Adsorption of a fungal hydrophobin onto surfaces as mediated by the associated polysaccharide schizophyllan

Martin, Gregory G.; Cannon, Gordon C.; McCormick, Charles L.

doi:10.1002/(sici)1097-0282(199906)49:7<621::aid-bip7>3.0.co;2-o

Cited by 12 publications

(25 citation statements)

References 36 publications

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“…In this work, we were interested in how class II hydrophobins in aqueous solution could assemble on a solid polar hydrophilic surface so that the hydrophobic side of the membrane would face outward significantly reducing the polarity of the surface. It is already known quite well how hydrophobin layers are formed on hydrophobic surfaces. , The mass of such layers corresponds to a monomolecular layer of protein, suggesting that the hydrophobin binds with its hydrophobic patch to the hydrophobic surface and exposes its hydrophilic side out toward the hydrophilic surroundings. Interestingly, it was found that this hydrophilic side has some unexpected properties.…”

Section: Introductionmentioning

confidence: 99%

Self-assembly of Class II Hydrophobins on Polar Surfaces

et al. 2012

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Hydrophobins are structural proteins produced by filamentous fungi that are amphiphilic and function through self-assembling into structures such as membranes. They have diverse roles in the growth and development of fungi, for example in adhesion to substrates, for reducing surface tension to allow aerial growth, in forming protective coatings on spores and other structures. Hydrophobin membranes at the air-water interface and on hydrophobic solids are well studied, but understanding how hydrophobins can bind to a polar surface to make it more hydrophobic has remained unresolved. Here we have studied different class II hydrophobins for their ability to bind to polar surfaces that were immersed in buffer solution. We show here that the binding under some conditions results in a significant increase of water contact angle (WCA) on some surfaces. The highest contact angles were obtained on cationic surfaces where the hydrophobin HFBI has an average WCA of 62.6° at pH 9.0, HFBII an average of 69.0° at pH 8.0, and HFBIII had an average WCA of 61.9° at pH 8.0. The binding of the hydrophobins to the positively charged surface was shown to depend on both pH and ionic strength. The results are significant for understanding the mechanism for formation of structures such as the surface of mycelia or fungal spore coatings as well as for possible technical applications.

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Section: Introductionmentioning

confidence: 99%

Self-assembly of Class II Hydrophobins on Polar Surfaces

et al. 2012

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“…Self-assembly of a rodlet layer has not been reported for the two other histidine-tagged hydrophobins that were expressed in E. coli (Peñas et al, 1998;Tagu et al, 2001). It cannot be excluded that components such as polysaccharides (Martin et al, 1999b) an impact on the formation of rodlet layers. When the native DGH1 was isolated from the hydrophobin extract it also failed to form rodlets: thus, other components in the extract are also important.…”

Section: Discussionmentioning

confidence: 96%

“…, 2001). It cannot be excluded that components such as polysaccharides (Martin et al. , 1999b) may have an impact on the formation of rodlet layers.…”

Section: Discussionmentioning

confidence: 99%

Differential expression of hydrophobins DGH1, DGH2 and DGH3 and immunolocalization of DGH1 in strata of the lichenized basidiocarp of Dictyonema glabratum

2002

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Summary• The expression of hydrophobin genes DGH1 , DGH2 and DGH3 in the lichenized fruitbody of Dictyonema glabratum (syn. Cora pavonia ) is reported here, as well as immunolocalization of the DGH1 protein.• In situ hybridization was conducted to determine expression patterns of hydrophobin genes DGH1 , DGH2 and DGH3 . The DGH1 protein was expressed in Escherichia coli and used to raise antibodies for immunolocalization of the DGH1 protein.• DGH1 and DGH2 are expressed by hyphae in the photobiont layer and the lower stratum. DGH3 is newly expressed by hyphae in the boundary layer. DGH1 is immunolocalized in the electron-dense outer layer of fungal walls lining gas-filled spaces in the photobiont layer, in aerial hyphae in the gas-filled lower stratum and in the transition zone between the two strata.• Dictyonema glabratum hydrophobins surround wall surfaces in the photobiont layer of the fruitbody. Hydrophobin layers probably function to keep interhyphal spaces water-free, seal the apoplast to enable water translocation, and define strata within the basidiocarp.

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“…Sc3p is able to form a self-assembled coat on various surfaces such as Teflon and Parafilm and render these surfaces hydrophilic based on water contact angle measurements (3,26). Sc3p can also coat hydrophilic surfaces such as glass or mica increasing the hydrophobic nature (3,26). Treatment of the hydrophobic surfaces with hot SDS, normally destructive to the secondary and tertiary structure of proteins, is ineffective in removing the hydrophobin coating.…”

Section: Hydrophobinmentioning

confidence: 99%

“…The studies conducted by our group first focused on de novo synthesis of a completely artificial polypeptide and then progressed to the detailed investigation of the naturally occurring polypeptides apolipophorin-III (Apo-III) (1,2) and hydrophobins (3)(4)(5)(6)(7)(8). Native functions make these proteins excellent candidates for recombinant modification and production as stimuli-controllable carriers of hydrophobic molecules in aqueous environments.…”

Section: Introductionmentioning

confidence: 99%

Proteins as Amphipathic Biopolymeric Materials

Stroud

Goodwin

Martin

et al. 2000

Stimuli-Responsive Water Soluble and Amphiphilic Polymers

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Many naturally-occurring macromolecules perform their respective native functions by changing conformation in response to local environmental changes. Of special interest are amphipathic transport proteins designed to capture and sequester hydrophobic molecules in water in a stimuli -responsive manner. Recombinant DNA methods have been utilized in our ongoing research with the eventual goal of exploiting physical and chemical attributes inherent to such native proteins. Reported in this chapter are (1) the design and synthesis of an artificial gene encoding desired microstructural sequences of a de novo protein, DN3L, and (2) the production of recombinantly modified proteins based on apolipophorin-III and hydrophobin.

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Adsorption of a fungal hydrophobin onto surfaces as mediated by the associated polysaccharide schizophyllan

Cited by 12 publications

References 36 publications

Self-assembly of Class II Hydrophobins on Polar Surfaces

Self-assembly of Class II Hydrophobins on Polar Surfaces

Differential expression of hydrophobins DGH1, DGH2 and DGH3 and immunolocalization of DGH1 in strata of the lichenized basidiocarp of Dictyonema glabratum

Proteins as Amphipathic Biopolymeric Materials

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