A peptide from the adenovirus fiber shaft forms amyloid‐type fibrils

FEBS Letters

Arlaud, Gérard⁴  Mitraki, Anna⁴  Ruigrok, Rob W.H.³  Hernandez, Jean-François⁴  Forsyth, V.Trevor¹  Luckey, Mary² 

[1] Physics Department, Keele University, Staffordshire ST5 5BG, UK;Department of Chemistry and Biochemistry, San Francisco State University, 1600 Holloway avenue, 94132 San Francisco, CA, USA;European Molecular Biology Laboratory, Grenoble Outstation, c/o Institut Laue-Langevin, 6 rue Jules Horowitz, BP 156, 38042 Grenoble Cedex 9, France;Institut de Biologie Structurale, 41 rue Jules Horowitz, 38027 Grenoble Cedex 1, France

关键词: Adenovirus;    Amyloid fibril;    Electron microscopy;    Congo red;    X-ray diffraction;    Boc;    tert-butyloxycarbonyl;    HPLC;    high performance liquid chromatography;    GdnHCl;    guanidine hydrochloride;    HAd2;    human adenovirus serotype 2;    SDS;    sodium dodecyl sulfate;   

DOI  :  10.1016/S0014-5793(00)01184-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The fiber protein of adenovirus consists of a C-terminal globular head, a shaft and a short N-terminal tail. The crystal structure of a stable domain comprising the head plus a part of the shaft of human adenovirus type 2 fiber has recently been solved at 2.4 Å resolution [van Raaij et al. (1999) Nature 401, 935–938]. A peptide corresponding to the portion of the shaft immediately adjacent to the head (residues 355–396) has been synthesized chemically. The peptide failed to assemble correctly and instead formed amyloid-type fibrils as assessed by electron microscopy, Congo red binding and X-ray diffraction. Peptides corresponding to the fiber shaft could provide a model system to study mechanisms of amyloid fibril formation.

【 授权许可】

Unknown