Literature DB >> 16219510

Hydrophobins: the protein-amphiphiles of filamentous fungi.

Markus B Linder1, Géza R Szilvay, Tiina Nakari-Setälä, Merja E Penttilä.   

Abstract

Hydrophobins are surface active proteins produced by filamentous fungi. They have a role in fungal growth as structural components and in the interaction of fungi with their environment. They have, for example, been found to be important for aerial growth, and for the attachment of fungi to solid supports. Hydrophobins also render fungal structures, such as spores, hydrophobic. The biophysical properties of the isolated proteins are remarkable, such as strong adhesion, high surface activity and the formation of various self-assembled structures. The first high resolution three dimensional structure of a hydrophobin, HFBII from Trichoderma reesei, was recently solved. In this review, the properties of hydrophobins are analyzed in light of these new data. Various application possibilities are also discussed.

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Year:  2005        PMID: 16219510     DOI: 10.1016/j.femsre.2005.01.004

Source DB:  PubMed          Journal:  FEMS Microbiol Rev        ISSN: 0168-6445            Impact factor:   16.408


  115 in total

1.  Self-assembly of functional, amphipathic amyloid monolayers by the fungal hydrophobin EAS.

Authors:  Ingrid Macindoe; Ann H Kwan; Qin Ren; Vanessa K Morris; Wenrong Yang; Joel P Mackay; Margaret Sunde
Journal:  Proc Natl Acad Sci U S A       Date:  2012-01-23       Impact factor: 11.205

2.  Expression and purification of a functionally active class I fungal hydrophobin from the entomopathogenic fungus Beauveria bassiana in E. coli.

Authors:  Brett H Kirkland; Nemat O Keyhani
Journal:  J Ind Microbiol Biotechnol       Date:  2010-07-17       Impact factor: 3.346

Review 3.  Ectomycorrhizas and water relations of trees: a review.

Authors:  Tarja Lehto; Janusz J Zwiazek
Journal:  Mycorrhiza       Date:  2010-12-08       Impact factor: 3.387

4.  Atomic force microscopy images suggest aggregation mechanism in cerato-platanin.

Authors:  F Sbrana; L Bongini; G Cappugi; D Fanelli; A Guarino; L Pazzagli; A Scala; M Vassalli; C Zoppi; B Tiribilli
Journal:  Eur Biophys J       Date:  2007-04-12       Impact factor: 1.733

5.  Interactions of hydrophobin proteins in solution studied by small-angle X-ray scattering.

Authors:  Kaisa Kisko; Géza R Szilvay; Ulla Vainio; Markus B Linder; Ritva Serimaa
Journal:  Biophys J       Date:  2007-09-07       Impact factor: 4.033

6.  Recombinantly produced hydrophobins from fungal analogues as highly surface-active performance proteins.

Authors:  Wendel Wohlleben; Thomas Subkowski; Claus Bollschweiler; Bernhard von Vacano; Yaqian Liu; Wolfgang Schrepp; Ulf Baus
Journal:  Eur Biophys J       Date:  2009-03-17       Impact factor: 1.733

7.  Structure-function relationships in hydrophobins: probing the role of charged side chains.

Authors:  Michael Lienemann; Julie-Anne Gandier; Jussi J Joensuu; Atsushi Iwanaga; Yoshiyuki Takatsuji; Tetsuya Haruyama; Emma Master; Maija Tenkanen; Markus B Linder
Journal:  Appl Environ Microbiol       Date:  2013-07-08       Impact factor: 4.792

8.  Surface display of HFBI and DewA hydrophobins on Saccharomyces cerevisiae modifies tolerance to several adverse conditions and biocatalytic performance.

Authors:  Cecilia Andreu; Javier Gómez-Peinado; Lex Winandy; Reinhard Fischer; Marcel Li Del Olmo
Journal:  Appl Microbiol Biotechnol       Date:  2021-01-23       Impact factor: 4.813

9.  Surface hydrophobicity of culture and water biofilm of Penicillium spp.

Authors:  Virginia Siqueira; Nelson Lima
Journal:  Curr Microbiol       Date:  2011-10-20       Impact factor: 2.188

10.  Hydrophobin fusions for high-level transient protein expression and purification in Nicotiana benthamiana.

Authors:  Jussi J Joensuu; Andrew J Conley; Michael Lienemann; Jim E Brandle; Markus B Linder; Rima Menassa
Journal:  Plant Physiol       Date:  2009-12-11       Impact factor: 8.340

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