hydrophobin of any species, e.g. a Trichoderma reesei hydrophobin, - or a non-naturally occurring or modified hydrophobin, e.g. a recombinant or mutant hydrophobin that results from the application of a biotechnological technique. In a preferred embodiment, the HFB-based capsule comprises a non-fusion hydrophobin selected from an HFBI, HFBII, HFB7, or which is a polypeptide of SEQ ID NO: 1-36, preferably the hydrophobin is a polypeptide of SEQ ID NO: 19. In an embodiment, the HFB-based capsule comprises a non-fusion hydrophobin selected from any one of SEQ ID NO: 1-36, or a polypeptide with at least 60%, preferably at least 85% sequence identity to any one of SEQ ID NO: 1-36. Preferably, a polypeptide with at least 60% sequence identity to any one of SEQ ID NO: 1-36. Preferably, a polypeptide with at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity to any one sequence of SEQ ID NO: 1-36.More preferably, a polypeptide with at least 85%, at least 86%, with at least 87%, with at least 88%, with at least 89%, with at least 90%, with at least 91%, with at least 92%, with at least 93%, with at least 94%, with at least 95%, with at least 96%, with at least 97%, with at least 98%, or with at least 99% sequence identity to any one sequence of SEQ ID NO: 1-36. As previously described, the HFB-based capsule of the first aspect of the present invention comprises an HFB fusion polypeptide having a receptor that recognizes and / or binds to a target molecule, it is necessary for the proper development of the HFB-based capsule of the present invention to provide an HFB fusion polypeptide. Thus, It is a second aspect of the present Invention to provide a hydrophobin (HFB) fusion polypeptide comprising a hydrophobin and a receptor, wherein the HFB fusion polypeptide recognizes and / or binds to a target molecule. In a particular embodiment, the receptor is a dimerizable receptor. Thus, in an embodiment the hydrophobin (HFB) fusion polypeptide comprising a hydrophobin, and a dimerizable receptor bound to said HFB, wherein the HFB fusion polypeptide recognizes and / or binds to its target molecule by forming a dimer. The HFB fusion polypeptide may comprise a hydrophobin that is naturally occurring, e.g., an HFBI, HFBII, or HFB7, or any other wild-type hydrophobin of any species, e.g. a Trichoderma reesei hydrophobin, or a non-naturally occurring or modified hydrophobin, e.g. a recombinant or mutant hydrophobin that results from the application of a biotechnological technique. In a preferred embodiment, the HFB fusion polypeptide comprises a hydrophobin selected from an HFBI, HFBII, HFB7, or which is a polypeptide of SEQ ID NO: 1-36, preferably the HFB is a polypeptide of SEQ ID NO: 19. In an embodiment, the HFB fusion polypeptide comprises a hydrophobin selected from any one of SEQ ID NO: 1-36, or a polypeptide with at least at least 60%, preferably at least 85% sequence identity to any one of SEQ ID NO: 1-36. Preferably, a polypeptide with at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity to any one sequence of SEQ ID NO: 1-36.More preferably, a polypeptide with at least 85%, at least 86%, with at least 87%, with at least 88%, with at least 89%, with at least 90%, with at least 91%, with at least 92%, with at least 93%, with at least 94%, with at least 95%, with at least 96%, with at least 97%, with at least 98%, or with at least 99% sequence identity to any one sequence of SEQ ID NO: 1-36. In an embodiment, the HFB fusion polypeptide comprises a receptor selected from a Pattern Recognition Receptor (PRR), more specifically, - a Leucine Rich Repeat – Receptor Kinase (LRR-RK), - a Leucine Rich Repeat – Receptor Protein (LRR-RP), - a Lysin motif – Receptor Kinase (LysM-RK) or a Lysin motif – Receptor protein (LysM- RP), - a receptor of SEQ ID NO: 56-63, - AtLORE, AtWAK1, AtLecRK-I.8, AtDORN1, AtLecRK-I.9, AtLLG1-3, AtFER, - a FLS2 comprising amino acid residues R294, H316 and N674, and - a BAK1 comprising amino acid residues T52, L53 and V54. In a preferred embodiment, the HFB fusion polypeptide comprises a receptor selected from a Pattern Recognition Receptor (PRR), more specifically, - a Leucine Rich Repeat – Receptor Kinase (LRR-RK) selected from o FLS2, BAK1, AtFLS2, AtBAK1, SlFLS3, AtEFR, SlCORE, SlSERK3a, AtXPS1, OsXA21, OsSERK2, AtMIK2, OsRLK1, AtNIL31, SlSYR1, SlSYR2, SlPORK1, AtRLK7, atPEPR1, and AtPEPR2, - a Leucine Rich Repeat – Receptor Protein (LRR-RP) selected from o NbCSPR, NbSOBIR1, NbBAK1, AtRLP1, AtSOBIR1, AtBAJ1, AtRLP23, AtSERKs, AtRLP30, AtRLP42, SICf2, SlCf4, SlCf5, SlCf9, SlSOBI1m, SlSOBIR1, SlSERK1 / 3a, SlEIX1, SlEIX2, SlVe1, SmELR, NbRXEG1, BnLepR3, BnRLM2, BnSOBIR1, VuINR, and sLcUrE1, and - a Lysin motif – Receptor Kinase (LysM-RK) or a Lysin motif – Receptor protein (LysM- RP) selected from o OsCEBiP, OsCERK1, AtLYK4, AtLYK5, AtLYM2, LjLYS6, MtLYK9, MtLYR3, MtLYR4, PsLYK9, VvLYK1-1, VvLYK1-2, MdCERK1, AtCERK1, OsLYP4, OsLYP6, OsCERK1, AtLYM1, AtLYM3, AtCERK1, LjEPR3, LjNFR1, LjNFR5, MtLYK3, MtNFP, PsSYM37, PsK, and PsLYR3. - a receptor of SEQ ID NO: 56-63, - AtLORE, AtWAK1, AtLecRK-I.8, AtDORN1, AtLecRK-I.9, AtLLG1-3, AtFER, - a FLS2 comprising amino acid residues R294, H316 and N674, and - a BAK1 comprising amino acid residues T52, L53 and V54. In an embodiment, the HFB and the receptor are linked via a linker sequence. Preferably, wherein said linker sequence is a (GGGGS)X sequence, wherein X is 1, 2, 3 or 4; more preferably wherein X is 2. In an embodiment, the HFB fusion polypeptide comprises a receptor capable of recognizing and / or binding to a target molecule, wherein said target molecule is a selected from a Pathogen- Associated Molecular Pattern (PAMP) and a Microbe-Associated Molecular Pattern (MAMP); preferably wherein said PAMP or MAMP is - a molecule that elicits an LRR-RK response, - a molecule that elicits an LRR-RP response, - a molecule that elicits a LysM-RK or LysM-RP response, - mc-3-OH fatty acid, pectin, oligogalacturonides, egg extract, NAD+, extracellular ATP, and an alkalinization factor, e.g., RALF1 and RALF2. In a preferred embodiment, the HFB fusion polypeptide comprises a receptor capable of recognizing and / or binding to a target molecule selected from - a molecule that elicits a LRR-RK response selected from o flagellin, e.g., flg22, flgll-28 or a fLg22 of SEQ ID NO: 37-55; or a flg22 comprising amino acids L3, D14, D15 and G18, Elongation factor-Tu, e.g. elf18, cold shock proteins, e.g., csp22, xanthine uracil permease, e.g., xup25, proRaxX, e.g., RaxX21, RaxX16, enriched Fusarium oxysporum elicitor EnFOE, nematode proteins, prosystemin, AtprePAMP-induced peptides (AtPIP1-11), and AtproPep 1-8; - a molecule that elicits LRR-RP responses, selected from o Cold shock protein, e.g., csp22, Enigmatic MAMP of Xanthomonas, e.g., eMax, NEP-1 like protein, e.g., nlp20, Sclerotinia culture filtrate elicitor, e.g., SCFE1, polygalacturonase, AVRs, e.g., AVR2, AVR4, AVR5, AVR9, SIRcr-1, SiRcr-2, Ethylene-inducing xylanase, e.g., EIX, Ave1, Elicitin Pre-INF1, XEG1, AvrLm1, AvrLm2, and Chloroplastic ATP synthase, e.g., inceptin, and Cuscuta factor CuF, - a molecule that elicits a LysM-RK or LysM-RP response selected from o chitin, e.g., a CO6 chitin, CO7 chitin or CO8 chitin, 1,3-β-D-glucan(Glc)6, peptidoglycan, chitooligosaccharide, a Nod factor, e.g., lipo- chitooligosaccharides (LCO), exopolysaccharide (EPS), or lipopolysaccharides (LPS), and - mc-3-OH fatty acid, pectin, oligogalacturonides, egg extract, NAD+, extracellular ATP, and an alkalinization factor, e.g., RALF1 and RALF2. In an embodiment, the HFB fusion polypeptide comprises a dimerizable receptor, wherein said receptor is capable of recognizing and / or binding to their target molecule through the formation of a dimer, and consequently, a dimer-target complex. As the person skilled in the art can appreciate from the teachings provided herein, the ability of the HFB fusion polypeptide of the present invention to recognize and / or bind to a particular target molecule is the result of the incorporation of a specific receptor to said HFB fusion polypeptide. In this regard, the HFB fusion polypeptide of the present invention can be modified by a person skilled in the art to incorporate any other receptor capable of recognizing another target molecule, according to their specific needs. Any embodiment resulting from such modification is to be considered as falling within the scope of the present invention. The HFB fusion polypeptide of the second aspect of the present invention comprises a hydrophobin, in any of its embodiments. In a particular embodiment, said hydrophobin is capable of undergoing a conformational change upon being part of a dimer-target complex. As it is known in the art, hydrophobins are capable of generating capsules and / or capable of encapsulating a compound or compounds, favoring their solubility in polar solvents, like water. Furthermore, thanks to the specific characteristics of the HFB fusion polypeptide of the second aspect of the present invention, it is possible to generate an HFB-based capsule of the first aspect of the present invention that’s capable of recognizing and / or binding to a target molecule and triggering its opening as a result of said recognition and / or binding. Thanks to the teachings provided herein, a person skilled in the art will be able to construct any HFB fusion polypeptide by using the adequate techniques known in the art for the construction of fusion polypeptides comprising an HFB, and a receptor according to their required needs. Any of these constructions shall be considered as falling within the scope of the present invention. As demonstrated by the examples of the present application, the HFB-based capsules of the present invention allow the suitable solubilization of compounds in aqueous solvents for their subsequent release in the presence of a specific target molecule, preferably a pathogen- associated molecule (PAMP) or microbes (MAMP). Thanks to this property, the HFB-based capsules of the present invention can be used as a means of administration of compounds that should only exert its effect under specific conditions, e.g., the presence of a pathogen or microbe. Accordingly, it is a third aspect of the invention to provide a composition comprising a) an HFB-based capsule of the first aspect of the present invention, b) at least one suitable excipient, and c) a compound of interest, wherein said compound of interest is encapsulated by the HFB- based capsule. The composition of the third aspect of the invention comprises a compound that is encapsulated by an HFB-based capsule of the first aspect of the present invention. Preferably wherein said compound of interest is a) an antibacterial, e.g., rifampicin, b) an antifungal, e.g., mancozeb, c) an antinematode, e.g. benznidazole, d) an antiviral, e) an antiparasitic, e.g. ivermectin, f) an analgesic, g) a nutraceutical, e.g., resveratrol, or coenzyme Q10, omega 3 h) an essential oil, e.g., lavender oil, tea tree oil, or peppermint oil; i) an industrial chemical, e.g., a dye or a pesticide, or j) a cosmetic ingredient, e.g., retinol, vitamin E or a ceramide. The composition may be formulated in a liquid and / or solid composition. Liquid compositions include emulsions, microemulsions, solutions, suspensions, flowable concentrates, emulsifiable concentrates, gels and the like. Solid compositions include powders, granules, tablets, pellets, pills, pastilles, and the like. The composition may be formulated as a sprayable composition, meaning a composition prepared for immediate spraying through various methods. Alternatively, the formulation can be easily diluted in an adequate polar or non-polar solvent before spraying. In another embodiment, the composition may be applied by any suitable administration route, including but not limited to topical, enteral or parenteral routes. In a preferred embodiment, the composition comprises suitable excipients for an intended purpose selected from surfactants, polar or non-polar solvents, pH buffer, antioxidants, preservatives, defoaming agents, wetting agents, stabilizers, propellants, chelating agents, dispersant agents, acidulants, sweeteners, colorants, flavor enhancers, nutrients, texturizers, gelling agents, among others. The composition of the present invention can be prepared by mixing or blending the ingredients together, e.g., for the preparation of a liquid composition. Alternatively, for the preparation of a solid composition, the process usually requires dry or wet milling. The composition of the present invention may be applied in an effective amount to an organism in need thereto. As used herein, the term "effective amount” refers to an amount sufficient to totally or partially achieve a desired effect, i.e., treating, ameliorating or preventing a disease or disorder. Said amount will depend, among others, on the organism in need, the target disease, the administered compound, the severity of the disease, the route of administration, the biometrical values (size, body weight, body surface or organ size) and / or condition (the age and general health) of the organism in need. The administered amount can be adjusted such that it can be administered to the organism once or over a series of administrations, and in order to obtain the optimal effect. As used herein, the term “organism in need” comprises a plant or animal that may or may not be suffering a disease or disorder, as well as those in which the disease or disorder is to be prevented, wherein said disease or disorder is produced by a pathogen or microbe. More specifically, the term comprises a) a plant selected from main row crops, fruits and vegetables; b) an animal selected from humans and other primates (e.g. apes and monkeys), farm animals (e.g. cattle, sheep, pigs, goats, horses), pets and other domestic animals (e.g. dogs, cats), laboratory animals (e.g. mice, rats, guinea pigs, rabbits), birds and poultry (chickens, turkeys, ducks, geese). When referring to an animal organism, the term “organism” and “organism in need” may be interchangeably used with the term “subject” or “subject in need”, correspondingly. As a person skilled in the art would recognize, the composition of the third aspect of the present invention can be used for different purposes, depending on the specific compound of interest that’s encapsulated by the HFB-based capsule to be delivered. Thus, the specific technical field of the composition depends on the nature of the compound delivered by the composition of the present invention. It is within the knowledge of a person skilled in the art the ability to produce a composition suitable for the delivery of an HFB-based capsule of the first aspect of the present invention and a compound of interest encapsulated by it. Likewise, the excipients specifically selected for the formulation of a composition of the present invention will depend on the technical field, i.e., the composition will comprise different excipients according to the intended use. Accordingly, the composition of the third aspect of the present invention can be designed, for example, for agronomical, gastronomical or pharmaceutical purposes. Thus, in an embodiment, the composition of the third aspect of the present invention comprises an agronomical composition comprising a) an HFB-based capsule of the first aspect of the present invention, b) at least one agronomically suitable excipient, and c) an agronomical compound, wherein said agronomical compound is encapsulated by the HFB-based capsule. As used herein, an “agronomical compound” refers to a molecule that can be administered to a plant for the treatment, amelioration or prevention of a disease or disorder. Preferably, the agronomical compound is administered in an amount that results in a total or partial treatment, amelioration or prevention of said disease or disorder. Accordingly, an “agronomical composition” refers to a composition comprising an agronomical compound. The agronomical compound comprises a compound, preferably selected from an antibacterial, an antifungal, an antinematode, and an antiviral compound. In another embodiment, the agronomical compound comprises a compound for enhancing a plant’s growth, health and / or productivity. Said compounds may include, but are not limited to a) a fertilizer, e.g., nitrogen-based fertilizer, phosphorus-based fertilizer, and potassium- based fertilizer; b) a soil amendment, e.g., lime, gypsum, or compost; c) a plant growth regulator, e.g., auxins, cytokinins, or gibberellins; d) a micronutrient, e.g., iron, zinc, and manganese; e) a biostimulant, e.g., humic acid, fulvic acid, and seaweed extract; or f) a biofertilizers, e.g., a nitrogen-fixing bacteria, a phosphate-solubilizing bacteria, or a mycorrhizal fungus. The agronomical composition may be formulated in a liquid and / or solid composition. Liquid compositions include emulsions, microemulsions, solutions, suspensions, flowable concentrates, emulsifiable concentrates, gels and the like. Solid compositions include powders, granules, tablets, pellets, pills, pastilles, and the like. The agronomical composition may be formulated as a sprayable composition, meaning a composition prepared for immediate spraying through various methods. Alternatively, the formulation can be easily diluted in an adequate polar or non- polar solvent before spraying. In a preferred embodiment, the agronomical composition comprises agronomically suitable excipients selected from surfactants, polar or non-polar solvents, pH buffer, antioxidants, preservatives, defoaming agents, wetting agents, stabilizers, propellants, chelating agents, and dispersant agents, among others. The agronomical composition of the present invention can be prepared by mixing or blending the ingredients together, e.g., for the preparation of a liquid composition. Alternatively, for the preparation of a solid composition, the process usually requires dry or wet milling. The agronomical composition may be applied to a target plant or the soil wherein said target plant grows. Preferably, the composition may be applied to any part of said target plant, comprising a surface of any said part of the plant, including seeds, leaves, flowers, stems, tubers, roots, or combinations thereof, preferably the leaves of a plant. In an embodiment, the agronomical composition may be applied to a plant selected from main row crops, fruits and vegetables. More preferably, to a plant selected from soybean, maize, wheat, apple, pear, and berries, e.g. bananas, blueberries, cranberries, coffee berries, gooseberries, redberry, blackberry and white currants, tomato, grapes and pepper. The plant to which the agronomical composition is applied may or may not be affected by a pathogen or microbe, preferably wherein said pathogen or microbe comprising a Pathogen- Associated Molecular Pattern (PAMP) or a Microbe-Associated Molecular Pattern (MAMP). More preferably, said pathogen or microbe comprises - A molecule that elicits an LRR-RK response, - a molecule that elicits an LRR-RP response, - a molecule that elicits a LysM-RK or LysM-RP response, - mc-3-OH fatty acid, pectin, oligogalacturonides, egg extract, NAD+, extracellular ATP, and an alkalinization factor, e.g., RALF1 and RALF2. The plant to which the agronomical composition is applied may or may not be affected by a pathogen or microbe. In an embodiment, the pathogen or microbe affecting the plant is selected from a) a bacterium, e.g. Xanthomonas spp., Pseudomonas spp, more preferably, Xanthomonas campestris, Pseudomonas syringae; b) a fungus, e.g., Cercospora spp., Exserohilum spp., Fusarium spp., Botrytis spp., Phytophthora spp., more preferably, Cercospora sojinia, Exserohilum turcicum, Fusarium graminearum, Botrytis cinerea, Phytophthora sojae; c) a nematode, e.g., Meloidogyne spp., more preferably, Meloidogyne exigua; and d) a virus, e.g., Tobacco mosaic virus, or Tomato yellow curl virus. As disclosed above, the composition of the third aspect of the present invention can be designed for agronomical, gastronomical, or pharmaceutical purposes. Thus, in an embodiment, the composition of the third aspect of the present invention comprises a gastronomical composition comprising a) an HFB-based capsule of the first aspect of the present invention, b) at least one gastronomically suitable excipient, and c) a gastronomical compound, wherein said gastronomical compound is encapsulated by the HFB-based capsule. As used herein, the term “gastronomical compound” refers to a compound that can be administered to a food product for the treatment, amelioration or prevention of a disease- Preferably, the gastronomical compound is administered in an amount that results in a total or partial treatment, amelioration or prevention of said disease. Accordingly, an “gastronomical composition” refers to a composition comprising a pharmaceutical compound. The term also refers to a compound that’s suitable for its application in a food product, and that can be in contact or mixed with other compounds that are suitable for a food product. In an embodiment, the composition comprises a gastronomical compound. Preferably a gastronomical compound selected from an antibacterial, an antifungal, an antinematode, an antiviral, an antiparasitic, an analgesic, a nutraceutical, and a colorant compound. In an embodiment, the gastronomical compound may be selected from compounds for the detection or prevention of reproduction of a pathogen. Preferably, a pathogen selected from a) a bacterium, e.g., Escherichia spp., Salmonella spp., Staphylococcus spp., Pseudomonas spp., more preferably, Escherichia coli, Salmonella typhimurium, Staphylococcus aureus, and Pseudomonas aureginosa; b) a fungus, e.g., Fusarium spp., Candida spp., Aspergillus spp., Spiroplasma spp.; more preferably, Fusarium solani, Candida albicans, Aspergillus fumigatus, and Spiroplasma kunkelii; c) a nematode, e.g., Ascaris spp., more preferably, Ascaris lumbricoides; d) a virus, e.g., Influenza virus, and Herpes simplex virus; and e) a parasite, e.g., Plasmodium spp., and Trypanozoma spp., more preferably, Plasmodium falciparum, and Trypanozoma cruzi. The gastronomical composition may be formulated in a liquid and / or solid composition. Liquid compositions include emulsions, microemulsions, solutions, suspensions, flowable concentrates, emulsifiable concentrates, gels and the like. Solid compositions include powders, granules, tablets, pellets, pills, pastilles, and the like. The gastronomical composition may be formulated as a sprayable composition, meaning a composition prepared for immediate spraying through various methods. Alternatively, the formulation can be easily diluted in an adequate polar or non- polar solvent before spraying. In a preferred embodiment, the gastronomical composition comprises gastronomically suitable excipients selected from surfactants, polar or non-polar solvents, pH buffer, antioxidants, preservatives, wetting agents, stabilizers, acidulants, sweeteners, colorants, flavor enhancers, nutrients, texturizers, gelling agents among others. The gastronomical composition of the present invention can be prepared by mixing or blending the ingredients together, e.g., for the preparation of a liquid composition. Alternatively, for the preparation of a solid composition, the process usually requires dry or wet milling. The gastronomical composition may be applied to a food product directly, for example to dairy products e.g., yogurt, milk, bakery products, e.g. bread, and meat-based products, e.g. chicken, pork, beef, etc. The food product to which the gastronomical composition is applied may or may not comprise a pathogen or microbe, preferably wherein said pathogen or microbe comprises a Pathogen- Associated Molecular Pattern (PAMP) or a Microbe-Associated Molecular Pattern (MAMP). More preferably, said pathogen or microbe comprises - a molecule that elicits an LRR-RK response, - a molecule that elicits an LRR-RP response, - a molecule that elicits a LysM-RK or LysM-RP response, - mc-3-OH fatty acid, pectin, oligogalacturonides, egg extract, NAD+, extracellular ATP, or an alkalinization factors, e.g., RALF1 or RALF2. In an embodiment, food product comprises a pathogen or microbe, preferably selected from a) a bacterium, e.g., Escherichia spp., Salmonella spp., Staphylococcus spp., Pseudomonas spp., more preferably, Escherichia coli, Salmonella typhimurium, Staphylococcus aureus, and Pseudomonas aureginosa; b) a fungus, e.g., Fusarium spp., Candida spp., Aspergillus spp., Spiroplasma spp., more preferably, Fusarium solani, Candida albicans, Aspergillus fumigatus, and Spiroplasma kunkelii; c) a nematode, e.g., Ascaris spp., more preferably, Ascaris lumbricoides; d) a virus, e.g., Influenza virus, Herpes simplex virus; and e) a parasite, e.g., Plasmodium spp., and Trypanozoma spp., more preferably, Plasmodium falciparum, and Trypanozoma cruzi. In another embodiment, the gastronomical composition may be applied to an organism in need, wherein said organism comprises humans and other primates (e.g. apes and monkeys), farm animals (e.g. cattle, sheep, pigs, goats, horses), pets and other domestic animals (e.g. dogs, cats), laboratory animals (e.g. mice, rats, guinea pigs, rabbits), birds and poultry (chickens, turkeys, ducks, geese). The subject to which the gastronomical composition is applied may or may not be affected by a pathogen or microbe, preferably wherein said pathogen or microbe comprises a Pathogen- Associated Molecular Pattern (PAMP) or a Microbe-Associated Molecular Pattern (MAMP). More preferably, said pathogen or microbe comprises - a molecule that elicits an LRR-RK response, - a molecule that elicits an LRR-RP response, - a molecule that elicits a LysM-RK or LysM-RP response, - mc-3-OH fatty acid, pectin, oligogalacturonides, egg extract, NAD+, extracellular ATP, or an alkalinization factors, e.g., RALF1 or RALF2. In an embodiment, the pathogen or microbe affecting the organism in need is selected from a a) a bacterium, e.g., Escherichia spp., Salmonella spp., Staphylococcus spp., Pseudomonas spp., more preferably, Escherichia coli, Salmonella typhimurium, Staphylococcus aureus, and Pseudomonas aureginosa; b) a fungus, e.g., Fusarium spp., Candida spp., Aspergillus spp., Spiroplasma spp., more preferably, Fusarium solani, Candida albicans, Aspergillus fumigatus, and Spiroplasma kunkelii; c) a nematode, e.g., Ascaris spp., more preferably, Ascaris lumbricoides; d) a virus, e.g., Influenza virus, Herpes simplex virus; and e) a parasite, e.g., Plasmodium spp., and Trypanozoma spp., more preferably, Plasmodium falciparum, and Trypanozoma cruzi. In an embodiment, the gastronomical composition is applied to an organism in need by the consumption of a food product to which a gastronomical composition of the present invention has been applied to. That is, the application of the gastronomical composition to an organism in need thereof is done indirectly. As disclosed above, the composition of the third aspect of the present invention can be designed for agronomical, gastronomical, or pharmaceutical purposes. Thus, in an embodiment, the composition of the third aspect of the present invention comprises a pharmaceutical composition comprising a) an HFB-based capsule of the first aspect of the present invention, b) at least one pharmaceutically suitable excipient, and c) a pharmaceutical compound, wherein said pharmaceutical compound is encapsulated by the HFB-based capsule. As used herein a “pharmaceutical compound” refers to a molecule that can be administered to an organism in need for the treatment, amelioration or prevention of a disease. Preferably, the pharmaceutical compound is administered in an amount that results in a total or partial treatment, amelioration or prevention of said disease. Accordingly, an “pharmaceutical composition” refers to a composition comprising a pharmaceutical compound. The pharmaceutical compound comprises a hydrophobic compound. The pharmaceutical composition may be formulated in a liquid and / or solid composition. Liquid compositions include emulsions, microemulsions, solutions, suspensions, flowable concentrates, emulsifiable concentrates, gels and the like. Solid compositions include powders, granules, tablets, pellets, pills, pastilles, and the like. The pharmaceutical composition may be formulated as a sprayable composition, meaning a composition prepared for immediate spraying through various methods. Alternatively, the formulation can be easily diluted in an adequate polar or non- polar solvent before spraying. In a preferred embodiment, the pharmaceutical composition comprises pharmaceutically suitable excipients selected from surfactants, polar or non-polar solvents, pH buffer, antioxidants, preservatives, defoaming agents, wetting agents, stabilizers, propellants, chelating agents, and dispersant agents, among others. The pharmaceutical composition of the present invention can be prepared by mixing or blending the ingredients together, e.g., for the preparation of a liquid composition. Alternatively, for the preparation of a solid composition, the process usually requires dry or wet milling. The pharmaceutical composition may be applied by any suitable administration route, including but not limited to topical, enteral or parenteral routes. In an embodiment, the pharmaceutical compound is selected for the treatment, amelioration or prevention of a disease or disorder associated with pathogens, including but not limited to diseases or disorders associated with a) a bacterium, e.g. Escherichia spp., Salmonella spp., Staphylococcus spp., Pseudomonas spp., more preferably, Escherichia coli, Salmonella typhimurium, Staphylococcus aureus, Pseudomonas aureginosa; b) a fungus, e.g., Fusarium spp., Candida spp., Aspergillus spp., Spiroplasma spp., more preferably, Fusarium solani, Candida albicans, Aspergillus fumigatus, Spiroplasma kunkelii; c) a nematode, e.g., Ascaris spp., e.g. Ascaris lumbricoides; d) a virus, e.g., Influenza virus, Herpes simplex virus; e) a parasite, e.g., Plasmodium spp., Trypanozoma spp., e.g., Plasmodium falciparum, Trypanozoma cruzi. The pharmaceutical composition may be applied to an organism in need, wherein said organism in need comprises humans and other primates (e.g. apes and monkeys), farm animals (e.g. cattle, sheep, pigs, goats, horses), pets and other domestic animals (e.g. dogs, cats), laboratory animals (e.g. mice, rats, guinea pigs, rabbits), birds and poultry (chickens, turkeys, ducks, geese). The subject to which the pharmaceutical composition is applied may or may not be affected by a pathogen or microbe, preferably wherein said pathogen or microbe comprises a Pathogen- Associated Molecular Pattern (PAMP) or a Microbe-Associated Molecular Pattern (MAMP). More preferably, said pathogen or microbe comprises - a molecule that elicits an LRR-RK response, - a molecule that elicits an LRR-RP response, - a molecule that elicits a LysM-RK or LysM-RP response, - mc-3-OH fatty acid, pectin, oligogalacturonides, egg extract, NAD+, extracellular ATP, or an alkalinization factors, e.g., RALF1 or RALF2. In an embodiment, the pathogen or microbe affecting the organism in need is selected from a) a bacterium, e.g., Escherichia spp., Salmonella spp., Staphylococcus spp., Pseudomonas spp., more preferably, Escherichia coli, Salmonella typhimurium, Staphylococcus aureus, and Pseudomonas aureginosa; b) a fungus, e.g., Fusarium spp., Candida spp., Aspergillus spp., Spiroplasma spp., more preferably, Fusarium solani, Candida albicans, Aspergillus fumigatus; and Spiroplasma kunkelii; c) a nematode, e.g., Ascaris spp., more preferably, and Ascaris lumbricoides; d) a virus, e.g., Influenza virus, Herpes simplex virus; and e) a parasite, e.g., Plasmodium spp., and Trypanozoma spp., more preferably, Plasmodium falciparum, and Trypanozoma cruzi. In this regard, it can be appreciated from the teachings of the present application that the compositions of the third aspect of the present invention and / or the HFB-based capsules of the first aspect of the present invention allow the application of a wide variety of compounds for various purposes, both for use in the agronomic industry, gastronomic industry and in the pharmaceutical industry. The release of these compounds occurs as a result of the recognition and binding of an HFB fusion polypeptide of the second aspect of the invention to its target molecule, thus generating the opening of the capsule comprised within the composition of the third aspect of the invention. It is a fourth aspect of the present invention a method of application of a compound of interest, comprising the steps of a) providing a composition of the third aspect of the present invention, b) applying an effective amount of the composition of the third aspect of the present invention to an organism in need, c) contacting an HFB-based capsule of the first aspect of the present invention with a target molecule, wherein the HFB-based capsule encapsulates said compound of interest with a target molecule. In an embodiment, the method of application of a compound of interest of the present invention comprises applying an agronomical composition. The method comprises applying an agronomical composition comprising an agronomical compound, wherein said compound is encapsulated by an HFB-based capsule of the first aspect of the present invention. The method comprises applying an agronomical composition formulated in a liquid and / or solid composition. Liquid compositions include emulsions, microemulsions, solutions, suspensions, flowable concentrates, emulsifiable concentrates, gels and the like. Solid compositions include powders, granules, tablets, pellets, pills, pastilles, and the like. The agronomical composition may be formulated as a sprayable composition, meaning a composition prepared for immediate spraying through various methods. Alternatively, the formulation can be easily diluted in an adequate polar or non-polar solvent before spraying. In a preferred embodiment, the method comprises applying an agronomical composition comprising agronomically suitable excipients selected from surfactants, polar or non-polar solvents, pH buffer, antioxidants, preservatives, defoaming agents, wetting agents, stabilizers, propellants, chelating agents, and dispersant agents, among others. When applying an agronomical composition, the “organism in need” comprises a target plant in need thereof. Preferably, a plant selected from main row crops, fruits and vegetables. More preferably, a plant selected from soybean, maize, wheat, apple, pear, and berries, e.g. bananas, blueberries, cranberries, coffee berries, gooseberries, redberry, blackberry and white currants, tomato, grapes and pepper. In an embodiment, the method comprises applying an agronomical composition to a target plant or the soil where the target plant grows. Preferably, applying the agronomical composition to any part of said target plant, comprising a surface of any said part of the plant, including seeds, leaves, flowers, stems, tubers, roots, or combinations thereof. The plant subjected to the method of application of the fourth aspect of the present invention may or may not be affected by a pathogen or microbe, preferably wherein said pathogen or microbe comprising a Pathogen-Associated Molecular Pattern (PAMP) or a Microbe-Associated Molecular Pattern (MAMP). More preferably, said pathogen or microbe comprises d) A molecule that elicits an LRR-RK response, e) a molecule that elicits an LRR-RP response, f) a molecule that elicits a LysM-RK or LysM-RP response, g) mc-3-OH fatty acid, pectin, oligogalacturonides, egg extract, NAD+, extracellular ATP, or an alkalinization factors, e.g., RALF1 or RALF2. In an embodiment, the pathogen or microbe affecting the plant is selected from a) a bacterium, e.g. Xanthomonas spp., Pseudomonas spp, more preferably, Xanthomonas campestris, and Pseudomonas syringae; b) a fungus, e.g., Cercospora spp., Exserohilum spp., Fusarium spp., Botrytis spp., Phytophthora spp., more preferably, Cercospora sojinia, Exserohilum turcicum, Fusarium graminearum, Botrytis cinerea, and Phytophthora sojae; c) a nematode, e.g., Meloidogyne spp., more preferably, Meloidogyne exigua; and d) a virus, e.g., Tobacco mosaic virus, and Tomato yellow curl virus. In another embodiment, the method of application of a compound of interest of the present invention comprises applying a gastronomical composition The method comprises applying a gastronomical composition comprising a gastronomical compound, wherein said compound is encapsulated by an HFB-based capsule of the first aspect of the present invention. Preferably wherein said gastronomical compound is a hydrophobic compound. The method comprises applying a gastronomical composition formulated in a liquid and / or solid composition. Liquid compositions include emulsions, microemulsions, solutions, suspensions, flowable concentrates, emulsifiable concentrates, gels and the like. Solid compositions include powders, granules, tablets, pellets, pills, pastilles, and the like. The gastronomical composition may be formulated as a sprayable composition, meaning a composition prepared for immediate spraying through various methods. Alternatively, the formulation can be easily diluted in an adequate polar or non-polar solvent before spraying. In a preferred embodiment, the method comprises applying a gastronomical composition comprises gastronomically suitable excipients selected from surfactants, polar or non-polar solvents, pH buffer, antioxidants, preservatives, defoaming agents, wetting agents, stabilizers, propellants, chelating agents, and dispersant agents, among others. In an embodiment, the method of application of the gastronomical composition comprises any suitable administration route, including but not limited to oral routes. When applying a gastronomical composition, the “organism in need” comprises humans and other primates (e.g. apes and monkeys), farm animals (e.g. cattle, sheep, pigs, goats, horses), pets and other domestic animals (e.g. dogs, cats), laboratory animals (e.g. mice, rats, guinea pigs, rabbits), birds and poultry (chickens, turkeys, ducks, geese). Furthermore, a subject comprises a subject who may or may not suffer a disorder, as well as those in which the disorder is to be prevented. The organism subjected to the method of application of the fourth aspect of the present invention may or may not be affected by a pathogen or microbe, preferably wherein said pathogen or microbe comprises a Pathogen-Associated Molecular Pattern (PAMP) or a Microbe-Associated Molecular Pattern (MAMP). More preferably, said pathogen or microbe comprises h) a molecule that elicits an LRR-RK response, i) a molecule that elicits an LRR-RP response, j) a molecule that elicits a LysM-RK or LysM-RP response, k) mc-3-OH fatty acid, pectin, oligogalacturonides, egg extract, NAD+, extracellular ATP, or an alkalinization factor, e.g., RALF1 or RALF2. In an embodiment, the pathogen or microbe affecting the subject is selected from a) a bacterium, e.g., Escherichia spp., Salmonella spp., Staphylococcus spp., Pseudomonas spp., more preferably, Escherichia coli, Salmonella typhimurium, Staphylococcus aureus, and Pseudomonas aureginosa; b) a fungus, e.g., Fusarium spp., Candida spp., Aspergillus spp., Spiroplasma spp., more preferably, Fusarium solani, Candida albicans, Aspergillus fumigatus; and Spiroplasma kunkelii, c) a nematode, e.g., Ascaris spp., more preferably, Ascaris lumbricoides; d) a virus, e.g., Influenza virus, Herpes simplex virus; and e) a parasite, e.g., Plasmodium spp., and Trypanozoma spp., more preferably, Plasmodium falciparum, and Trypanozoma cruzi. In another embodiment, the method of application of a compound of interest of the present invention comprises applying a pharmaceutical composition. The method comprises applying a pharmaceutical composition comprising a pharmaceutical compound, wherein said compound is encapsulated by an HFB-based capsule of the first aspect of the present invention. Preferably wherein said pharmaceutical compound is a hydrophobic compound. The method comprises applying a pharmaceutical composition formulated in a liquid and / or solid composition. Liquid compositions include emulsions, microemulsions, solutions, suspensions, flowable concentrates, emulsifiable concentrates, gels and the like. Solid compositions include powders, granules, tablets, pellets, pills, pastilles, and the like. The pharmaceutical composition may be formulated as a sprayable composition, meaning a composition prepared for immediate spraying through various methods. Alternatively, the formulation can be easily diluted in an adequate polar or non-polar solvent before spraying. In a preferred embodiment, the method comprises applying a pharmaceutical composition comprises pharmaceutically suitable excipients selected from surfactants, polar or non-polar solvents, pH buffer, antioxidants, preservatives, defoaming agents, wetting agents, stabilizers, propellants, chelating agents, and dispersant agents, among others. In an embodiment, the method of application of the pharmaceutical composition comprises any suitable administration route, including but not limited to topical, enteral or parenteral routes. When applying a pharmaceutical composition, the “organism in need” comprises humans and other primates (e.g. apes and monkeys), farm animals (e.g. cattle, sheep, pigs, goats, horses), pets and other domestic animals (e.g. dogs, cats), laboratory animals (e.g. mice, rats, guinea pigs, rabbits), birds and poultry (chickens, turkeys, ducks, geese). Furthermore, a subject comprises a subject who may or may not suffer a disorder, as well as those in which the disorder is to be prevented. The organism subjected to the method of application of the fourth aspect of the present invention may or may not be affected by a pathogen or microbe, preferably wherein said pathogen or microbe comprises a Pathogen-Associated Molecular Pattern (PAMP) or a Microbe-Associated Molecular Pattern (MAMP). More preferably, said pathogen or microbe comprises l) a molecule that elicits an LRR-RK response, m) a molecule that elicits an LRR-RP response, n) a molecule that elicits a LysM-RK or LysM-RP response, o) mc-3-OH fatty acid, pectin, oligogalacturonides, egg extract, NAD+, extracellular ATP, or an alkalinization factor , e.g., RALF1 or RALF2. In an embodiment, the pathogen or microbe affecting the subject is selected from f) a bacterium, e.g., Escherichia spp., Salmonella spp., Staphylococcus spp., Pseudomonas spp., more preferably, Escherichia coli, Salmonella typhimurium, Staphylococcus aureus, and Pseudomonas aureginosa; g) a fungus, e.g., Fusarium spp., Candida spp., Aspergillus spp., Spiroplasma spp., more preferably, Fusarium solani, Candida albicans, Aspergillus fumigatus; and Spiroplasma kunkelii; h) a nematode, e.g., Ascaris spp., more preferably, Ascaris lumbricoides; i) a virus, e.g., Influenza virus, Herpes simplex virus; and j) a parasite, e.g., Plasmodium spp., and Trypanozoma spp., more preferably, Plasmodium falciparum, and Trypanozoma cruzi. Each and every embodiment of the objects, methods, and / or aspects of the present invention resulting from the combination of particular embodiments described herein are to be considered as falling within the scope of the present invention. It is a fifth aspect of the present invention a method of detection of a pathogen or microbe of interest, comprising the steps of a) providing an HFB-based capsule of the first aspect of the present invention and a reporter compound encapsulated by the HFB-based capsule. b) contacting the HFB-based capsule of step a) with a sample that may or may not contain a target pathogen or microbe, c) revealing the contact of step b) by measuring the release or lack of release of the reporter compound. The term “sample” as used herein, refers to a portion obtained from an organism that may or may not be suffering from a disorder or disease, or from a food product that may or may or may not be contaminated with a pathogen or microbe of interest. The HFB-based capsule of step a) comprises any embodiment of the HFB-based capsule as previously described in the present Specification. The reporter compound encapsulated by the HFB-based capsule, comprises any compound suitable for the detection or revealing through any technique known by a person skilled in the art. Non-limiting examples of reporter compounds are chromophores, fluorophores, colorants, and radio-isotopes. The pathogen or microbe of step b) may comprise a pathogen or microbe comprising a Pathogen- Associated Molecular Pattern (PAMP) or a Microbe-Associated Molecular Pattern (MAMP). In another embodiment, the pathogen or microbe is selected from a) a bacterium, e.g., Escherichia spp., Salmonella spp., Staphylococcus spp., Xanthomonas spp., and Pseudomonas spp.; b) a fungus, e.g., Cercospora spp., Exserohilum spp., Fusarium spp., Botrytis spp., Phytophthora spp., Candida spp., Aspergillus spp., and Spiroplasma spp.; c) a nematode, e.g., Meloidogyne spp., and Ascaris spp.; d) a virus, e.g., Tomato mosaic virus, Tomato yellow curl virus, Influenza virus, Herpes simplex virus; and e) a parasite, e.g., Plasmodium spp., and Trypanozoma spp. More preferably, the pathogen or microbe is selected from a) a bacterium, e.g., Escherichia spp., Salmonella spp., Staphylococcus spp., Xanthomonas spp., Pseudomonas spp., more preferably, Escherichia coli, Salmonella typhimurium, Staphylococcus aureus, Xanthomonas campestris, Pseudomonas syringae, and Pseudomonas aureginosa; b) a fungus, e.g., Cercospora spp., Exserohilum spp., Fusarium spp., Botrytis spp., Phytophthora spp., Candida spp., Aspergillus spp., Spiroplasma spp., more preferably, Cercospora sojinia, Exserohilum turcicum, Fusarium graminearum, Fusarium solani, Botrytis cinerea, Phytophthora sojae, Candida albicans, Aspergillus fumigatus, and Spiroplasma kunkelii; c) a nematode, e.g., Meloidogyne spp., Ascaris spp., more preferably, Meloidogyne exigua, Ascaris lumbricoides; and d) a virus, e.g., Tomato mosaic virus, Tomato yellow curl virus, Influenza virus, and Herpes simplex virus; The revealing of step c) may be performed by a person skilled in the art by any technique known in the art. For example, and without intent of limiting the scope of the present invention, techniques for revealing a reporter compound comprise direct visual observation, optical microscopy, fluorescence microscopy, radiometry. EXAMPLES The examples presented herein shall be understood only as exemplary embodiments of the different objects, methods and aspects of the present invention without intent to limit the scope thereof in any way. EXAMPLE 1 - STRUCTURAL ANALYSIS OF THE LRR-RK AND LRR-RP BINDING METHOD Example 1.1 – Receptor searching Pattern-triggered immunity (PTI) relates to the ability of multicellular eukaryotic organisms to employ pattern recognition receptors (PRRs) to detect microbial structures, called pathogen- or microorganism-associated patterns (PAMP / MAMPs). Plants recognize patterns on the cell surface through membrane-localized PRRs. Depending on the presence or absence of an intracellular kinase domain, PRRs are classified as receptor kinases (RK) or receptor proteins (RP), respectively. A) LEUCINE-RICH REPEAT-RKS Leucine-rich repeat RKs (LRR-RKs) in plants typically recognize protein ligands and are involved in developmental and immune processes. In plants, LRR-RKs comprise a prolific family of several hundred proteins grouped into different clades. The leucine-rich repeat receptor-like kinase gene TaLRRK-6D is induced in wheat by DON treatment during the early stage of F. graminearum infection. Inhibition of TaLRRK-6D compromises wheat resistance to F. graminearum by suppressing the expression of salicylic acid signaling genes, including ICS1, PAL, NPR1, NPR3-like and NPR4. Table 1. Main LRR-RK and LRR-RP receptors identified. Adapted from Albert et al., 2020. Receptor complex Pattern Pattern origin AtFLS2, AtBAK1 FLG22 bacteria SlFLS3, BAK1 FLGII-28 bacteria AtEFR, Atbak1 elf18 bacteria LRR-RK SlCORE, SlSERK3 csp22 bacteria AtXPS1 xup25 bacteria OsXA21, OsSERK2 RaxX21 / RaxX26 Xanthomonas oryzae pv. Oryzae AtMIK2, AtBAK1 EnFoE Fusarium spp. OsRLK1 u.i. herbivores AtNILR1, AtBAK1 nematode water nematodes SlSYR1, SlSYR2, SlPORK1 prosystemin (systemin) plants AtRLK7, AtBAK1 AtPIP1-11 plants AtPEPR1, AtPEPR2, AtBAK1 AtPep 1-8 plants NbCSPR, NbSOBR1, NbBAK1 csp22 bacteria AtRLP1, AtSOBIR1, enmigatic MAMP of AtBAK1 xnathomonas Xanthomonas spp. AtRLP23, AtSOBIR1, AtSERKs NLP20 bacteria, oomycetes, fungi AtRLP30, AtSOBIR1, AtBAK1 SCFE1 Sclerotina sclerotiorum AtRLP42, AtSOBIR1 polygalacturonase fungi SlCf2, SlSOBIR1 AVR2 / SlRcr3 Cladosporium fulvum SlCf4, SlSOBIR1, SlSERK1 / 3A AVR4 Cladosporium fulvum SlCF5 AVR5 Cladosporium fulvum SlCf9, SlSOBIR1, SlSERK1 / 3A AVR9 / SlRcr-1, SlRcr2 Cladosporium fulvum SlEIX2, SlEIX1, SOBIR1, ethylene-inducing xylanase BAK1 EIX Trichoderma spp. Verticillium, fusarium, slve1, SlSOBIR1 Ave1 Colleotrichum spp. SmELR, SOBIR1, BAK1 INF1 Phytophthora, Phytium spp. NbRXEG1, SOBIR1, BAK1 XEG1 Phytophthora sojarium BnLepR3 / BnRLM2, BnSOBIR1 AvrLm1 / AvrLm2 Leptosphaeria maculans Plants treated with Spododoptera VulNR, SOBIR1, BAK1 inceptin exigua LRR-RP SlCuRe1, SlSOBIR1 Cuscuta factor CuF Cuscuta reflexa B) LYSIN MOTIF-RKS AND RPS Plants detect polysaccharide patterns using lysine motif (LysM) receptors. LysM-RKs contain three extracellular LysM domains, a transmembrane domain and an intracellular kinase domain. LysM-RPs lack kinase and transmembrane domains, instead they are bound to the plasma membrane by GPI anchors. Compared to the LRR receptor family, the LysM receptor family is smaller, comprising five to 22 LysM-RKs and two to five LysM-RPs. LysM-RK and -RP contribute to both immunity and symbiosis by sensing N-acetylglucosamine- containing patterns, such as lipochitooligosaccharides, chitooligosaccharides (CO) and peptidoglycan (PGN). The interaction between receptors and coreceptors appears to be complex, especially in distinguishing between defense and symbiosis. Table 2. Main LysM-RK and LysM-RP receptors identified. Adapted from Albert et al., 2020. Pattern Receptor complex Pattern origin OsCEBIP, OsCERK1 chitin (CO8) fungi AtLYK4, AtLYK5, AtCERK1 chitin fungi AtLYK4, AtLYK5, AtLYM2 chitin fungi LjLYS6 chitin (CO6-8) fungi MtLYK9, MtLYR4 chitin fungi PsLYK9 chitin fungi VvLYK1-1, VvLYK1-2 chitin fungi MdCERK1 chitin fungi LysM-RK / RP AtCERK1 1,3-beta-Glucan fungi fungi, OsLYP4, OsLYP6, OsCERK1 chitin (CO6), peptidoglycan bacteria AtLYM1, AtLYM3, AtCERK1 peptidoglycan bacteria LjNFR1, LjNFR3 Nod factors (LCO) bacteria MtLYK3, MtNFP, MtLYR3 Nod factors (LCO) bacteria PsSYM37, PsK, PsLYR3 Nod factors (LCO) bacteria MtLYK9 chitooligosaccharides (CO) bacteria LjEPR3 exopolysaccharides (EPS) bacteria OsCERK1 lipopolysaccharides (LPS) bacteria C) OTHER TYPE OF RECEPTORS The EGF domain-like receptor kinase AtWAK1 senses oligogalacturonide (OG), which is released from pectin during fungal infection. Table 3. Other receptors identified. Adapted from Albert et al.2020. Pattern Receptor complex Pattern origin AtLORE mc-3-OH fatty acid bacteria AtWAK1 pectin fungi OTHER AtLecRK-1.8 egg extract (u.i.) insects RECEPTORS AtLecRK-1.8 NAD+ plants AtDORN1 Extracellular ATP plants AtLLF1.3, AtFER rapid alkalinization factors plants Further receptors identified include, but are not limited to, - Receptor of bacterial antigens, such as AtFLS2 for binding to flg22, AtEFR for binding to elf18, AtXPS1 for binding to XUP25, AtRLP1 for binding to eMAX, AtRLP32 for binding to IF1, AtLYM1 / 3 for binding to PG, AtLORE for binding to 3-OH, OsXa21 for binding to Raxx21, OsLYP4 / 6 for binding to PG and chitin, SlCORE / NbCSPR for binding to csp22, and LjEPR3 for binding to EPS; - Receptor of fungal antigens, such as AtMIK2 for binding to SCOOP (Fo), AtLYK2 / 4 / 5 for binding to chitin, AtRLP30 for binding to SCFE1, AtLRP42 for binding to Endo-PG, AtWAK ½ for binding to OG, SlCF-2 / 4 / 5 / 9 for binding to Avr2 / 4 / 5 / 9, SlEIX2 for binding to EIX, SlVe1 for binding to Ave1, SlI for binding to Avr1, SlI-3 for binding to Avr3, BnRLM2 for binding to AvrLM1 / 2, MtLYK 4 / 9 for binding to chitin, VvLYK1-1 / 2 for binding to chitin, LjLYS6 for binding to chitin, PsLYK9 for binding to chitin, TaWAK for binding to TOX1; - Receptor of oomycetes antigens, such as At-RLP23 for binding to nlp20(Pp), Nb.RXEG1 for binding to XEG1, Sm-ELR for binding to INF1, AtRDA2 for binding to Pi-CER D; - Receptor of self molecules, such as AtMIK2 for binding to SCOOP (At), AtPEPR1 / 2 for binding to AtPeps, AtHSL3 for binding to AtCTNIPs, AtFER for binding to AtRALF, AtRLK7 for binding to AtPIP1, AtHPCA1 for binding to eH2O2 and DMBQ, At-DORN1 for binding to e-ATP, AtLecRK1.8 for binding to e-NAD+, SlSYR1 / 2 for binding to systemin; - Receptor of parasitic plant antigens, such as AtCARD1 for binding to DMBQ, SlCuRe1 for binding to Crip21; - Receptor of virus antigens; - Receptor of animal antigens, AtLecRK-1.1 / 1.8 for binding to insect eggs, AtNILR1 for binding to Nemawater, VuINR for binding to Inceptin; - Receptor of Co-receptors antigens, BAK1 / SERKs, SOBIR1, CERK1. Specific pattern recognition receptors (PRRs) are required for symbiosis or function in pattern- triggered immunity (PTI) and recognize conserved microorganism-associated microbial patterns (MAMPs) such as chitin, flagellin and peptidoglycan. Taken together, these observations suggest that plants have the receptor diversity necessary to distinguish a large number of potential symbionts and pathogens. Multiple receptor inputs contribute to specific and robust responses in both immunity and symbiosis. To decide whether to engage in immunity or symbiosis, a plant must identify the type of microorganism with which it is interacting and determine whether that microorganism is mutualistic or pathogenic. Robust activation of a specific pathway depends on the combination of associated microbial patterns (MAMPs) and one or more lifestyle-associated factors (e.g., damage-associated molecular patterns [DAMPs], effectors, lipochitooligosaccharides [LCOs]). Example 1.2 – Specifically selected receptors Present in most higher plant species and essential for antibacterial immunity, the 'flagellin- sensitive 2' (FLS2) protein is an LRR-RLK receptor that recognizes the bacterial flagellin peptide (flg22). Binding of flg22 almost instantaneously triggers the association of FLS2 with the coreceptor 'BRI1-associated kinase 1' (BAK1). This coreceptor also possesses LRR domains and forms heteromers with other receptors, playing an important role in plant immunity. The most studied receptor is the FLS2 receptor of Arabidopsis thaliana (Q9FL28). FLS2 has 1173 residues, with the following domain structure: - a succession of 28 extracellular LLRs (PF00560, PF08263, PF13855), and. - an intracellular domain of the eukaryotic protein kinase type (PF00069). Additionally, the BAK1 coreceptor (BAK1 - BRASSINOSTEROID INSENSITIVE 1-associated receptor kinase 1 - Arabidopsis thaliana ((Mouse-ear cress) | UniProtKB | UniProt) is a 615 amino acid protein, which possesses 6 LLRs (PF00560, PF08263, PF13855) and a tyrosine and serine / threonine kinase domain (PF07714). In Arabidopsis, the extracellular LRR domains of FLS2 (residues 25 to 800) and BAK1 (residues 1 to 220) were observed to form a heterodimer induced by flg22 binding, this complex was able to crystallize and is available in PDB (4MN8, Figure 1). Example 1.3 – Binding of FLS2 to BAK1 and flg22 Flg22 was observed to bind to the concave surface of FLS2 formed by the LRR3 to LRR16 repeats (Figure 2). The C-terminal ends of BAK1LRR and FLS2LRR are similarly oriented, presumably pointing toward the membrane surface (Figure 2), located in the crystal at a distance of 58.3 Å. However, from the structure it is observed that it would be possible to prune some repeat(s) in the C-terminal section thus modifying the distance between the extremes in the dimer. As seen in Figure 3 and 4, the N-terminal region of the FLS2 receptor establishes interactions with flagellin, whereas the C-terminal residues are involved in binding to the co-receptor BAK1. Adding to these observations, in precipitation assays it was observed that FLS2 with two mutants ARG294 and His316 to Ala (R294A / H316A) resulted in loss of interaction with flg22. This is also observed in Figure 4, performing a mutation at these positions returns an elevated △△G for interaction with flg22. Example 1.4 – Binding of BAK1 to FLS2 and flg22 On the other hand, BAK1 interacts with LRR18 to 26 of FLS2. Mutation of FLS2 residue N674 to tryptophan or alanine disrupted the interaction between FLS2 and BAK1 (Koller and Bent 2014). In the case of the BAK1 coreceptor, phenylalanines 60 and 144 play a key role in this interaction. As seen in Figure 5, the mutations evaluated at these positions generate a stabilization of the interaction with FLS2 (elevated △△G). This has been experimentally verified, as replacing them with alanine (F60A / F144A) negatively affects heterodimerization. It also recognizes the C- terminal region of flg22, residues T52, L53, V54 are involved (Figure 3C). These are also highlighted in the matrix of Figure 5 (right), several of the mutants evaluated would affect the interaction with flagellin. Example 1.5 – Binding of flg22 to FLS2 and BAK1 In the case of flg22, according to the concept of "address-message", flg22 can be divided into two functional domains. The "address" segment consists of the first 17 residues and is the one that interacts with FLS2. interacts with FLS2. The five C-terminal residues make up the message segment and constitute the BAK2 binding site. constitute the BAK1 binding site (Colaianni et al., 2021; Parys et al., 2021). How sequence variability affects their interaction with both receptors has been studied, both by targeted mutagenesis (Parys et al., 2021) and by analyzing variants in nature (Colaianni et al., 2021). nature (Colaianni et al., 2021). The mutants in aspartic acids 14 and 15 (D14 and D15) are the ones that have shown, in these experimental assays, a greater negative impact on the flg22-FLS2 interaction. flg22-FLS2 interaction. This goes hand in hand with the values obtained in the matrix in Figure 6. EXAMPLE 2 – Analysis of the sequence variation of flg22 In the analyzed structure (4MN8), flg22 is a 22 amino acid peptide derived from the N-terminal region of the FliC protein of Pseudomonas aeruginosa (residues 30-52, P21184). It is located within the "flagellin N-terminal" domain of Pfam (PF00669). A multiple sequence alignment (MSA) of the seed sequences of this family shows that these 22 residues are the most conserved in FliC (Figure 7). Overall, it can be observed that FoldX is able to evaluate the change in binding energy between FLS2, BAK1 and flg22. As a first indication that the predictions were adequate, the mutants with the highest impact are located in those residues involved in the interactions observed in the crystal. Furthermore, for FLS2 and BAK1, in those cases where a specific substitution was experimentally found to abrogate flg22 recognition or prevent dimerization, this could be reflected in the generated matrices, as mutants at these key positions result in elevated ΔΔΔG. Although there is a limitation in the experimental data that would allow us to validate all the mutants evaluated, for the cases analyzed where there is experimental evidence, this agrees with the FoldX prediction. As for flagellin, it binds robustly to the FLS2 receptor. Although there are key residues involved in this interaction, as evidenced in the FoldX results and in experimental assays, it has been proposed that similar to what occurs in nature, more than one variant must be present simultaneously to evade recognition. However, for this peptide more information is available than in the case of the receptors, the non-immunogenic sequences and those that affect its interaction with both FLS2 and BAK1 are known. EXAMPLE 3 - STRUCTURAL ANALYSIS OF THE LysM-RK and LysM-RP BINDING METHOD Chitin is a long-chain polymer of N-acetylglucosamine (NAG), chitin oligosaccharides derived from fungal cell walls can be recognized as a PAMP by fungal cell walls. derived from fungal cell walls can be recognized as a PAMP by PRRs, thus inducing PTI. PRRs, thus inducing PTI. In relation to receptors that detect polysaccharide patterns, The most studied LysMs are two types of plasma membrane (glyco)proteins, OsM and OsM plasma membrane (glyco)proteins, OsCEBiP ("Chitin elicitor-binding protein") and OsCERK1 ("Chitin elicitor receptor kinase 1") in the receptor kinase 1") in rice, and AtCERK1 in Arabidopsis. OsCEBiP belongs to the group of LysM-RP receptor-like proteins, whereas OsCEBiP belongs to the LysM-RP receptor-like proteins. receptor LysM-RP, whereas AtCERK1 / OsCERK1 are of the LysM-RK type, with intracellular kinase. The extracellular portion of these molecules present LysM, which interact with NAG chains. This induces transient oligomerization of these receptors. AtCERK1 forms homodimers connected by chitin. Homodimeric association has also been reported for the protein OsCEBiP protein, but it can also form heterodimers with OsCERK1 AtCERK1 has 617 residues (A8R7E6), has 2 Pfam families, "LysM domain" (PF01476) and "Pfam tyrosine and serine / threonine kinase" (PF07714). Its extracellular domain was crystallized (residues 25-230) in its free state and bound to chitin have been deposited in the PDB with accession codes 4EBY and 4EBZ, respectively. The extracellular region of AtCERK1 contains three LysMs in tandem (LysM1-3), only LysM2 was found to bind to (NAG)5. Figures 8 and 9 show in detail the interaction between the receptor residues and the NAG chain. OsCERK1 (A0A0P0XII1) of 624 residues, also presents the PF07714 domain and has been recently crystallized, PDB: 7VS7. On the other hand, OsCEBiP is a smaller receptor, 356 amino acids in size, as it does not present intracellular kinase. It also possesses the PF01476 family. The accession numbers for the structures of OsCEBiP in its apo and chitin-bound state are PDB: 5JCD and 5JCE, respectively. Analysis of the interaction between chitin and the receptor shows that it is mediated by a few key residues, that many of the interactions are solvent-mediated, and that few of the -OH groups that determine the nature of the sugar determine the interaction. Thus, the analysis suggests little ability to engineer the receptor to generate selective receptors for other sugars, which coupled with the low variability of the receptors in the different pathogens suggests that the receptor does not have great potential for platform development. EXAMPLE 4 - STRUCTURAL MECHANISM OF SIGNAL TRANSDUCTION To analyze the possible allosteric mechanism of signal transduction, the structure of the receptors in the presence and absence of the ligand was comparatively analyzed. For FLS2 the structures in both states (free and bound) shown in Figure 11 are extremely similar with an RMSD of 0.43 Å. Similarly, the structures of both states in LysM for both OsCEBiP and AtCERK1 are also very similar, with an RMSD of 0.18 Å (4EBY vs 4EBZ, Figure 12A) and 0.83 Å (5JCE vs 5JCD, Figure 12B). Also performing a LysM2 comparison the structures of OsCERK1 and AtCERK1 gave an RMSD of 1.5Å (51 Ca), indicating that the NAD recognition region is similar in both receptors (Figure 12C). Once the NAG chain is recognized, oligomerization occurs (Figure 13). AtCERK1 forms homodimers, but in the case of OsCEBiP it can also form heterodimers with OSCERK1. Extended analysis of the binding mode structures of both FLS2 and LysM receptors shows that the main effect of ligand binding is oligomerization specifically FLS2 / BAK1 heterodimerization in the former case (Figure 1 and 14) and homodimerization mediated by polyvalent saccharide ligands (Figure 13). It can be observed in the 4MN8 crystal of the FLS2-BAK1-flg22 complex that the C-terminal ends of the extracellular domains of BAK1 and FLS2 are similarly oriented (Figure 2). EXAMPLE 5 – HYDROPHOBIN STRUCTURAL PROPERTIES Hydrophobins are fungal proteins involved in the growth and development of filamentous fungi. Their ability to perform functions is based on their ability to self-assemble at interfaces with hydrophilic-hydrophobic properties. Structurally, hydrophobins constitute a family of low molecular weight proteins characterized by the presence of 8 highly conserved cysteine residues that form a specific pattern. They form 4 disulfide bridges, which stabilize an amphipathic tertiary structure that confers surfactant-like activity. They are divided into two groups, class I and class II, according to their hydrophobicity graphs, solubility characteristics, cysteine patterns and structures formed during their self- assembly. Given their characteristics, several applications have been identified for these proteins ranging from hydrophobic drug encapsulation, protein purification tags, protein and cell immobilization, antimicrobial coatings, biosensors and emulsifying agents. The inventors of the present invention disclose herein a way of taking advantage of the self- assembly capacity of the hydrophobin for an HFB-based capsule formation. To carry out the experimental tests, the hydrophobin HFB7 from Trichoderma harzianum, which belongs to class II, and has a sequence of SEQ ID NO: 36, is used. A BLASTp search of this database yielded the best results for the proteins "Hydrophobin 2" (2B97, coverage 89%, identity 60.29%) and "Hydrophobin 1" (2FZ6, coverage 90%, identity 50.72%) from Trichoderma reesei. All three belong to the same Pfam family "Fungal hydrophobin" (PF06766) and are class II hydrophobins. The alignment of these proteins together with the PF06766 seed shows that some residues are highly conserved, especially the cysteines that make the disulfide bridges responsible for structural stability (Figure 15). In this sense all hydrophobins were assumed to form capsids in the same way and that there would be no particular advantage / disadvantage to work with one or the other. EXAMPLE 6 – HYDROPHOBIN FUNCTIONALIZING Hydrophobins 1 and 2 of T. reesei have been fused to various proteins, such as green fluorescent protein (GFP), Staphylococcus aureus protein A, and maltose-binding protein (MBP). As seen in Figure 17, both the C-terminus and the N-terminus are not part of the hydrophobic region. This has allowed fusions to be performed at both ends, either with or without a linker, without losing the ability to self-assemble. One of their applications is the formation of nanoparticles capable of encapsulating drugs. Such a capsule has been successfully labeled using a GFP-fused hydrophobin (in a 1:3 ratio of GFP-HFBI / HFBII), suggesting that hydrophobin fusions could be used to modify the surface of nanocarriers. Based on this evidence the inventors performed a first proof of concept to analyze what the structure of a hydrophobin chimera with FLS2 / BAK1 receptors would look like. The sequence corresponding to the crystals of FLS2 and BAK1 (4MN8) was used, and these were fused to the N-terminal end of HFB7. The structure obtained with Alphafold is shown in Figure 17. The models show that these do not impede the correct folding of the hydrophobin and that it would therefore not lose its self-assembly capacity. Based on the evidence mentioned in the previous points, in particular the fact a) that no allosteric changes are observed due to flg22 binding on FSL2 and / or BAK1 and b) that flg22 binding will trigger heterodimerization and c) the putative mode of capsule formation by hydrophobin, the following mechanism for the production of modified hydrophobin that responds to and triggers capsule opening as a consequence of flg22 binding is disclosed (Figure 16). The mechanism involves generating 2 hydrophobin constructs, one with BAK1 and one with FLS2, capable of self-assembling on a hydrophobic substrate forming mixed capsules in a 1:1 stoichiometric ratio. Furthermore, these constructs are used to generate a hydrophobin based capsule comprising additional non-fused hydrophobin in a BAK1 fusion polypeptide:FLS2 fusion polypeptide: non-fusion polypeptide ratio of 1:1:3. In the absence of the ligand (flg22) there is no interaction between the co-receptors (BAK1 and FLS2) and therefore the hydrophobins are free to optimally accommodate on the substrate. The binding of flg22 results in heterodimerization, which imposes a structural constraint between adjacent hydrophobin monomers (bound to the co-receptors), resulting in destabilization of the capsid resulting in its opening. It is key for this destabilization and consequent opening to occur that the structural restriction imposed by heterodimer formation results in a position of the hydrophobin dimer incompatible with capsule formation. To this end, it is key to control the distance between the C-terminal ends of the co-receptors in the heterodimer that imposes such a distance to the hydrophobin dimer, and that it is incompatible with the distance necessary to form the capsule optimally. EXAMPLE 7 - NANOCAPSULE OPENING BY INTERACTION OF AN HFB FUSION POLPYPEPTIDE WITH A LIGAND The inventors of the present invention worked with a protein that is present in different fungi species and to test the functionality they have chosen HFB7 from Trichoderma harzianum (denominated from hereon as PDI). During their work, the inventors first isolated the protein directly from a fungal culture and demonstrated its ability to form protein bodies, which they categorized as nanocapsules or biocapsules based on their size and biological nature. Using transmission electron microscopy (TEM) and dynamic light scattering, the inventors detected particles ranging in size from 10 nm to an average of 100 nm. EXAMPLE 8 – NANOCAPSULE FORMATION 0.26 μg / μl of PDI protein was extracted from fungal solid culture through ATPS methodology (Linder et al 2001). Briefly, it consist in the use of detergent (Triton x114) and isobutanol to separate the phases and extract the protein from the rest of the components. Each suspension was deposited on a 400 mesh nickel grid covered with a carbon film. The samples were observed at a voltage of 120 kV in the transmission electron microscope. JEOL JEM2100 Plus equipped with Gatan Orius SC200 camera, using the Digital program Micrography. To characterize more deeply these nanocapsules the inventors conducted dynamic light scattering of the protein alone and a mix between the protein and an extract of metabolites from Trichoderma which was denominated SNA Steps summary: 1) 0.26 μg / μl PDI (70% purity) 2) Sonication (3 pulses of 10 sec 40% amplitude, 30 sec of rest) 3) Facility TEM IFIR The results of this Example are summarized in Figure 18. To characterize more deeply these nanocapsules the inventors conducted dynamic light scattering of the protein alone and a mix between the protein and an extract of metabolites from Trichoderma denominated SNA. EXAMPLE 9 – EVALUATION OF NANODISPERSION Reagents: ^ H2Od ^ PDI obtained by ATPS from a fungal culture 0.2 mg / ml ^ Metabolite cocktail obtained from extraction of a supernatant of culture from Trichoderma (SNA, see the other provisional)) ^ Ultrasonic (sonicator) ^ G25 Sephadex column Steps summary: 1) The protein without any additive and the protein plus a cocktail of metabolites were sonicated to allow the nanocapsule formation. 2) After this procedure active ingredients not encapsulated were filtrated by exclusion chromatography using Sephadex G25 resin 3) DLS using water as blank. o Parameters: Calculation: Narrow o Advance LS o Measurement Manual (129-240) o Number of measurements 10 The results of this Example are summarized in Figure 19. Based on these results, it was concluded that a mix of proteins obtained from the fungus can form protein bodies, and the presence of other metabolites seems to affect the size of the nanocapsules. To deeply characterize the nanocapsules the inventors proceed to the heterologous expression of the protein in E. coli. The protein sequence is cloned to be produced as a fusion protein to thioredoxin in pET-32a from genescript. Then the fusion protein is digested using Thrombin® according to the manufacturer's instruction. The purification protocol allows the inventors to obtain a higher amount of protein with an average of 80% purity, as evidenced in Figure 20. EXAMPLE 10 – EVALUATION OF DIFFERENT STRATEGIES TO OBTAIN NANOCAPSULES Following the same procedure as before, the inventors corroborate the ability to form nanocapsules using the pure protein Reagents: PDI413.9 mg / ml in buffer Tris pH 7,5, Fl- 11.44 mg / ml (dissolved in methanol) (following the ratio descripted in Valo et al 2010). Ratio 1(PDI) 14 (Fl-) 1) A mix was prepared where the final cc of PDI was 0.5 mg / ml and the Fl- was 0.28 mg / ml in a final volume of 20 ml that was completed with water. In addition, a control with Fl- without PDI was also prepared 2) Sonication (4 pulses of 10 sec at 40 % amplitude followed by 30 sec on ice) 3) In this step each sample was divided into 3 treatments: Ultacentrifugation @ 45000 rpm, Mild centrifugation @ 13000 rpm and Sephadex G25 gel filtration 4) Then the pellets and supernatants were evaluated by TEM in Santa Fe The results are summarized in Figure 21. The highest amount of nanocapsules were obtained from the ultracentrifugation procedure. However, mild centrifugation also yields nanocapsule formation. Thus, for routine nanocapsule preparation the inventors follow with mild centrifugation step EXAMPLE 11– TEST OF NANOCAPSULES OPENING BY THE INTERACTION OF THE SENSOR WITH ITS LIGAND The Scheme of interaction between the sensor portion of the HFB polypeptide protein of the invention and the Ni-NTA resin is summarized in Figure 22. Reagents: o Purification protocol ID 4 (Spanish), o thrombin digestion protocol ID5 (Spanish) o PDI13 (5mg / ml), PDI-Trex14 (5mg / ml), o buffer TrisHCl pH 5.5, H2Od, o fluorescein (50 mM in methanol), o Ni-NTA agarose resin. PDI-Trx ^ Cytosolic Trx (thioredoxin) from E. coli is a common tag protein used for fusion protein expression in E. coli due to its high solubility and expression efficiency ^ Trx has 109 amino acid residues, with 11.8 kDa, i.e. Trx is similar in size to PDI (78 aa) ^ Linker: 50 aas ^ N-terminal His Tag Steps summary: 1) Assembly of nanocapsules with PDI-Trxhis (HFB fusion polypeptide), PDI and fluorescein. Molar ratios: o Ratio I: PDITrex : PD I :Fl 0.05:1:14 o PDI : Fl ratio 1:14 o Fl: 14 2) For each tube, sonication (3x 10”; amplitude 40%) +centrifugation Sorvall 20' 18,000 rpm (44192 x g). Pellet (nanocapsules) + 200 uL Tris buffer pH 5.5. 3) Once the nanocapsules are formed and isolated (pellet, 200 ul) we first validated the nanocapsule formation (Fig.27) and then evaluated the interaction with the Ni-NTA resin according to the following protocol: a) Mix 100 μL resin Ni-NTA + 180 μL buffer pH5.5 + 20 μL of i) PDITrex : PDI : FI – Ratio I ii) PDITrex : PDI : FI – Ratio II iii) PDITrex : PDI : FI – Ratio III iv) PDI : FI v) FI b) Let it interact for 1 hour, room temperature, 180 rpm c) Centrifuge 3’, 3000 rpm ^ supernatant 1: fluoresceine should be released in samples 1, 2, and the sensor interacts with the resin, intact nanocapsules in 4, in 5. d) Add 200 μL buffer Tris pH 7.5, NaCl 300 mM, 500 mM imidazole. e) Let it interact for 1 hour, room temperature, 180 rpm f) Centrifuge 3’, 3000 rpm ^ supernatant 2: Everything should be peel off from the resin, in all samples 4) Determination of the melting temperature (Tm) values was performed using a Q-PCR thermal cycler (Applied Biosystems StepOne™). The assays were performed in 20 μL in a MicroAmp™ Fast Optical 48-Well Reaction Plate (Applied Biosystems). All the assays were performed in duplicated and protein samples were centrifuged (10 min, 10000 rpm, 4°C) before being aliquot to the plate. Then the plates were sealed using MicroAmp™ 48- Well Optical Adhesive Film (Applied Biosystems) and heated from 25°C to 95°C in the Q- PCR thermal cycler with a ramp speed of 0.5°C per min. The nanocapsule opening induced by the increasing of the temperature was monitored by the increase in fluorescence of fluorescein. Fluorescence intensities were plotted against temperature for each sample well (Fig 28) EXAMPLE 12 – DETERMINATION OF NANOCAPSULE FORMATION IN THE PDI : SENSOR MIX Reagents: ^ PDI51,57 mM in buffer Tris pH 7,5, ^ NaCl 300 mM PDI-Trex 60 uM, ^ Fl- 50 mM (dissolved in methanol), ^ H2Od Steps summary: 1) Assembly of nanocapsules using PDI, PDI-Trex (sensor-like protein), fluorescein or ssDNA according to the following scheme. Molar ratios: PDI:Fl ratio 1:14 (sonication and 45 rpm ultracentrifuge) PDITrex:PDI:Fl ratio 1:10:14 (shaking and 15000 rpm centrifugation) PDITrex:PDI ratio 1:10 (shaking and 15000 rpm centrifugation) 2) Vortex by 1 hour or sonication 3) Centrifugation in Sorvall at 15000 rpm / ultracentrifugation 45000 rpm 4) Separate the SN (free nucleic acids) and pellet (nanocapsules) 5) Resuspend the pellet in 200 uL of H2O 4 Facility TEM IFIR: Each suspension was deposited on a 400 mesh nickel grid covered with a carbon film. The excess solution was then removed and the sample was allowed to air dry at room temperature. The samples were observed at a voltage of 120 kV in the transmission electron microscope. JEOL JEM2100 Plus equipped with Gatan Orius SC200 camera, using the Digital program Micrography. Results are summarized in Figure 24. The conditions nanocapsules in which the nanocapsules form were observed. Nanoencapsulation of Fluorescein with PDI alone and using ultracentifugation seem to generate smaller and more abundant nanocapsules. Using alternative procedures and active ingredients, bigger nanocapsules were observed. It is noteworthy to mention that with the procedure above described and the ratio PDI : Sensor 10: 1 nanocapsules of about 10-50 nm containing fluorescein are formed. EXAMPLE 13 – TEMPERATURE STABILITY OF NANOCAPSULES Once the nanocapsules were formed, and prior to the interaction assay, the nanocapsule stability at different temperatures was evaluated by monitoring fluorescence intensity in qPCR thermal cycler. Figure 25 shows the fluorescence intensities of various treatments as temperature increases. A rise in fluorescence intensity is observed in nanocapsules, both with and without the sensor component. In contrast, this behavior is not seen in the sample containing only the fluorophore. Then the nanocapsules and the control tube with fluorescein were incubated with the Ni:NTA resin according to the following protocol: a) Mix 100 μL resin Ni-NTA + 180 μL buffer pH5.5 + 20 μL oF i) PDITrex : PDI : FI – Ratio I ii) PDITrex : PDI : FI – Ratio II iii) PDITrex : PDI : FI – Ratio III iv) PDI : FI v) FI b) Let it interact for 1 hour, room temperature, 180 rpm c) Centrifuge 3’, 3000 rpm ^ supernatant 1: fluoresceine should be released in samples 1, 2, and 3; wherein the sensor interacts with the resin, intact nanocapsules in 4, in 5. d) Add 200 μL buffer Tris pH 7.5, NaCl 300 mM, 500 mM imidazole. e) Let it interact for 1 hour, room temperature, 180 rpm f) Centrifuge 3’, 3000 rpm ^ supernatant 2: Everything should be peel off from the resin, in all samples After incubating the samples in batch with the resin and centrifuging, the flowthrough was evaluated as a function of temperature. The resulting behavior is depicted in Figure 26. After interaction with the resin, the presence of nanocapsules is only evident in the sample with PDI:Fl suggesting the absence of interaction with the resin and the delivery of fluorescein only by temperature increase. In the SN1 samples from the nanocapsules having HFB fusion polypeptide, an invariant response with temperature is seen (Fig 28A), suggesting the previous breaking of the nanocapsules and delivery of fluorescein. The fluorescence for the SN1 samples from the nanocapsules comprising the HFB fusion polypeptide is lower, but this may be due to the fluorescein being retained in the resin. The absence of increase of fluorescence after the elution with imidazole in SN2 means the absence of nanocapsules bound to resin As can be seen in Figure 26A, the nanocapsules having the HFB fusion polypeptide interact with the resin, creating a movement or mechanical stress in the capsule that ends in its rupture and delivery of fluorescein. However, the nanocapsules with PDI:Fl, which have no protein capable of interacting with the resin, do not break and the fluorescein delivery is only observed when temperature is applied. EXAMPLE 14 – ADDITIONAL EVIDENCE OF NANOCAPSULE OPENING STRATEGY ^ Cytosolic MBP (maltose binding protein) from E. coli is a common tag protein used for fusion protein expression in E. coli due to its high solubility and expression efficiency ^ MBP has 449 amino acid residues, with 48.4 kDa, i.e.. MBP is 5.75 times larger than PDI (78 aa) ^ Short Linker SSS (at the C-terminus of MBP) Reagents: ^ PDI13 (5mg / ml), ^ MBP-PDI (2.5mg / ml), ^ buffer (Tris HCl pH 7.5), ^ fluorescein (50 mM in methanol), ^ maltose resin, ^ H2Od. Molar ratio: MBP-PDI : PDI : Fl ratio 0.36:1:14 PDI : Fl ratio 1:14 Fl 14 1) For each tube, sonication (3x 10”; amplitude 40%) +centrifugation Sorvall 20' 18,000 rpm (44192 x g). Pellet (nanocapsules) + 200 uL BUFFER 2) Once the nanocapsules are formed and isolated (pellet, 200 ul) the inventors first validate the nanocapsule formation in each condition and then after the interaction with the Maltose resin after 30 min incubation. 3) Determination of the melting temperature (Tm) values was performed using a Q-PCR thermal cycler (Appied Biosystems StepOne™). The assays were performed in 20 μL in a MicroAmp™ Fast Optical 48-Well Reaction Plate (Applied Biosystems). EJEMPLO 15 – ANALYZING WITH APPLIED BIOSYSTEMS THE SAMPLES OF NANOCAPSULES + RESIN MALTOSE After interaction with the resin, the inventors evidence the presence of nanocapsules in the samples with PDI : Fl (with and without maltose resin), evidenced by their response to temperature. It is worth mentioning that these nanocapsules were assembled 15 days before the experiment, and this time might influence their stability. However, for the sample with HFB fusion polypeptide, it can be seen that after the interaction with the maltose resin, they do not respond to temperature increase, suggesting the breaking of the capsules. Those capsules with MBP-PDI : PDI : Fl without resin show a clear response against the temperature, opening totally at 60 °C. The control (Fl only) remains constant with temperature. In conclusion, the capsule open in response to the interaction of the sensor with maltose. The results of this Example are summarized in Figures 30 and 31. REFERENCES Reuter LJ, Shahbazi MA, Mäkilä EM, Salonen JJ, Saberianfar R, Menassa R, Santos HA, Joensuu JJ, Ritala A. Coating Nanoparticles with Plant-Produced Transferrin-Hydrophobin Fusion Protein Enhances Their Uptake in Cancer Cells. Bioconjug Chem.2017 Jun 21;28(6):1639-1648. doi: 10.1021 / acs.bioconjchem.7b00075. Epub 2017 Jun 12. PMID: 28557453. Xiao Y, Zhang Q, Wang Y, Wang B, Sun F, Han Z, Feng Y, Yang H, Meng S, Wang Z. Dual- functional protein for one-step production of a soluble and targeted fluorescent dye. Theranostics. 2018 Apr 30;8(11):3111-3125. doi: 10.7150 / thno.24613. PMID: 29896306; PMCID: PMC5996361. Maiolo D, Pigliacelli C, Sánchez Moreno P, Violatto MB, Talamini L, Tirotta I, Piccirillo R, Zucchetti M, Morosi L, Frapolli R, Candiani G, Bigini P, Metrangolo P, Baldelli Bombelli F. Bioreducible Hydrophobin-Stabilized Supraparticles for Selective Intracellular Release. ACS Nano.2017 Sep 26;11(9):9413-9423. doi: 10.1021 / acsnano.7b04979. Epub 2017 Aug 17. PMID: 28806871; PMCID: PMC5618140. LIST OF SEQUENCES SEQ ID NO Description Sequence Hydrophobin MKFTFAIAAAIFTGLVSALPAKEVESRQVPYIPCSGIYGSAQCCATDVLGLVNLDCGQPPETP 1 B2AV25 TDADTFSAICSAIGQRARCCALPVLDQGVLCNTPAGVQP Hydrophobin MQFSVVLVALFTSATMAAPTTETETSVYIPCSGLYSSVQCCATSVLDLADLTCRPPPKVPTSA 2 E3QVP2 ANFGKICADIGQRARCCVLPALGLGVLCQTPAGVTY MRYTILAFAAGAAAAPFVTTGTSLCPAGLYSNPQCCATDVLGAIGLDCAVPATTPADVDAFIS Hydrophobin GCAAVGQQAKCCVIPIAGQDLLCQDVKGSGGGGGGSGGAPGITATGGGGGGGTPTSVPG 3 E3RPZ7 GGGGGGATSTSCESSAVVTPPPQPTKPAPSYPTTTSDCGCGK Hydrophobin MQFTIATVLSLLTVALAAPAAVVERQVPYTACTGLYGTAQCCATDILGLADLDCANPPATLTS 4 F7VY75 AVQFQATCSDIGQRARCCLLPILGQALVCETPAGLPTA MKSKSIMAASTVMELALAQASAEPLCSTIINLQPIEYQFQQPVLIDSYFPANTDIVLDDGHVVH VTNAPTSLSTVLTDVSTSSTTLTSSASNVNGNPPDGGYLTFTVPANPDDIGNHPVTKTYPPTE PGQPGIVVIQVPTSPPGADGIPTSSVPYVTVTTTGDFPSLTGPVTTTITPDEPGATGSVIIEVPN TKIASPSASYVTVTTPGSLAPTDAPHTSTIPPSNPTDPGTVIVVVPSSQASSVSSIPFVTVTTTG STLNPTDDPITSTISPSGSTGSGTVIVEVPPSSFPSGSGASSSPVSFVTRTVTGDDGNGEPST Hydrophobin TTITPTASSGPGTVIVEVPPPTNSPSATSSGSSMPGGPGSSGTGSSASQGPSDSAAPSSSTG 5 F9FRS1 DTGPSSVPESSSPSRATTDDAASSTSASAPASSSAASSTTQSETPSSAGAETSTPATSPASS SAPSTSDADTSSPVNPTTSSPASSAATSAPGSSTESAPSSSTSAAAANFDPCPDSLYGNPQ CCSVDVLGVADVECDSPTESPTDAENFQAICAASGQRARCCVLPVLGQALVCLTPVGVSN Hydrophobin MQIHIFATFFFASMAVAMPADSLSRRADFYLPCGTGLSATAECCSANLDGLLELNCAAVPKTP F9XJS4 TSGEHFVAICAAQGQEARCCLTVVLGQGVKCQTPPGA Hydrophobin MQFSTITAVFFASLAVASPTYGGKYEPCGSALYSQAQCCATDVLEVAGLDCDGVGARIDNAQ F9XJU2 HFVNLCAAKGQRARCCAIPVLGQALLCQEPEGTN MQFIILALAALAAAAPGGAPSYGGSGSGMAGGMAGGHGGSGGYSGGSNNGGSNGGSNGG Hydrophobin SSNGGSNGGSNGGKFQCSAPLQSSPQCCAVNALGVASLPCNAPTRDIESREDFVKYCGQS F9XMQ8 GATAQCCVLPALGAGVACEEVKSN Hydrophobin MKSFATVALFIAGILAAPQPNMKLPRSPVCSGLTSTPQCCATDVLGVADLDCQTPSSPVPDA G0RBZ9 QTFEAVCAAGGQRARCCAIPVAGQDLLCQTPAGI MKLLAVTALLVAGSLAVPAGSYPPPPPTYGDDPSGEVGHPPEYPPDYSSQYPEYPPGHGGK DDGDEDSYTPPSTTLSPSYPTSVGGDKSSYPPPSSTPYPPPEADGDGGNNNSGNNSGDNN GDDNDDNNGDDDDDNNGDDDDDDNDNGDDDDDNVPGAPEQPPTDGDSDSPDNGTGGD Hydrophobin GTVGGGDDGDGEDNASDLCPGILYASPQCCDTSVLGLLDLSCEPPRSAPADVEAFNDICQE G0RFI5 VGAKAQCCVLPVALLCEDVPN Hydrophobin MQFFTVTTALFASLALAAPVVEDRQVYIPCSGLYGSPQCCATDVLGVANLDCGEPPAVPTNA G2XCF6 SEFQATCATIGQRARCCVLPILDQGVLCNNPAGVDE MKFTTVAVAFFVGLAAALPTTDSYTPAPYGGNGGHNGGHNGGNNGGHNGGHNGGNNGGN NGGNGGNNGGNGGNGNNGGNNGGNNGGNNGGNNGGNNGGNGGNNGGNGGNNGGNG GNGNNGGNGNNGGNGGNNGGNNGGNNGGNGGNNGGNGGNNGGNNGGNGGNNGGNN Hydrophobin GGNNGGNGGNNDYAPCPSGLSMTPVCCATNVLGLLALNCDAPSKTPTSAKDFQKICADAGT G2XCG9 AAKCCTLNLLNQGVLCQVPVGVAA Hydrophobin MQFSTIIATIFVAATGAVALPAEVQERQVPYTPCSGLYGSAQCCATDILGLANLDCGQPSDAP G4MWK2 VDADNFSEICAAIGQRARCCVLPILDQGILCNTPAGVTP Hydrophobin MQIKTLIVALFAGIAMAMPTDPPKNGGGGGSTPPTTPPTTPPGGGSGDYDACEGNGLLYSSA G4N8U1 QCCATDVLGVADLDCAVPPSLPTSASGFTDICAALGQRARCCVLPLAGQAVLCQAPVGA MKLLAITALFIAGTLAVPASSYPPPPPEYGDGHKGDVGYGGDHGGDHGKDHGKDHGGHYP GDPNYPPPPPPGYHNGGSDKPPTDGDGYPSDGGDDGDDSDGGGHGGDRENDPSDLCPT Hydrophobin LLYSNPQCCSASVLNIADLDCEPPRKRPSRKHDFKQICAAQGSDAKCCVLPLLGLGILCTDAI G9MS02 V Hydrophobin MKSFAAAVLFIAGILAAPSPNAKAIRSPLCPGGLESNPQCCSTDVLGIADLDCANPSSPVTDV G9N5V3 QSFRAVCAAGGQRARCCAIPVAGQALLCESPVGI Hydrophobin MQFFAVATLFVVGVLAAPSPSGLNSRDTLCAAGLYSTPQCCAVDVLGVADLNCAGLVGTVTT G9NHP9 AAEFKANCAAIGQEARCCVLPVLGQDVLCQTPPGL MKHLLVTALLAAGALAMPAGSSCASPSTDYPPPSTDYPPPSTDYPPPSTDYTPPSYPTPTPT PTYTPPPPKNGGGKYPPPPPPPSSPPYSTAPHNGGGGGNGGNGGNGGNGGNNGGGNSG Hydrophobin NGGGNNGNGGNNGGGNNGGGNNGQYECSGGGGLYSNLQCCSVDVLGIADLDCKPPSKT G9P209 PVSGSDFKSICQASGAKPKCCVLPILGQGLLCEDAIGTA Hydrophobin RALFVASAMASPMGSEGCPGGLTNTVPLCCATNVLGVATLDCSTPTVPVPNVGIFQAHCAS HFB7 KGKQPVCCTVPVAGLGLLCQKPTGAQ Hydrophobin MKFSLAAVALLGAVVSALPANEKRQAYIPCSGLYGTSQCCATDVLGVADLDCGNPPSSPTDA I1RDW3 DNFSAVCAEIGQRARCCVLPILDQGILCNTPTGVQD Hydrophobin MQFKTIIIALFAGAAVAVPTGGGSGGGGSGGGGSGGGGSGGGGSGGGAYDACSGLYDSLQ J3NM79 CCATDVLGLANLDCSPPTKAPTSAADFKATCAKGGQRARCCVLPILGQAVLCQSPLGVTY Hydrophobin MQFNAVFATLFATAAAVALPAAELLQRQVPYTPCSGLQSTALCCATDVLGVVNLDCGTPLST J3NP79 PSNGTEFSAICAEIGQRARCCAIPILEQGILCTAPSGVQG Hydrophobin MQFTTALIAIFASVAVAAPTGDGHNGGGSTPAPYDPCSGLYDSAQCCATDVLGVADLDCASP L2G1J6 TSVPSSANDFRKICAVGGQRARCCVLPVLGQAVLCQTPVGV MRYTILAFAIGATAAPLTGYPSAVCPPGLYSTPQCCATDILGAAALNCKAPATTPTSTNQLISG Hydrophobin CAATGQQAKCCVIPVAGQALLCQDVSPGANGGNNAGANGSNNGGANGSNNGGANGGNN M2RZC8 GWC MRYTILAFAIGAIAAPLTDYPTALCPAGLYSNAQCCATDILGVAALNCQNPTTTPTSTGDFISG Hydrophobin CAAVGQQAQCCVIPVAGQALLCQDVSPSGNGGINGDANGGNTGSANGGANGGNNGSADD M2URC1 GGANGATGGGAQAVQTPTSSPASQATPCPSDAPN Hydrophobin MQFSITTILAFAATAAFAAPLEERQVGLCSSGNPVCCATDVLDLADLDCAAPSITPTSTDEFIN M2UUF3 TCASAGQQAKCCLIPILGQALICSDVNPTAPAPSAA Hydrophobin MQFTVLIATLFAAAAVASPVEVVDLEARTKTPPAYDACPDGLYSNPQCCATDVLGVADLDCG M7SEM8 NVKKTPTNAKDFQAVCAKGGQRARCCVLPILGQGVLCETPVGVVY Hydrophobin MQFTTVAAIFFAGLAAAVPTAEVHERGDYTACTGLYGTSQCCATDVLGVADLDCANPPEVPI M7TCM1 SADNFSEVCSAIGQRARCCVLPILGQDVLCQTPVGVDS MRTFILASLALGASLVAAMPQDGLQADSNQVDRRWNDEIYRGSDYRGTGYRGWRGNDNR GNRYNTNGYHGYDNCGDDEDCQRNGPSPQGYGEDDYNDNYNDAKLRRRTWDNNYDGDR Hydrophobin PQQYGNSRYGDNGYSGDGYSRNGYNGDCEDGNCDSRDGDYGGNFRCPGLAAVPQCCEL N1PH52 NAAGVVSATCKNPSRTPDSKGEFQEDCAQSGKSAQCCVLPLGIGISVACNNV Hydrophobin MKFFAIAALFAAAAVAQPLEDRSNGNGNVCPPGLFSNPQCCATQVLGLIGLDCKVPSQNVYD P52754 GTDFRNVCAKTGAQPLCCVAPVAGQALLCQTAVGA Hydrophobin MQFFAVALFATSALAAVCPTGLFSNPLCCATNVLDLIGVDCKTPTIAVDTGAIFQAHCASKGS P79073 KPLCCVAPVADQALLCQKAIGTF Hydrophobin MLYTTILAFAVAAFAAPLEDKRQVGLCASGSPVCCATDVLNLANLDCAPPTTTPADVNTFIDV Q0UYP2 CATGGQQAKCCLIPILGQALLCSDVNPTAAAPATPSA Hydrophobin MQFTITAVLAFAATAAFAAPLEGRQAGICSSGTPLCCATDVLNVADLNCYNPATTPANVDELI R0K9D8 TGCADAGQQAKCCLIPILGQALICNDVSPSAGGASTS Hydrophobin VAFASGAFAAPLLSGYGGDSTVCPSGLYSTPQCCATDILGVAALNCYAPYTAPTDVNDFKAG R0KBF4 CATSGQQAKCCVLPIAGQDILCQDVSPSA Hydrophobin MQFYTIVSLFLAGTAFAAPATSSNGYEACPSGGLFGNPQCCSLNLVGVLSGDCRAPTKTPNS S0E6W4 AKEFQEICAESGQKARCCGLSEILELGAFCQKPVGVAA Hydrophobin of T. PMGSEGCPGGLTNTVPLCCATNVLGVATLDCSTPTVPVPNVGIFQAHCASKGKQPVCCTVP harzianum VAGLGLLCQKPTGAQ MKTSFISSLAMQNSMRSTILKAQLEMTNLNTELTTGKHADLGLTLGANTARSLDLNRDIDRISS LVSVNSIATQRLKSSQTALDGMAKAAQEIQKVLVPNTSSEAPTLTTVSQTISNAFNNFTSFANT AVNGEFLFSGINTDVKPVDDYFADGSPLKAAYETELNAFMAAQTPPVGDFASLSKTQVEGFM THIEGVFKGTTTVTNPPHTSLTAGQNYDFWTTFGSKASNTNMTSRISQNEIVETSSNSNSQG Flagellin MRYFALTAMTSMTFLDPKVDSGIREMVAMKSVTNIGTAINGLNQQQSQLGLSESRVSKANDS A9CK66 LEAQKKIIETHLLDIEGIDTYEAKTRLDLLQQQIEIAYSLTSRLQKMSLVNYL MAFQVNTNINALTTHTSAVATQLGLKNSLEKLSSGLRINKAADDASGMTISDSLRSQASALGQ AISNANDGIGIIQVADKAMDEQLKILDTIKVKATQAAQDGQSLESRKAIQSDIIRLIQGLDNIGNT TSYNGQSLLSGQWTNKEFQIGAYSNQSIKVSVGSTTSDKIGQVRINTGAMITAASEATLTFKQI NGGENITLEGVKISHSVGTGLGVLAEVINKNSDKTGIRAKASVETTSDKEIMSGNLKNLTINDV NIGNIVDIKKGDADGRLVQAINALTSSTGVEASTDSKGRLNLRSVDGRGIVLKADASKDDGDG KSAPMAIDAVNGGQSITDGEGAANYGRLSLARLDARDIILTSSDKPDENKFSAIGFGDNNVAM ATVNLRDVLGKFDASVKSAAGANYNAVVASGNSNLGAGVTTLVGAMLVMDIAESAQKTLDKI Flagellin RSDLGSVQGQMVSTVNNISVTQVNVKAAESRIREVDFAAESAEFNKYNILAQSGSYAMSQAN D3UH73 AVQQNILRLLS MSFRINTNIAALNAHSIGVQTNRNIAGSLEKLSSGLRINKAADDASGMAIADSLRSQSESLGQA VRNANDAIGMIQIADKAMDEQLKILDTIKAKAIQAAQDGQSQESRRSLQSDIRRLMEELDNIAN TTSFNGQQMLSGAFTNKEFQIGAYSNTTVKASIGPTSSDKIGHIRMETASFSGVGMLASAGG NNLTEVALNFKATDGVNSFELENVRISTSAGTGIGALSEVINRFSDKLGIRATYNVMATGTSPV MSGTVRGLVINGVRIGTVNEVRKNDSDGRLINAINSVKNQTGVEASLDITGRINLVSLDGRAIS VHADGEASHVFGEGNFTGISGNNHAIVGRLTLIRTDARDIIVSGVNFSHIGLHSAQGVAETTAN LRQLRGMFGADIASAAGANANKAQADINRQGIGAGVTSLKGAMIVMDMVDSARTQLDKVRS Flagellin DMGSVQIQLVSTINNISTTQVNVKAAESQIRDVDFAAESANFSKNNILAQSGSFALAQANAVQ D3UHK0 QNVLRLLQ MALTVNTNVASLNTQRNLNSSSNSLQTSLQRLSTGSRINSAKDDAAGLQIANRLTSQVNGLG VAVKNANDGISLAQTAEGALQQSTNILQRMRDLSLQSANGSNSDSERDALNSEVGQLKKEL DRISNTTTFGGRKLLDGSFGTASFQVGSAANELISVGIDKMSADSLTGSYYKTAATLGSEVDP DTFAAGKATATITLDDDSTVTVDFDIKKGDDADAIDAKIAAAVNDANVGVSVQKDSAGAWQM VTKTNKDGDAPAVKSFEVAAAATGGVAGVTFPDAVEVDADADLVTANTVKDIDISDAVGAQA Flagellin AVLVIDDAIKQIDSQRADLGAVQNRFDNTIANLQNISENVSAAKGRIQDTDFAAETANLTKNQIL F6A8I8 QQAGTAILSQANQLPQAVLSLLQ MRINHNIAALNTLNRLSSNNSASQKNMEKLSSGLRINRAGDDAAGLAISEKMRGQIRGLEMA Flagellin SKNSQDGISLIQTAEGALTETHAILQRVRELVVQAGNTGTQDKATDLQSIQDEISALTDEIDGIS NRTEFNGKKLLDGTYKVDTATPANQKNLVFQIGANATQQISVNIEDMGADALGIKEADGSIAA FLA_BACSU LHSVNDLDVTKFADNAADTADIGFDAQLKVVDEAINQVSSQRAKLGAVQNRLEHTINNLSAS P02968 GENLTAAESRIRDVDMAKEMSEFTKNNILSQASQAMLAQANQQPQNVLQLLR MIINHNLPAMNAHRNMGINLNQGQKAMEKLSSGLRINRAGDDAAGLAISEKMRAQIRGLDQA Flagellin SRNSQDGISLIQTAEGALDEVHSILQRMRELAVQSSNETNVEQDQAALNDEFQQLVEEIERIK DTTQFNTQKLLDDTVDTVQLQVGANSGELIELDLTKVDLSAIHTALAAEDITDHTNAQSAIDAID FLA_HALH5 EQLKAVSEGRSYLGAMQNRLEHTIKNLDNASENLQAAESRIRDVDMAKEMMEFTRTNILNQA Q05203 SQAMLAQANQQPQAVLQLLR MIINHNTSAINASRNNGINAANLSKTQEKLSSGYRINRASDDAAGMGVSGKINAQIRGLSQAS RNTSKAINFIQTTEGNLNEVEKVLVRMKELAVQSGNGTYSDADRGSIQIEIEQLTDEINRIADQ Flagellin AQYNQMHMLSNKSASQNVRTAEELGMQPAKINTPASLSGSQASWTLRVHVGANQDEAIAV NIYAANVANLFSGEGAQTAQAAPVQEGVQQEGAQQPAPATAPSQGGVNSPVNVTTTVDAN FLA1_BORB TSLAKIENAIRMISDQRANLGAFQNRLESIKDSTEYAIENLKASYAQIKDATMTDEVVAATTNSI U P11089 LTQSAMAMIAQANQVPQYVLSLLR MGFRINTNVAALNAKANADLNSKSLDASLSRLSSGLRINSAADDASGMAIADSLRSQANTLG QAISNGNDALGILQTADKAMDEQLKILDTIKTKATQAAQDGQSLKTRTMLQADINRLMEELDNI ANTTSFNGKQLLSGNFINQEFQIGASSNQTVKATIGATQSSKIGLTRFETGGRISTSGEVQFTL KNYNGIDDFQFQKVVISTSVGTGLGALADEINKNADKTGVRATFTVETRGIAAVRAGATSDTF Flagellin AINGVKIGKVDYKDGDANGALVAAINSVKDTTGVEASIDANGQLLLTSREGRGIKIDGNIGGGA FINADMKENYGRLSLVKNDGKDILISGSNLSSAGFGATQFISQASVSLRESKGQIDANIADAM FLA1_CAMJE GFGSANKGVVLGGYSSVSAYMSSAGSGFSSGSGYSVGSGKNYSTGFANAIAISAASQLSTV P56963 YNVSAGSGFSSGSTLSQFATMKTTAFGVKDETAGVTTLKGAMAVMDIAETAITNLDQIRADIG SVQNQVTSTINNITVTQVNVKAAESQIRDVDFAAESANYSKANILAQSGSYAMAQANSVQQN VLRLLQ MATRINYNYEAAVTYTSLKQNERLMNKSLLRLSTGLRILSAADDASGLFIADQLALVSAGLEQ GNRNIQFGISALQIAEGGVSQIYDKLKTMYQKAVSAANDINDPNARAALQRDIENLRDAILKIA QDTEYNGIRLLNGSFNNVRIHYGARSAQTLSVSISSVLPQQLGGYVAEDSPATATDTNNVLTN IGTTNTNYSVASGDSLAFTFTDGTSITFNSLNQLGYDFNNTGTYILDASAIVNTINNNPTLQGK GIRAYAENVSEADLTFDTTNVNIDQGDEVTITFYSGGELVFTKTYTDTVTLDQFIADINNQAGG Flagellin KLIASKDPSGTKLVLSTPNGETISVEVTVNDADGDTVVSSINLGALLQGAAGTVVNTSGATAS AVKVGTLIVMGSENFTVQGTGIAYFTAATSGTFNSLNDVDVTTNKGAEIAQVLIQRAVRQVDTI FLAA_AQUA RTQIGSTINNLQAIYDAQAVAKDNTDNAESIIRNVDFAKEMTEFTKYQIRMQSGVAMLAQANA E O67803 LPQLVLQLLR MKVNTNIISLKTQEYLRKNNEGMTQAQERLASGKRINSSLDDAAGLAVVTRMNVKSTGLDAA Flagellin SKNSSMGIDLLQTADSALSSMSSILQRMRQLAVQSSNGSFSDEDRKQYTAEFGSLIKELDHV ADTTNYNNIKLLDQTATGAATQVSIQASDKANDLINIDLFNAKGLSAGTITLGSGSTVAGYSAL FLAA_LISMO SVADADSSQQATEAIDELINNISNGRALLGAGMSRLSYNVSNVNNQSIATKASASSIEDADMA Q02551 AEMSEMTKYKILTQTSISMLSQANQTPQMLTQLINS MTSILTNNSAMAALSTLRSISSSMEDTQSRISSGLRVGSASDNAAYWSIATTMRSDNQALSAV QDALGLGAAKVDTAYSGMESAIEVVKEIKAKLVAATEDGVDKAKIQEEITQLKDQLTSIAEAAS FSGENWLQADLSGGPVTKSVVGGFVRDSSGAVSVKKVDYSLNTDTVLFDTTGNTGILDKVY Flagellin NVSQASVTLPVNVNGTTSEYTVGAYNVDDLIDASATFDGDYANVGAGALAGDYVKVQGSWV KAVDVAATGQEVVYDDGTTKWGVDTTVTGAPATNVAAPASIATIDITIAAQAGNLDALIAGVD FLAA_RHIME EALTDMTSAAASLGSISSRIDLQSDFVNKLSDSIDSGVGRLVDADMNEESTRLKALQTQQQLA Q03841 IQALSIANSDSQNVLSLFR MALSMHTNYASLVTQNTLNSTSGLLNTAMERLSTGFRVNSASDDAAGLQIANRLEAQTRGM Flagellin SVAMRNAQDGISMMQTAEGAMEEMTNITYRMNDLATQSLNGSNSDKDRAAMDAEFKQLSA ELNNIMGNTSFGGQKLLAAGGGFEAGAVTFQIGASSAETLDVDASASIKKVAATLADAAITDGI FLAL_VIBPA GDATKAKAALDKISDAGGLIEDIGATRAQFGANINRLEHTMTNLGNMVENTSAAKGRIMDADF Q03473 AVESSNMTKNQMLMQAGTTVLSKTNQLPSMAMSLLR MRFSTQMMYQQNMRGITNSQAEWMKYGEQMSTGKRVVNPSDDPIAASQAVVLSQAQAQN SQYTLARTFATQKVSLEESVLSQVTTAIQNAQEKIVYASNGTLSDDDRASLATDIQGLRDQLL Flagellin NLANTTDGNGRYIFAGYKTETAPFSEEKGKYVGGAESIKQQVDASRSMVIGHTGDKIFDSITS NAVAEPDGSASETNLFAMLDSAIAALKTPVADSEADKETAAAALDKTNRGLKNSLNNVLTVR FLGL_ECOLI AELGTQLNELESLDSLGSDRALGQTQQMSDLVDVDWNATISSYIMQQTALQASYKAFTDMQ P29744 GLSLFQLSK MAQVINTNSLSLITQNNINKNQSALSSSIERLSSGLRINSAKDDAAGQAIANRFTSNIKGLTQAA RNANDGISVAQTTEGALSEINNNLQRVRELTVQATTGTNSESDLSSIQDEIKSRLDEIDRVSG QTQFNGVNVLAKNGSMKIQVGANDNQTITIDLKQIDAKTLGLDGFSVKNNDTVTTSAPVTAFG ATTTNNIKLTGITLSTEAATDTGGTNPASIEGVYTDNGNDYYAKITGGDNDGKYYAVTVANDG Flagellin TVTMATGATANATVTDANTTKATTITSGGTPVQIDNTAGSATANLGAVSLVKLQDSKGNDTD TYALKDTNGNLYAADVNETTGAVSVKTITYTDSSGAASSPTAVKLGGDDGKTEVVDIDGKTY FLIC_ECOLI DSADLNGGNLQTGLTAGGEALTAVANGKTTDPLKALDDAIASVDKFRSSLGAVQNRLDSAVT P04949 NLNNTTTNLSEAQSRIQDADYATEVSNMSKAQIIQQAGNSVLAKANQVPQQVLSLLQG MALSVNTNQPALIALQNLNRTNDDMQAVQTRINTGEAISTAKDTAAVWSHRPGAGDMSGLA Flagellin REDEPGSGDIDRGRGPRAGESVSDLLKLMREKVVAAKDTSLTTTSRQALNADFQGLIKNLNQ VLRSATFDGANLLDGSQAADMSFLADADAGQAITLTLQNLSLGGTINTLTATDDILDPVNAAG FLJJ_CAUVC VLTRLDATLSAVNQAVGNIGTQAKQIDAHNTFVAKLNDVLETGVGNLVDADLAKESARLQAL P02969 QVKQPLGAQALSIANGAPQIILSLFKGG MALTVNTNIASLNTQRNLNNSSASLNTSLQRLSTGSRINSAKDDAAGLQIANRLTSQVNGLNV ATKNANDGISLAQTAEGALQQSTNILQRMRDLSLQSANGSNSDSERTALNGEVKQLQKELD RISNTTTFGGRKLLDGSFGVASFQVGSAANEIISVGIDEMSAESLNGTYFKADGGGAVTAATA SGTVDIAIGITGGSAVNVKVDMKGNETAEQAAAKIAAAVNDANVGIGAFSDGDTISYVSKAGK DGSGAITSAVSGVVIADTGSTGVGTAAGVTPSATAFAKTNDTVAKIDISTAKGAQSAVLVIDEA Flagellin IKQIDAQRADLGAVQNRFDNTINNLKNIGENVSAARGRIEDTDFAAETANLTKNQVLQQAGTAI P21184 LAQANQLPQSVLSLLR MKAQSISTYGATSALRALVAKNKAEMVKAQQEATTGTVFDVGLSLGSRTGQTVSLRKEYDRL SVLTDMNKLVQQRMTATQTAAGKIIENTQNFLGDLAGANNSGETAKTVAKSARSMLDSVTGL LNTSFNGEYIFAGVNTDVKPISDYADGSTAQNAVRQAFQDHFGFAMDDPQVANISGDEMKA FLEGDFAEQFNDANWAANWSDASDTRIKSRISPTETADTSISANADGFRKTVMSAVMVTEFA Flagellin DIGLNASAFDALTTQALQITTQAVTETTSEQTTLGLAQSRTEAATTRIAAQQKILNQSVLNLEE Q2YJG1 VDPYDAATRVNALKTQIETSYSLTVQLQNMSLLNYLR MMSANYISTLMLSSSLRTSITNNQAALSKASKEATTGRFADVGLELGATTGGDLTLRADWSF ADQLVDTNELVSGRLDVTQTRITQLGTTATSFLKDLIAARSTDNGGRIVLPPASANLQDLIGAL NVSYNGSYLFSGINTQNMPITAYATGSASKNQVDADFAAAPPTGFGFPQSSASVSSITPAQM QTFLNTTFDAEFASPAWNTNWSSATDQVMQSRISTTEVADTSVSANQTGFRKLAEAYTMMA Flagellin DLGNAKLSQETFQVVVDKAIGLIGGAITDLATLGGGVGTVQQRITSATNKLKTQQDILNNQIVG Q89F45 MEKVDPTEASVRVNTLQTQIQTALALTSQLQKISLINYL MKTSFVSNLAVQNAMRLTIQQGQAELLKLQTEVTTGRHADVGLALGSSAARSVSLQRELARL GTLVDTNSVVTQRLAASQSALSAMAEAAQQVRNTLVTFKGNDAADQLAIQKTEIQSAMSAFS SAANLSFNGEFLFAGINTDVRPLEDYNAAAKSTFDTALATYMSANGITSMSDFTKAQMEDFIT NTLEPLYDTEWAADWSKASSQNMTSRISTTEVVQSSTNATTEGFRKFALASVIALELMDENV Flagellin SSEVRAYIGEAALGYVEQANTQITAERSTLGISEARVKKANTSLQAQIKLINTHITDLEGVDTYE Q92RZ1 ASTRMNTLLTQVETSYTLTARIQRLSLIDFL Receptor CRTSCPLALASYYLENGTTLSVINQNLNSSIAPYDQINFDPILRYNSNIKDKDRIQMGSRVLVP AtCERK1 FPCECQPGDFLGHNFSYSVRQEDTYERVAISNYANLTTMESLQARNPFPATNIPLSATLNVLV NCSCGDESVSKDFGLFVTYPLRPEDSLSSIARSSGVSADILQRYNPGVNFNSGNGIVYVPGR DPNGAFPPFKSSKQDGVHHHHHH ANFTCAVASGTTCKSAILYTSPNATTYGNLVARFNTTTLPDLLGANGLPDGTLSSAPVAANST VKIPFRCRCNGDVGQSDRLPIYVVQPQDGLDAIARNVFNAFVTYQEIAAANNIPDPNKINVSQ TLWIPLPCSCDKEEGSNVMHLAYSVGKGENTSAIAAKYGVTESTLLTRNKIDDPTKLQMGQIL Receptor DVPLPVCRSSISDTSADHNLMLLPDGTYGFTAGNCIRCSCSSTTYQLNCTAVQNKGCPSVPL OsCEBiP CNGTLKLGETNGTGCGSTTCAYSGYSNSSSLIIQTSLATNQTTACQ GDGCSAGCDLALASFYVTPNQNVTNMADLFGIGAANYRSLAPYNPNIPNLDFINVGGRVNVY FTCGCRSLPGSPGATYLAGAFPFQMSRGQIYTSVAANYNNLTTAEWLQATNSYPANNIPDTA Receptor VINATVNCSCGDASISPDYGLFLTYPLRAEDTLASVAATYGLSSQLDVVRRYNPGMESATGS OsCERK1 GIVYIPVKDPNGSYLPLKSPGKGASHHHHHH Receptor for QQEYVNNKQLDCNNEYNSTKGNLCNSLPSCTSYLTFKSSPPEYTTPAAISFLLNSTPALIAAA NNITDVQTLPADTLVTVPVNCSCSGPYYQHNASYTIKVQGETYFSIANNTYQALTTCQALELQ Cercospora NTVGMRDLLKGQNLHVPLRCACPTQKQREAGFKYLLTYLVSQGESVSAIGDIFGVDEQSILD sojinia ANELSTSSVIFYFTPISVPLKTEP EPLLPSTYNVSMCSESFSCGGVEIRYPFYLANATADYSGSYYSCGYTDLSVSCELEVEGPPT Receptor for TWTPTIRLGGDNYTVKNIFYDFHTISLTDRDVLGGGECPVVRHNVSFDETWLHNASAFDNLT FFFGCHWGPRDTLPEFAGNNISCAGFSPPTISGGASFVFKPEDLDEQEEQELASHCDEVFSV Exserohilum PVGSEALRATDTFSLPRGGYGELLRQGFELEWNRASEDQCGQCEGSGSGGRCAYNQKRE turcicum FLGCLCSGGKAGNPFCKPSRSKRKE Receptor for GYPWQDCSDDQFAAGSKYLANINLLAASLPKNASASPDLFATAEAGAAPDKVWALALCRGD ANATSCLSCLAQAFRDLPNVCDYSKVATMYYDSCTLHYSNASRDPAPVAARTYRYWESTNV Fusarium TSEQAQFNSLVARLVNATADYAAYNSTRRYASGEADFNREFPKIYSWAQCTPDLTSSQCRQ graminearum CLAKNMVLLPQLFVDSTGARALQVSCSFRYQTYSF QSFEPEIEALKSFKNGISNDPLGVLSDWTIIGSLRHCNWTGITCDSTGHVVSVSLLEKQLEGVL SPAIANLTYLQVLDLTSNSFTGKIPAEIGKLTELNQLILYLNYFSGSIPSGIWELKNIFYLDLRNN LLSGDVPEEICKTSSLVLIGFDYNNLTGKIPECLGDLVHLQMFVAAGNHLTGSIPVSIGTLANLT DLDLSGNQLTGKIPRDFGNLLNLQSLVLTENLLEGDIPAEIGNCSSLVQLELYDNQLTGKIPAE LGNLVQLQALRIYKNKLTSSIPSSLFRLTQLTHLGLSENHLVGPISEEIGFLESLEVLTLHSNNF TGEFPQSITNLRNLTVLTVGFNNISGELPADLGLLTNLRNLSAHDNLLTGPIPSSISNCTGLKLL DLSHNQMTGEIPRGFGRMNLTFISIGRNHFTGEIPDDIFNCSNLETLSVADNNLTGTLKPLIGK LQKLRILQVSYNSLTGPIPREIGNLKDLNILYLHSNGFTGRIPREMSNLTLLQGLRMYSNDLEG Receptor PIPEEMFDMKLLSVLDLSNNKFSGQIPALFSKLESLTYLSLQGNKFNGSIPASLKSLSLLNTFDI FLS2 from SDNLLTGTIPGELLASLKNMQLYLNFSNNLLTGTIPKELGKLEMVQEIDLSNNLFSGSIPRSLQ ACKNVFTLDFSQNNLSGHIPDEVFQGMDMIISLNLSRNSFSGEIPQSFGNMTHLVSLDLSSNN Arabodpsis LTGEIPESLANLSTLKHLKLASNNLKGHVPESGVFKNINASDLMGNTDLCGSKKPLKPCTIKQ thaliana KSSHHHHHHH Receptor BAK1 from MERRLMIPCFFWLILVLDLVLRVSGNAEGDALSALKNSLADPNKVLQSWDATLVTPCTWFHV TCNSDNSVTRVDLGNANLSGQLVMQLGQLPNLQYLELYSNNITGTIPEQLGNLTELVSLDLYL Arabodpsis NNLSGPIPSTLGRLKKLRFLRLNNNSLSGEIPRSLTAVLTLQVLDLSNNPLTGDIPVNGSFSLF thaliana TPISFANTKLTPLPASPPPPISPTPPSPAGSHHHHHH

Claims

CLAIMS 1. An HFB-based capsule comprising a) at least one non-fusion hydrophobin, and b) at least one HFB fusion polypeptide, having a hydrophobin bound to a receptor, wherein the binding of the receptor to its target is sufficient to destabilize the HFB-based capsule, leading to its opening.

2. The HFB-based capsule of claim 1, wherein the binding of the receptor to its target results in the spatial fixing of the receptor to its target molecule.

3. The HFB-based capsule of any one of the preceding claims, wherein the at least one HFB fusion polypeptide comprises a hydrophobin selected from an HFBI, HFBII, HFB7, or which is a polypeptide of SEQ ID NO: 1-36, or a variant thereof with at least at least 85% sequence identity to any one of SEQ ID NO: 1-36.

4. The HFB-based capsule any one of the preceding claims, wherein the at least one HFB fusion polypeptide comprises a receptor selected from a) a Leucine Rich Repeat – Receptor Kinase (LRR-RK), b) a Leucine Rich Repeat – Receptor Protein (LRR-RP), c) a Lysin motif – Receptor Kinase (LysM-RK) or a Lysin motif – Receptor protein (LysM-RP), d) a receptor of SEQ ID NO: 56-63, e) AtLORE, AtWAK1, AtLecRK-I.8, AtDORN1, AtLecRK-I.9, AtLLG1-3, AtFER, o f) a FLS2 comprising amino acid residues R294, H316 and N674, and g) a BAK1 comprising amino acid residues T52, L53 and V54.

5. The HFB-based capsule of any one of the preceding claims, wherein the at least one HFB fusion polypeptide comprises a receptor capable of binding to a pathogen or microbe having a Pathogen-Associated Molecular Pattern (PAMP) or a Microbe-Associated Molecular Pattern (MAMP).

6. The HFB-based capsule of any one of the preceding claims, wherein the at least one HFB fusion polypeptide comprises a receptor capable of binding a target molecule from a pathogen or microbe selected from f) a bacterium selected from Escherichia spp., Salmonella spp., Staphylococcus spp., Xanthomonas spp., and Pseudomonas spp.; g) a fungus, selected from Cercospora spp., Exserohilum spp., Fusarium spp., Botrytis spp., Phytophthora spp., Candida spp., Aspergillus spp., and Spiroplasma spp.; h) a nematode selected from Meloidogyne spp., and Ascaris spp;i) a virus selected from Tomato mosaic virus, Tomato yellow curl virus, Influenza virus, and Herpes simplex virus; and j) a parasite, selected from Plasmodium spp., Trypanozoma spp.

7. The HFB-based capsule of any one of the preceding claims, wherein the HFB-based capsule comprises a non-fusion hydrophobin selected from an HFBI, HFBII, HFB7, or which is a polypeptide of SEQ ID NO: 1-36, or a variant thereof with at least 85% sequence identity to any one of SEQ ID NO: 1-36.

8. The HFB-based capsule of any one of the preceding claims, comprising at least two HFB fusion polypeptides, each having a hydrophobin bound to a receptor, wherein each receptor is a dimerizable receptor, and the dimerization of each receptor with the target is sufficient to destabilize the HFB-based capsule, leading to its opening.

9. The HFB-based capsule of claim 8, wherein the binding of the dimerizable receptor to its target molecule induces the formation of a dimer-target complex, and reduces the interaction of the dimer-target complex, and the at least one non-fusion hydrophobin, destabilizing the HFB-based capsule, leading to its opening.

10. The HFB-based capsule of any one of the preceding claims, wherein the HFB-based capsule encapsulates a compound selected from an antibacterial, an antifungal, an antinematode, an antiviral, an antiparasitic, an analgesic, a nutraceutical, an essential oil, an industrial chemical, and a cosmetic ingredient.

11. A hydrophobin (HFB) fusion polypeptide comprising a hydrophobin, and a dimerizable receptor bound to said HFB, wherein the HFB fusion polypeptide binds to its target molecule by forming a dimer.

12. The hydrophobin fusion polypeptide of claim 11, wherein the hydrophobin is selected from an HFBI, HFBII, HFB7, or which is a polypeptide of SEQ ID NO: 1-36, or a variant thereof with at least 85% sequence identity to any one of SEQ ID NO: 1-36.

13. The hydrophobin fusion polypeptide of any one of claims 11 or 12, wherein the dimerizable receptor is selected from a) a Leucine Rich Repeat – Receptor Kinase (LRR-RK), b) a Leucine Rich Repeat – Receptor Protein (LRR-RP), c) a Lysin motif – Receptor Kinase (LysM-RK) or a Lysin motif – Receptor protein (LysM-RP), d) a receptor of SEQ ID NO: 56-63, e) AtLORE, AtWAK1, AtLecRK-I.8, AtDORN1, AtLecRK-I.9, AtLLG1-3, AtFER, orf) a FLS2 comprising amino acid residues R294, H316 and N674, or g) a BAK1 comprising amino acid residues T52, L53 and V54; 14. The hydrophobin fusion polypeptide of any one of claims 11-13, wherein the dimerizable receptor binds to a target selected from a Pathogen-Associated Molecular Pattern (PAMP) and a Microbe-Associated Molecular Pattern (MAMP) 15. A composition comprising a) an HFB-based capsule of any one of claims 1-10, b) at least one suitable excipient, and c) a compound of interest, wherein said compound of interest is encapsulated by the HFB-based capsule.

16. The composition of claim 15, wherein the compound of interest is an agronomical compound selected from an antibacterial, an antifungal, an antinematode, or an antiviral compound.

17. The composition of claim 16, wherein the composition is applied to a plant selected from main row crops, fruits and vegetables.

18. The composition of claim 17, wherein the plant is affected by a pathogen or microbe selected from a) a bacterium selected from Xanthomonas spp., Pseudomonas spp.; b) a fungus selected from Cercospora spp., Exserohilum spp., Fusarium spp., Botrytis spp., Phytophthora spp.; c) a nematode selected from Meloidogyne spp.; and d) a virus, selected from Tobacco mosaic virus, and Tomato yellow curl virus.

19. The composition of claim 15, wherein the compound of interest is a gastronomical compound selected from an antibacterial, an antifungal, an antinematode, an antiviral, an antiparasitic, an analgesic, a nutraceutical, or a colorant compound.

20. The composition of claim 19, wherein the composition is applied to a food product selected from dairy products, bakery products, and meat-based products.

21. The composition of claim 20, wherein the food product comprises a pathogen or microbe selected from a) a bacterium selected from Escherichia spp., Salmonella spp., Staphylococcus spp., Pseudomonas spp; b) a fungus selected from Fusarium spp., Candida spp., Aspergillus spp. Spiroplasma spp.;c) a nematode selected from Ascaris spp.; d) a virus selected from Influenza virus, or Herpes simplex virus; and e) a parasite selected from Plasmodium spp., Trypanozoma spp.

22. The composition of claim 15, wherein the compound of interest is a pharmaceutical compound selected from an antibacterial, an antifungal, an antinematode, an antiviral, an antiparasitic, an analgesic, a nutraceutical, or a colorant compound.

23. The composition of claim 22, wherein the pharmaceutical composition is applied to an organism in need selected from humans and other primates (e.g. apes and monkeys), farm animals (e.g. cattle, sheep, pigs, goats, horses), pets and other domestic animals (e.g. dogs, cats), laboratory animals (e.g. mice, rats, guinea pigs, rabbits), birds and poultry (chickens, turkeys, ducks, geese) for the treatment of a condition caused by a pathogen or microbe.

24. The composition of claim 23, wherein the pathogen or microbe is selected from a) a bacterium selected from Escherichia spp., Salmonella spp., Staphylococcus spp., Pseudomonas spp; b) a fungus selected from Fusarium spp., Candida spp., Aspergillus spp. Spiroplasma spp.; c) a nematode selected from Ascaris spp.; d) a virus selected from Influenza virus, or Herpes simplex virus; and e) a parasite selected from Plasmodium spp., Trypanozoma spp.

25. A method for applying a compound of interest, comprising the steps of a) providing the composition of any one of claims 15-24, b) applying an effective amount of said composition to an organism in need, c) contacting the HFB-based capsule with a target molecule.

26. A method for detecting a pathogen or microbe of interest, comprising the steps of a) providing an HFB-based capsule of any one of claims 1-10, and a reporter compound encapsulated by the HFB-based capsule, b) contacting the HFB-based capsule of step a) with the pathogen or microbe of interest, c) revealing the contact of step b) by measuring the release of the reporter compound.

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