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

Abstract

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.