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. © 2014 S. Karger AG, Basel.