Intervirology · 2014
Non-axial view of the varicella-zoster virus portal protein reveals conserved crown, wing and clip architecture.
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Visalli Robert J, Howard Alexander J
Аннотация
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.
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.