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

FEBS Lett. 2000 Feb 18;468(1):23-7. doi: 10.1016/s0014-5793(00)01184-4.

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 A 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenoviruses, Human / chemistry*
  • Amino Acid Sequence
  • Amyloid / chemistry*
  • Amyloid / ultrastructure
  • Birefringence
  • Capsid / chemistry*
  • Capsid Proteins*
  • Coloring Agents / metabolism
  • Congo Red / metabolism
  • Microscopy, Electron
  • Models, Chemical
  • Molecular Sequence Data
  • Peptide Fragments / chemical synthesis
  • Peptide Fragments / chemistry*
  • Peptide Fragments / metabolism
  • Peptide Fragments / ultrastructure
  • Protein Binding
  • X-Ray Diffraction

Substances

  • Amyloid
  • Capsid Proteins
  • Coloring Agents
  • Peptide Fragments
  • hexon capsid protein, Adenovirus
  • Congo Red