Supplementary Material for: Non-Axial View of the Varicella-Zoster Virus Portal Protein Reveals Conserved Crown, Wing and Clip Architecture

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.背景：疱疹病毒科（Herpesviridae）编码一类蛋白质同源物，此类蛋白在病毒衣壳化过程中，充当将病毒DNA插入预组装衣壳的"入口位点"。方法：针对重组水痘带状疱疹病毒pORF54开展透射电子显微镜（Transmission electron microscopy, TEM）检测。结果：结果表明，pORF54可与自身形成高阶多聚结构。经透射电子显微镜分析的富集组分中，可见非轴向取向的门户结构，该结构具备明确的中央通道，且可清晰区分冠部、翼部与夹部区域。结论：上述形态学特征与此前报道的其他疱疹病毒及噬菌体门户蛋白的特征相符。