Non-axial view of the varicella-zoster virus portal protein reveals conserved crown, wing and clip architecture.

Abstract:

BACKGROUND:Herpesviridae encode a family of protein homologues that function as the 'port of entry' for insertion of the viral DNA into preformed capsids during encapsidation. METHODS:Transmission electron microscopy (TEM) of recombinant varicella-zoster virus pORF54 was performed. RESULTS:Results suggest that pORF54 forms higher-order structures with itself. Enriched fractions analyzed by TEM revealed non-axial oriented portals with defined central channels and distinguishable crown, wing and clip regions. CONCLUSION:These morphological features are consistent with those previously reported for other herpesvirus and bacteriophage portal proteins.

journal_name

Intervirology

journal_title

Intervirology

authors

Visalli RJ,Howard AJ

doi

10.1159/000360225

subject

Has Abstract

pub_date

2014-01-01 00:00:00

pages

121-5

issue

2

eissn

0300-5526

issn

1423-0100

pii

000360225

journal_volume

57

pub_type

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