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

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 omega virus (NomegaV), 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 NomegaV 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 A 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 NomegaV, was developed to initiate the structure solution of PrV.

journal_name

Arch Virol

journal_title

Archives of virology

authors

Taylor DJ,Speir JA,Reddy V,Cingolani G,Pringle FM,Ball LA,Johnson JE

doi

10.1007/s00705-005-0637-3

keywords:

subject

Has Abstract

pub_date

2006-01-01 00:00:00

pages

155-65

issue

1

eissn

0304-8608

issn

1432-8798

journal_volume

151

pub_type

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