Hydroxyproline in the major capsid protein VP1 of polyomavirus.

Abstract:

:Amino acid analysis of [3H]proline-labeled polyomavirus major capsid protein VP1 by two-dimensional paper chromatography of the acid-hydrolyzed protein revealed the presence of 3H-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 [35S]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.

journal_name

J Virol

journal_title

Journal of virology

authors

Ludlow JW,Consigli RA

doi

10.1128/JVI.63.6.2881-2884.1989

subject

Has Abstract

pub_date

1989-06-01 00:00:00

pages

2881-4

issue

6

eissn

0022-538X

issn

1098-5514

journal_volume

63

pub_type

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