期刊
NATURE COMMUNICATIONS
卷 6, 期 -, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/ncomms6980
关键词
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资金
- Leverhulme Trust [RPG-2012-793]
- Royal Society (University Research Fellowship)
- Engineering and Physical Sciences Research Council, UK [EP/H018301/1]
- Medical Research Council [MR/K015850/1]
- Alzheimers Research UK [ARUK-PG2013-14] Funding Source: researchfish
- Engineering and Physical Sciences Research Council [EP/H018301/1] Funding Source: researchfish
- Medical Research Council [MR/K02292X/1] Funding Source: researchfish
- EPSRC [EP/H018301/1] Funding Source: UKRI
- MRC [MR/K015850/1, MR/K02292X/1] Funding Source: UKRI
Herpes simplex virus type-1 (HSV-1) is one of the most widespread pathogens among humans. Although the structure of HSV-1 has been extensively investigated, the precise organization of tegument and envelope proteins remains elusive. Here we use super-resolution imaging by direct stochastic optical reconstruction microscopy (dSTORM) in combination with a model-based analysis of single-molecule localization data, to determine the position of protein layers within virus particles. We resolve different protein layers within individual HSV-1 particles using multi-colour dSTORM imaging and discriminate envelope-anchored glycoproteins from tegument proteins, both in purified virions and in virions present in infected cells. Precise characterization of HSV-1 structure was achieved by particle averaging of purified viruses and model-based analysis of the radial distribution of the tegument proteins VP16, VP1/2 and pUL37, and envelope protein gD. From this data, we propose a model of the protein organization inside the tegument.
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