Hydrophobin

Hydrophobin
Hydrophobin
Identifiers
Symbol	Hydrophobin
Pfam	PF01185
InterPro	IPR001338
Pfam
Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Fungal hydrophobin
Fungal hydrophobin
	Structure of hydrophobin HFBII from Trichoderma reesei
Identifiers
Symbol	Hydrophobin_2
Pfam	PF06766
InterPro	IPR010636
PROSITE	PDOC00739
SCOP2	1r2m / SCOPe / SUPFAM
OPM superfamily	96
OPM protein	1r2m
Pfam
Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Last updated October 10, 2024

Hydrophobins 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.^[1] Hydrophobins are known for their ability to form a hydrophobic (water-repellent) coating on the surface of an object.^[2] They were first discovered and separated in Schizophyllum commune in 1991.^[3] 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. Class I monolayer contains the same core structure as amyloid fibrils, and is positive to Congo red and thioflavin T. The monolayer formed by class I hydrophobins has a highly ordered structure, and can only be dissociated by concentrated trifluoroacetate or formic acid. Monolayer assembly involves large structural rearrangements with respect to the monomer.^[4]

Hydrophobins have been identified in lichens ^[5] as well as non-lichenized ascomycetes and basidiomycetes; whether they exist in other groups is not known.^[6] Hydrophobins are generally found on the outer surface of conidia and of the hyphal wall, and may be involved in mediating contact and communication between the fungus and its environment.^[7] Some family members contain multiple copies of the domain.

Hydrophobins have been found to be structurally and functionally similar to cerato-platanins, another group of small cysteine-rich proteins,^[8] which also contain a high percentage of hydrophobic amino acids,^[6] and are also associated with hyphal growth.^[9]^[10]

This family of proteins includes the rodlet proteins of Neurospora crassa (gene eas) and Emericella nidulans (gene rodA), these proteins are the main component of the hydrophobic sheath covering the surface of many fungal spores.^[11]^[12]

Genomic sequencing of two fungi from dry or salty environments ( Wallemia sebi and W. ichthyophaga ) revealed that these species contain predicted hydrophobins with unusually high proportion of acidic amino acids and therefore with potentially novel characteristics.^[13] High proportion of acidic amino acids is thought to be an adaptation of proteins to high concentrations of salt.^[14]

Structure

Hydrophobins are characterised by the presence of 8 conserved cysteine residues that form 4 disulphide bonds.^[15] They are able to reverse the wettability of surfaces by spontaneous self-assembly of the monomeric proteins into amphipathic monolayers at hydrophobic:hydrophilic surfaces. Despite this common feature, hydrophobins are subdivided into two classes based on differences on their monomeric structure, such as the spacing between the cysteine residues, and based on the different physicochemical properties of the amphipathic monolayers they form.^[15]^[16] Extensive structural analyses of individual hydrophobins from the two classes have elucidated that the morphological and physical differences between the class I and class II polymer forms are the results of significant structural differences at the monomer-assembly level.

Class I

Class I hydrophobins are characterised by having a quite diverse amino acid sequence between different types (with exception of the conserved cysteine residues), and compared to class II, they have long, varied inter-cysteine spacing.^[17] They form rodlets which have been identified as functional amyloids due to their amyloid-like characteristics as seen in X-ray diffraction studies and confirmed by their capacity to bind to amyloid-specific dyes such as Congo red and Thioflavin T.^[18] The formation of rodlets involves conformational changes^[19] that lead to formation of an extremely robust β-sheet structure^[20] that can only be depolymerised by treatment with strong acids.^[21] The rodlets can spontaneously form ordered monolayers by lateral assembly, displaying a regular fibrillary morphology on hydrophobic:hydrophilic interfaces.^[22] The most well characterised class I hydrophobin is EAS, which coats the spores of the fungus Neurospora crassa , followed by characterisation of DewA from Aspergillus nidulans .^[23]

Class II

Class II hydrophobins have overall a more conserved amino acid sequence between the different types and, contrary to class I, they have short, regular inter-cysteine spacing.^[17] Opposite to class I, the class II hydrophobins monolayer formed at hydrophobic:hydrophilic interfaces is not fibrillar and it is not associated with formation of amyloid-structures, nor with large conformational changes.^[22] Nonetheless, high resolution atomic-force microscopy studies revealed the formation of a notable hexagonal repeating pattern over surfaces coated with the class II hydrophobin HBFI, meaning that these proteins are also able to form an ordered network in surface films.^[24]

The crystal structures or HFBI and HFBII from Trichoderma reesei were the first class II hydrophobins to be determined.

Rodlet self-assembly of class I hydrophobins

There is special interest in understanding the mechanism underlying class I monomers self-assembly that leads to formation of tough, ordered amphipathic rodlet monolayers, due to their intrinsic properties and due to substantial information available from several characterisation studies of the class I hydrophobins EAS and DewA. These mechanisms have been greatly studied by targeted mutagenesis in an effort to identify the key amino acid sequence regions driving rodlet self-assembly. A model for the monomeric form of EAS was proposed by Kwan et al. (2006) from structural data obtained from NMR spectroscopy and X-ray diffraction experiments that indicated the presence of four-stranded, antiparallel β-barrel core structure in EAS that allows monomer linking through backbone H-bonding.^[18] There are secondary elements around this β-barrel core like the Cys3-Cys4 and Cys7-Cys8 loops. This model is consistent with the amyloid-like structure that class I rodlets form, in which the β-strands are oriented perpendicular to the cross-β scaffold axis of the fibre.^[25]

Site-directed mutagenesis of EAS has given insights into the specific structural changes responsible for self-assembly of monomers into rodlets and subsequent formation of amphipathic monolayer in hydrophobic:hydrophilic interfaces. Kwan et al. (2008) reported that the long hydrophobic Cys3-Cys4 loop is not required for rodlet assembly because its deletion does not affect the folding and physical properties of the monomeric protein, neither the morphology of the polymeric rodlet form.^[26] Instead, a region of the short Cys7-Cys8 loop, containing mainly uncharged polar residues, has been found to be critical for rodlet assembly.^[15]

Characterization of EAS secondary elements involved in rodlet assembly have given insights into the mechanism behind class I hydrophobins self-assembly, but important structural differences with DewA, another class I hydrophobin, suggest that the mechanisms driving rodlet assembly vary among different types of hydrophobins. Like EAS, DewA also has a β-barrel core structure, but it differs significantly from it because of its considerable content of helical secondary elements.^[27] A unique feature of DewA is its capacity to exist as two types of conformers in solution, both able to form rodlet assemblies but at different rates.^[23] Despite these differences in structural and self-assembly mechanisms, both EAS and DewA form robust fibrillar monolayers, meaning that there must exist several pathways, protein sequences and tertiary conformations able to self-assemble into amphipathic monolayers. Further characterisation of both EAS and DewA and their rodlet self-assembly mechanisms will open up opportunities for rational design of hydrophobins with novel biotechnological applications.

Potentiality for use

Since the very first studies that gave insights into the properties of hydrophobins, these small proteins have been regarded as great candidates for technological use.^[16] The detailed understanding of the molecular mechanisms underlying hydrophobin self-assembly into amphipathic monolayer in hydrophobic:hydrophilic interfaces is of great academic interest but mainly of commercial interest. This is because a deep understanding of the elements driving these mechanisms would allow engineering of hydrophobins (or other biomolecules) for nano and biotechnological applications. An example is that the hydrophobin-coating of carbon nanotubes was found to increase their solubility and reduce their toxicity, a finding that increases the prospects of carbon nanotubes to be used as vehicles for drug delivery.^[28] Other areas of potential use of hydrophobins include:

Fabrication and coating of nanodevices and medical implants to increase biocompatibility.
Emulsifiers in food industry and personal care products.
Hydrophobins' high stability can be very useful in the coating of surfaces of prolonged use or under harsh conditions.
The easy dissociation of a class II hydrophobin monolayer might be desirable and this can easily be achieved by the use of detergents and alcohols.
The use of hydrophobins in protein purification,^[29]^[30]^[31] drug delivery^[32]^[33]^[34] and cell attachment^[35]^[36]^[37] has been reported.

For more about the potential biotechnological applications of hydrophobins see Hektor & Scholtmeijer (2005)^[38] and Cox & Hooley (2009).^[39]

Related Research Articles

A biological membrane, biomembrane or cell membrane is a selectively permeable membrane that separates the interior of a cell from the external environment or creates intracellular compartments by serving as a boundary between one part of the cell and another. Biological membranes, in the form of eukaryotic cell membranes, consist of a phospholipid bilayer with embedded, integral and peripheral proteins used in communication and transportation of chemicals and ions. The bulk of lipids in a cell membrane provides a fluid matrix for proteins to rotate and laterally diffuse for physiological functioning. Proteins are adapted to high membrane fluidity environment of the lipid bilayer with the presence of an annular lipid shell, consisting of lipid molecules bound tightly to the surface of integral membrane proteins. The cell membranes are different from the isolating tissues formed by layers of cells, such as mucous membranes, basement membranes, and serous membranes.

Protein folding is the physical process by which a protein, after synthesis by a ribosome as a linear chain of amino acids, changes from an unstable random coil into a more ordered three-dimensional structure. This structure permits the protein to become biologically functional.

Cysteine is a semiessential proteinogenic amino acid with the formula HOOC−CH(−NH₂)−CH₂−SH. The thiol side chain in cysteine often participates in enzymatic reactions as a nucleophile. Cysteine is chiral, but both D and L-cysteine are found in nature. L‑Cysteine is a protein monomer in all biota, and D-cysteine acts as a signaling molecule in mammalian nervous systems. Cysteine is named after its discovery in urine, which comes from the urinary bladder or cyst, from Greek κύστη kýsti, "bladder".

Amyloids are aggregates of proteins characterised by a fibrillar morphology of typically 7–13 nm in diameter, a β-sheet secondary structure and ability to be stained by particular dyes, such as Congo red. In the human body, amyloids have been linked to the development of various diseases. Pathogenic amyloids form when previously healthy proteins lose their normal structure and physiological functions (misfolding) and form fibrous deposits within and around cells. These protein misfolding and deposition processes disrupt the healthy function of tissues and organs.

<span class="mw-page-title-main">Amphiphile</span> Chemical compound with both hydrophilic and lipophilic properties

In chemistry, an amphiphile, or amphipath, is a chemical compound possessing both hydrophilic and lipophilic properties. Such a compound is called amphiphilic or amphipathic. Amphiphilic compounds include surfactants and detergents. The phospholipid amphiphiles are the major structural component of cell membranes.

<span class="mw-page-title-main">Dipalmitoylphosphatidylcholine</span> Chemical compound

Dipalmitoylphosphatidylcholine (DPPC) is a phospholipid (and a lecithin) consisting of two C₁₆ palmitic acid groups attached to a phosphatidylcholine head-group.

In protein structures, a beta barrel(β barrel) is a beta sheet composed of tandem repeats that twists and coils to form a closed toroidal structure in which the first strand is bonded to the last strand. Beta-strands in many beta-barrels are arranged in an antiparallel fashion. Beta barrel structures are named for resemblance to the barrels used to contain liquids. Most of them are water-soluble outer membrane proteins and frequently bind hydrophobic ligands in the barrel center, as in lipocalins. Others span cell membranes and are commonly found in porins. Porin-like barrel structures are encoded by as many as 2–3% of the genes in Gram-negative bacteria. It has been shown that more than 600 proteins with various function such as oxidase, dismutase, and amylase contain the beta barrel structure.

Hydrophobic collapse is a proposed process for the production of the 3-D conformation adopted by polypeptides and other molecules in polar solvents. The theory states that the nascent polypeptide forms initial secondary structure creating localized regions of predominantly hydrophobic residues. The polypeptide interacts with water, thus placing thermodynamic pressures on these regions which then aggregate or "collapse" into a tertiary conformation with a hydrophobic core. Incidentally, polar residues interact favourably with water, thus the solvent-facing surface of the peptide is usually composed of predominantly hydrophilic regions.

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The enzyme cutinase is a member of the hydrolase family. It catalyzes the following reaction:

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References

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↑ Wessels J, De Vries O, Asgeirsdottir SA, Schuren F (August 1991). "Hydrophobin Genes Involved in Formation of Aerial Hyphae and Fruit Bodies in Schizophyllum". The Plant Cell. 3 (8): 793–799. doi:10.1105/tpc.3.8.793. PMC 160046 . PMID 12324614.
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↑ Peter Döbbeler, Gerhard Rambold (2004). Contributions to Lichenology. Gebrüder Borntraeger Verlagsbuchhandlung. p. 207.
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1 2 Morris VK, Kwan AH, Sunde M (January 2013). "Analysis of the structure and conformational states of DewA gives insight into the assembly of the fungal hydrophobins". Journal of Molecular Biology. 425 (2): 244–56. doi:10.1016/j.jmb.2012.10.021. PMID 23137797.
↑ Szilvay GR, Paananen A, Laurikainen K, Vuorimaa E, Lemmetyinen H, Peltonen J, Linder MB (March 2007). "Self-assembled hydrophobin protein films at the air-water interface: structural analysis and molecular engineering". Biochemistry. 46 (9): 2345–54. doi:10.1021/bi602358h. PMID 17297923.
↑ Sunde M, Serpell LC, Bartlam M, Fraser PE, Pepys MB, Blake CC (October 1997). "Common core structure of amyloid fibrils by synchrotron X-ray diffraction". Journal of Molecular Biology. 273 (3): 729–39. doi:10.1006/jmbi.1997.1348. PMID 9356260.
↑ Kwan AH, Macindoe I, Vukasin PV, Morris VK, Kass I, Gupte R, Mark AE, Templeton MD, Mackay JP, Sunde M (October 2008). "The Cys3-Cys4 loop of the hydrophobin EAS is not required for rodlet formation and surface activity". Journal of Molecular Biology. 382 (3): 708–20. doi:10.1016/j.jmb.2008.07.034. PMID 18674544.
↑ Morris VK, Kwan AH, Mackay JP, Sunde M (April 2012). "Backbone and sidechain ¹H, ¹³C and ¹⁵N chemical shift assignments of the hydrophobin DewA from Aspergillus nidulans". Biomolecular NMR Assignments. 6 (1): 83–6. doi:10.1007/s12104-011-9330-5. PMID 21845363. S2CID 29402126.
↑ Yang W, Ren Q, Wu YN, Morris VK, Rey AA, Braet F, Kwan AH, Sunde M (January 2013). "Surface functionalization of carbon nanomaterials by self-assembling hydrophobin proteins". Biopolymers. 99 (1): 84–94. doi:10.1002/bip.22146. PMID 23097233.
↑ Linder MB, Qiao M, Laumen F, Selber K, Hyytiä T, Nakari-Setälä T, Penttilä ME (September 2004). "Efficient purification of recombinant proteins using hydrophobins as tags in surfactant-based two-phase systems". Biochemistry. 43 (37): 11873–82. doi:10.1021/bi0488202. PMID 15362873.
↑ Collén A, Penttilä M, Stålbrand H, Tjerneld F, Veide A (January 2002). "Extraction of endoglucanase I (Ce17B) fusion proteins from Trichoderma reesei culture filtrate in a poly(ethylene glycol)-phosphate aqueous two-phase system". Journal of Chromatography A. 943 (1): 55–62. doi:10.1016/S0021-9673(01)01433-9. PMID 11820281.
↑ Joensuu JJ, Conley AJ, Lienemann M, Brandle JE, Linder MB, Menassa R (February 2010). "Hydrophobin fusions for high-level transient protein expression and purification in Nicotiana benthamiana". Plant Physiology. 152 (2): 622–33. doi:10.1104/pp.109.149021. PMC 2815860 . PMID 20018596.
↑ Haas Jimoh Akanbi M, Post E, Meter-Arkema A, Rink R, Robillard GT, Wang X, Wösten HA, Scholtmeijer K (February 2010). "Use of hydrophobins in formulation of water insoluble drugs for oral administration". Colloids and Surfaces B: Biointerfaces. 75 (2): 526–31. doi:10.1016/j.colsurfb.2009.09.030. PMID 19836932.
↑ Bimbo LM, Sarparanta M, Mäkilä E, Laaksonen T, Laaksonen P, Salonen J, Linder MB, Hirvonen J, Airaksinen AJ, Santos HA (May 2012). "Cellular interactions of surface modified nanoporous silicon particles". Nanoscale. 4 (10): 3184–92. Bibcode:2012Nanos...4.3184B. doi:10.1039/c2nr30397c. PMID 22508528.
↑ Sarparanta M, Bimbo LM, Rytkönen J, Mäkilä E, Laaksonen TJ, Laaksonen P, Nyman M, Salonen J, Linder MB, Hirvonen J, Santos HA, Airaksinen AJ (March 2012). "Intravenous delivery of hydrophobin-functionalized porous silicon nanoparticles: stability, plasma protein adsorption and biodistribution". Molecular Pharmaceutics. 9 (3): 654–63. doi:10.1021/mp200611d. PMID 22277076.
↑ Nakari-Setälä T, Azeredo J, Henriques M, Oliveira R, Teixeira J, Linder M, Penttilä M (July 2002). "Expression of a fungal hydrophobin in the Saccharomyces cerevisiae cell wall: effect on cell surface properties and immobilization". Applied and Environmental Microbiology. 68 (7): 3385–91. Bibcode:2002ApEnM..68.3385N. doi:10.1128/AEM.68.7.3385-3391.2002. PMC 126783 . PMID 12089019.
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