title: 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.
  
  
  CONCLUSIONS
  These morphological features are consistent with those previously reported for other herpesvirus and bacteriophage portal proteins.
authors.affiliation: Department of Biomedical Sciences, Mercer University School of Medicine, Savannah, Ga., USA.
authors.forename: Robert J
authors.initials: RJ
authors.lastname: Visalli
authors.forename: Alexander J
authors.initials: AJ
authors.lastname: Howard
mesh_terms: D014645:Herpesvirus 3, Human / Q000378:metabolism / Q000648:ultrastructure*; D046529:Microscopy, Electron, Transmission; D011487:Protein Conformation; D055503:Protein Multimerization; D014764:Viral Proteins / Q000378:metabolism / Q000648:ultrastructure*
chemical_list: D014764:Viral Proteins