ArticleBiophysical journal2007
Two-color fluorescence analysis of individual virions determines the distribution of the copy number of proteins in herpes simplex virus particles.
Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 20 citations in OpenAlex.
- A Viral Mutation Profiling and Discovery Strategy for Sensitive Multiplex Detection of Viruses and Variants in Saliva by Proteomics.bioRxiv : the preprint server for biology · 2026Article
- A molecular mechanism for probabilistic bet hedging and its role in viral latency.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Quantitative Evaluation of Protein Heterogeneity within Herpes Simplex Virus 1 Particles.Journal of virology · 2017Article
- A single gD glycoprotein can mediate infection by Herpes simplex virus.Journal of the American Chemical Society · 2013Article
- Differential protein partitioning within the herpesvirus tegument and envelope underlies a complex and variable virion architecture.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- From target selection to the minimum acceptable biological effect level for human study: use of mechanism-based PK/PD modeling to design safe and efficacious biologics.The AAPS journal · 2011Article
- Mechanisms of receptor/coreceptor-mediated entry of enveloped viruses.Biophysical journal · 2009Article
- Differing roles of inner tegument proteins pUL36 and pUL37 during entry of herpes simplex virus type 1.Journal of virology · 2009Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 3 countries.
Funding
Abstract
We present a single virion method to determine absolute distributions of copy number in the protein composition of viruses and apply it to herpes simplex virus type 1. Using two-color coincidence fluorescence spectroscopy, we determine the virion-to-virion variability in copy numbers of fluorescently labeled tegument and envelope proteins relative to a capsid protein by analyzing fluorescence intensity ratios for ensembles of individual dual-labeled virions and fitting the resulting histogram of ratios. Using EYFP-tagged capsid protein VP26 as a reference for fluorescence intensity, we are able to calculate the mean and also, for the first time to our knowledge, the variation in numbers of gD, VP16, and VP22 tegument. The measurement of the number of glycoprotein D molecules was in good agreement with independent measurements of average numbers of these glycoproteins in bulk virus preparations, validating the method. The accuracy, straightforward data processing, and high throughput of this technique make it widely applicable to the analysis of the molecular composition of large complexes in general, and it is particularly suited to providing insights into virus structure, assembly, and infectivity.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.