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Structural stability of adenovirus type 5
Jason Rexroad1, Christopher M Wiethoff, Anthony P Green
1Department of Pharmaceutical Chemistry, University of Kansas, 2095 Constant Ave., Lawrence, KS 66047, USA.
Journal of Pharmaceutical Sciences
|February 15, 2003
Summary
Adenovirus type 5 (Ad) undergoes structural changes and disassembly at 45°C in 2% sucrose. Higher sucrose concentrations stabilize viral proteins but do not prevent capsid disassembly.
Area of Science:
- Biophysics
- Structural Biology
- Virology
Background:
- Adenovirus type 5 (Ad) is a common human pathogen.
- Understanding Ad stability is crucial for developing antiviral therapies and gene delivery vectors.
Purpose of the Study:
- To investigate thermally induced structural changes in adenovirus type 5 (Ad).
- To determine the effect of sucrose concentration on Ad thermal stability.
Main Methods:
- Biophysical techniques including tryptophan fluorescence, UV absorption spectroscopy, circular dichroism (CD), dynamic and static light scattering.
- Transmission electron microscopy (TEM) and SDS-PAGE.
- Differential scanning calorimetry (DSC).
Main Results:
- A cooperative structural transition and partial disassembly of Ad occurred at 45°C in 2% sucrose, increasing viral DNA accessibility.
- Penton base (protein III) and protein IIIa were identified as labile capsid proteins initiating disassembly.
- Higher temperatures induced DNA rearrangements, detected by CD spectra and decreased DNA accessibility.
- 10% sucrose stabilized viral proteins but did not prevent capsid quaternary structure loss at 45°C.
Conclusions:
- Adenovirus type 5 undergoes significant thermal-induced structural transitions and disassembly around 45°C.
- Sucrose concentration influences Ad stability, with higher concentrations offering partial stabilization.
- Specific viral proteins are more susceptible to thermal denaturation, initiating the disassembly process.