Hydrophobins:: the protein-amphiphiles of filamentous fungi

被引:491
作者
Linder, MB
Szilvay, GR
Nakari-Setälä, T
Penttilä, ME
机构
[1] VTT Biotechnol, FIN-02044 Espoo, Finland
[2] Univ Helsinki, Inst Biotechnol, Programme Struct Biol & Biophys, FIN-00014 Helsinki, Finland
基金
芬兰科学院;
关键词
hydrophobin; filamentous fungus; protein amphiphile; protein surfactant; protein self-assembly; protein adhesion;
D O I
10.1016/j.femsre.2005.01.004
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
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. (c) 2005 Federation of European Microbiological Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码:877 / 896
页数:20
相关论文
共 98 条
[71]   Cerato-ulmin, a hydrophobin secreted by the causal agents of Dutch elm disease, is a parasitic fitness factor [J].
Temple, B ;
Horgen, PA ;
Bernier, L ;
Hintz, WE .
FUNGAL GENETICS AND BIOLOGY, 1997, 22 (01) :39-53
[72]   Biological roles for cerato-ulmin, a hydrophobin secreted by the elm pathogens, Ophiostoma ulmi and O-novo-ulmi [J].
Temple, B ;
Horgen, PA .
MYCOLOGIA, 2000, 92 (01) :1-9
[73]   CLUSTAL-W - IMPROVING THE SENSITIVITY OF PROGRESSIVE MULTIPLE SEQUENCE ALIGNMENT THROUGH SEQUENCE WEIGHTING, POSITION-SPECIFIC GAP PENALTIES AND WEIGHT MATRIX CHOICE [J].
THOMPSON, JD ;
HIGGINS, DG ;
GIBSON, TJ .
NUCLEIC ACIDS RESEARCH, 1994, 22 (22) :4673-4680
[74]   Aggregation and self-assembly of hydrophobins from Trichoderma reesei:: Low-resolution structural models [J].
Torkkeli, M ;
Serimaa, R ;
Ikkala, O ;
Linder, M .
BIOPHYSICAL JOURNAL, 2002, 83 (04) :2240-2247
[75]   Hydrophobins DGH1, DGH2, and DGH3 in the lichen-forming basidiomycete Dictyonema glabratum [J].
Trembley, ML ;
Ringli, C ;
Honegger, R .
FUNGAL GENETICS AND BIOLOGY, 2002, 35 (03) :247-259
[76]   Surface attachment and pre-penetration stage development by plant pathogenic fungi [J].
Tucker, SL ;
Talbot, NJ .
ANNUAL REVIEW OF PHYTOPATHOLOGY, 2001, 39 :385-+
[77]   SC3 and SC4 hydrophobins have distinct roles in formation of aerial structures in dikaryons of Schizophyllum commune [J].
van Wetter, MA ;
Wösten, HAB ;
Wessels, JGH .
MOLECULAR MICROBIOLOGY, 2000, 36 (01) :201-210
[78]   A comparison of the surface activity of the fungal hydrophobin SC3p with those of other proteins [J].
vanderVegt, W ;
vanderMei, HC ;
Wosten, HAB ;
Wessels, JGH ;
Busscher, HJ .
BIOPHYSICAL CHEMISTRY, 1996, 57 (2-3) :253-260
[79]  
WANG X, 2004, DEPT BIOCH, P153
[80]   Oligomerization of hydrophobin SC3 in solution: From soluble state to self-assembly [J].
Wang, XQ ;
Graveland-Bikker, JF ;
De Kruif, CG ;
Robillard, GT .
PROTEIN SCIENCE, 2004, 13 (03) :810-821