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A peptide from the adenovirus fiber shaft forms amyloid-type fibrils
M Luckey1, J Hernandez, G Arlaud
1Department of Chemistry, San Francisco State University, 1600 Holloway avenue, 94132, San Francisco, CA, USA.
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.
Insights
Synthesized adenovirus fiber shaft peptides unexpectedly formed amyloid-type fibrils. This finding suggests these peptides could serve as a model system for studying amyloid fibril formation mechanisms.
Area of Science:
- Structural biology
- Biochemistry
- Virology
Background:
- Adenovirus fiber protein structure includes a globular head, shaft, and tail.
- The crystal structure of a human adenovirus type 2 fiber head-shaft domain is known.
- The specific assembly properties of the fiber shaft are not well understood.
Purpose of the Study:
- To investigate the assembly properties of a synthesized peptide corresponding to the adenovirus fiber shaft.
- To determine if adenovirus fiber shaft peptides can form ordered structures.
Main Methods:
- Chemical synthesis of a peptide (residues 355-396) from the human adenovirus type 2 fiber shaft.
- Assessment of peptide assembly using electron microscopy.
- Analysis of fibril formation via Congo red binding and X-ray diffraction.
Main Results:
- The synthesized peptide failed to assemble into its native structure.
- The peptide spontaneously formed amyloid-type fibrils.
- Characterization confirmed the fibrillar nature of the aggregates.
Conclusions:
- The adenovirus fiber shaft contains sequences prone to forming amyloid-type structures.
- Adenovirus fiber shaft peptides represent a novel model system for studying amyloidogenesis.
- Further research can elucidate the mechanisms underlying this fibril formation.