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


ABSTRACT: 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.Transmission electron microscopy (TEM) of recombinant varicella-zoster virus pORF54 was performed.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.These morphological features are consistent with those previously reported for other herpesvirus and bacteriophage portal proteins.

SUBMITTER: Visalli RJ 

PROVIDER: S-EPMC4477527 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature

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

Visalli Robert J RJ   Howard Alexander J AJ  

Intervirology 20140314 2


<h4>Background</h4>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.<h4>Methods</h4>Transmission electron microscopy (TEM) of recombinant varicella-zoster virus pORF54 was performed.<h4>Results</h4>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 distinguish  ...[more]

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