Preliminary x-ray characterization of authentic providence virus and attempts to express its coat protein gene in recombinant baculovirus

Preliminary x-ray characterization of authentic providence virus and attempts to express its coat... Providence Virus (PrV) is a non-envoloped, T = 4 icosahedral beta-tetravirus that undergoes autocatalytic cleavage of its coat protein precursor after capsid assembly. This is also a well characterized function of Nudaurelia capensis ω virus (NωV), a member of the related omegatetraviruses, whose x-ray structure has been determined. Virus-like particle (VLP) production of PrV in a recombinant baculovirus expression system was attempted to obtain high VLP yields for comparison of structural and autocatalytic active site properties between these virus groups. This resulted in insoluble aggregates of PrV coat protein even though NωV VLPs have been successfully produced in the same system. Betatetraviruses may be more dependent on compartmentalization and availability of their full-length genome for proper folding and assembly. However, crystals were grown of limited quantities of authentic PrV produced in cell culture and a partial X-ray data set collected to 3.8 Å resolution. The virus particle position and orientation in the unit cell was determined by space group consideration and rotation function analysis. A phasing model, based on NωV, was developed to initiate the structure solution of PrV. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Archives of Virology Springer Journals

Preliminary x-ray characterization of authentic providence virus and attempts to express its coat protein gene in recombinant baculovirus

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Publisher
Springer Journals
Copyright
Copyright © 2006 by Springer-Verlag/Wien
Subject
Biomedicine; Medical Microbiology; Infectious Diseases; Virology
ISSN
0304-8608
eISSN
1432-8798
D.O.I.
10.1007/s00705-005-0637-3
Publisher site
See Article on Publisher Site

Abstract

Providence Virus (PrV) is a non-envoloped, T = 4 icosahedral beta-tetravirus that undergoes autocatalytic cleavage of its coat protein precursor after capsid assembly. This is also a well characterized function of Nudaurelia capensis ω virus (NωV), a member of the related omegatetraviruses, whose x-ray structure has been determined. Virus-like particle (VLP) production of PrV in a recombinant baculovirus expression system was attempted to obtain high VLP yields for comparison of structural and autocatalytic active site properties between these virus groups. This resulted in insoluble aggregates of PrV coat protein even though NωV VLPs have been successfully produced in the same system. Betatetraviruses may be more dependent on compartmentalization and availability of their full-length genome for proper folding and assembly. However, crystals were grown of limited quantities of authentic PrV produced in cell culture and a partial X-ray data set collected to 3.8 Å resolution. The virus particle position and orientation in the unit cell was determined by space group consideration and rotation function analysis. A phasing model, based on NωV, was developed to initiate the structure solution of PrV.

Journal

Archives of VirologySpringer Journals

Published: Jan 1, 2006

References

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