Skip to main content
U.S. Department of Energy
Office of Scientific and Technical Information

Hydroxyproline in the major capsid protein VP1 of polyomavirus

Journal Article · · J. Virol.; (United States)
OSTI ID:6156449

Amino acid analysis of (/sup 3/H)proline-labeled polyomavirus major capsid protein VP1 by two-dimensional paper chromatography of the acid-hydrolyzed protein revealed the presence of /sup 3/H-labeled hydroxyproline. Addition of the proline analog L-azetidine-2-carboxylic acid to infected mouse kidney cell cultures prevented or greatly reduced hydroxylation of proline in VP1. Immunofluorescence analysis performed on infected cells over a time course of analog addition revealed that virus proteins were synthesized but that transport from the cytoplasm to the nucleus was impeded. A reduction in the assembly of progeny virions demonstrated by CsCl gradient purification of virus from (/sup 35/S)methionine-labeled infected cell cultures was found to correlate with the time of analog addition. These results suggest that incorporation of this proline analog into VP1, accompanied by reduction of the hydroxyproline content of the protein, influences the amount of virus progeny produced by affecting transport of VP1 to the cell nucleus for assembly into virus particles.

Research Organization:
Kansas State Univ., Manhattan (USA)
OSTI ID:
6156449
Journal Information:
J. Virol.; (United States), Journal Name: J. Virol.; (United States) Vol. 63:6; ISSN JOVIA
Country of Publication:
United States
Language:
English