Appearance of the bona fide spiral tubule of ORF virus is dependent on an intact 10-kilodalton viral protein.

Abstract:

:Parapoxviruses can be morphologically distinguished from other poxviruses in conventional negative staining electron microscopy (EM) by their ovoid appearance and the spiral tubule surrounding the virion's surface. However, this technique may introduce artifacts. We have examined Orf virus (ORFV; the prototype species of the Parapoxvirus genus) by cryoelectron microscopy (cryo-EM) and cryo-negative staining EM. From these studies we suggest that the shape and unique spiral tubule are authentic features of the parapoxviruses. We also constructed an ORFV mutant deleted of a gene encoding a 10-kDa protein, which is an orthologue of the vaccinia virus (VACV) 14-kDa fusion protein, and investigated its ultrastructure. This mutant virus multiplied slowly in permissive cells and produced infectious but morphologically aberrant particles. Mutant virions lacked the spiral tubule but displayed short disorganized tubules similar to those observed on the surface of VACV. In addition, thin extensions or loop-like structures were appended to the ORFV mutant particles. We suggest that these appended structures arise from a failure of the mutant virus particles to properly seal and that the sealing activity is dependent on the 10-kDa protein.

journal_name

J Virol

journal_title

Journal of virology

authors

Spehner D,De Carlo S,Drillien R,Weiland F,Mildner K,Hanau D,Rziha HJ

doi

10.1128/JVI.78.15.8085-8093.2004

subject

Has Abstract

pub_date

2004-08-01 00:00:00

pages

8085-93

issue

15

eissn

0022-538X

issn

1098-5514

pii

78/15/8085

journal_volume

78

pub_type

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