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Vaccinia Virus Proteome: Identification of Proteins in Vaccinia Virus Intracellular Mature Virion Particles

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TLDR
This study provides the first comprehensive structural analysis of the infectious vaccinia virus IMV, showing that it contains 75 viral proteins, including structural proteins, enzymes, transcription factors, and predicted viral proteins not known to be expressed or present in the IMV.
Abstract
Vaccinia virus is a large enveloped poxvirus with more than 200 genes in its genome. Although many poxvirus genomes have been sequenced, knowledge of the host and viral protein components of the virions remains incomplete. In this study, we used gel-free liquid chromatography and tandem mass spectroscopy to identify the viral and host proteins in purified vaccinia intracellular mature virions (IMV). Analysis of the proteins in the IMV showed that it contains 75 viral proteins, including structural proteins, enzymes, transcription factors, and predicted viral proteins not known to be expressed or present in the IMV. We also determined the relative abundances of the individual protein components in the IMV. Finally, 23 IMV-associated host proteins were also identified. This study provides the first comprehensive structural analysis of the infectious vaccinia virus IMV.

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Citations
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Journal ArticleDOI

Less label, more free: approaches in label-free quantitative mass spectrometry.

TL;DR: In this review, techniques, software, and statistical analyses used in label‐free quantitative proteomics studies for area under the curve and spectral counting approaches are examined and it is concluded that label‐ free quantitative proteochemistry is a reliable, versatile, and cost‐effective alternative to labelled quantitation.
Book ChapterDOI

In a nutshell: structure and assembly of the vaccinia virion.

TL;DR: This review summarizes significant advances in poxvirus genetics and molecular biology during the past 15 years and attempts to assemble them into a comprehensible and thoughtful picture of poxVirus structure and assembly.
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Cellular proteins in influenza virus particles.

TL;DR: The identification of cellular constituents of influenza virions has important implications for understanding the interactions of influenza virus with its host and brings us a step closer to defining the cellular requirements for influenza virus replication.
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A Proteomic Atlas of the African Swine Fever Virus Particle.

TL;DR: A comprehensive model of the ASFV architecture is provided that integrates both compositional and structural information and strongly supports the suggestion that these host membrane-associated proteins are recruited during virus budding at actin-dependent membrane protrusions.
References
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Journal ArticleDOI

A simple method for displaying the hydropathic character of a protein

TL;DR: A computer program that progressively evaluates the hydrophilicity and hydrophobicity of a protein along its amino acid sequence has been devised and its simplicity and its graphic nature make it a very useful tool for the evaluation of protein structures.
Journal ArticleDOI

Probability-based protein identification by searching sequence databases using mass spectrometry data.

TL;DR: A new computer program, Mascot, is presented, which integrates all three types of search for protein identification by searching a sequence database using mass spectrometry data, and the scoring algorithm is probability based.
Journal ArticleDOI

Large-scale analysis of the yeast proteome by multidimensional protein identification technology.

TL;DR: MudPIT was applied to the proteome of the Saccharomyces cerevisiae strain BJ5460 grown to mid-log phase and yielded the largest proteome analysis to date, identifying 131 proteins with three or more predicted transmembrane domains which allowed us to map the soluble domains of many of the integral membrane proteins.
Journal ArticleDOI

Proteomics to study genes and genomes

TL;DR: Proteomics can be divided into three main areas: protein micro-characterization for large-scale identification of proteins and their post-translational modifications; ‘differential display’ proteomics for comparison of protein levels with potential application in a wide range of diseases; and studies of protein–protein interactions using techniques such as mass spectrometry or the yeast two-hybrid system.
Journal ArticleDOI

Exponentially Modified Protein Abundance Index (emPAI) for Estimation of Absolute Protein Amount in Proteomics by the Number of Sequenced Peptides per Protein

TL;DR: It is reported that PAI values obtained at different concentrations of serum albumin show a linear relationship with the logarithm of protein concentration in LC-MS/MS experiments, and the values of emPAI are suggested that they should be reported in large scale proteomic identification projects.
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