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Comparative Proteomics of Human Monkeypox and Vaccinia Intracellular Mature and Extracellular Enveloped Virions
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Orthopoxviruses are among the largest and most complex of the animal viruses. In response to the recent emergence of monkeypox in Africa and the threat of smallpox bioterrorism, two orthopoxviruses with different pathogenic potentials, human monkeypox virus and vaccinia virus, were proteomically compared with the goal of identifying proteins required for pathogenesis. Orthopoxviruses were grown in HeLa cells to two different viral forms (intracellular mature virus and extracellular enveloped virus), purified by sucrose gradient ultracentrifugation, denatured using RapiGest surfactant, and digested with trypsin. Unfractionated samples and strong cation exchange HPLC fractions were analyzed by high-resolution reversed-phase nano-LC-MS/MS, and analyses of the MS/MS spectra using SEQUEST and X! Tandem resulted in the confident identification of hundreds of monkeypox, vaccinia, and copurified host-cell proteins. The unfractionated samples were additionally analyzed by LC-MS using an LTQ-Orbitrap, and the accurate mass and elution time tag approach was used to perform quantitative comparisons. Possible pathophysiological roles of differentially abundant Orthopoxvirus proteins are discussed. Data, processed results, and protocols are available at http://www.proteomicsresource.org/.
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Most virion compositional mass spectrometry studies have focused on viruses with high proteomic complexity, including Herpesviridae and Poxviridae.
“For compositional analysis, most studies have focused on viruses with high proteomic complexity, including those in the families Herpesviridae (4–9) and Poxviridae (10–12).”
From The Impact of Mass Spectrometry–Based Proteomics on Fundamental Discoveries in Virology (2014) · cites this paper as [11]
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Metadata
- Authors
- Manes, N. P., Estep, R. D., Mottaz, H. M., Moore, R. J., Clauss, T. R. W., Monroe, M. E., Du, X., Adkins, J. N., Wong, S. W., & Smith, R. D.
- Affiliations
- Pacific Northwest National Laboratory (US)
- Corresponding author
- Smith, Richard D.
- ORCID
- Venue
- Journal of Proteome Research
- Publisher
- American Chemical Society (ACS)
- Published
- 2008-01-19
- Volume
- 7
- Issue
- 3
- Pages
- 960-968
- ISSN
- 1535-3893 (ISSN-L)
- 1535-3907
- PMC
- PMC2517256
- OpenAlex
- W2085841863
- Cited by
- 103
- References
- 54
- Citations by year
- 2026: 6 · 2025: 4 · 2024: 14 · 2023: 17 · 2022: 11 · 2021: 1 · 2020: 1 · 2019: 2 · 2018: 1 · 2017: 2 · 2016: 1 · 2015: 1 · 2014: 7 · 2013: 3 · 2012: 3
- FWCI
- 3.14
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Journal of Proteome Research (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute of Allergy and Infectious Diseases (Y1 AI 489401)
- National Center for Research Resources (RR18 522, P41RR018522)
- Topics
- Life Sciences › Immunology and Microbiology › Virology › Poxvirus research and outbreaks
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › vaccines and immunoinformatics approaches
- Keywords
- monkeypox virus, vaccinia virus, orthopoxvirus, intracellular mature virus, extracellular enveloped virus, viral proteome, host-virus interaction, pathogenesis, HeLa cells, quantitative proteomics, mass spectrometry
- MeSH terms
- Chromatography, High Pressure Liquid, Chromatography, Liquid, Electrophoresis, Polyacrylamide Gel, Monkeypox virus, Vaccinia virus, Virion, Proteomics, Tandem Mass Spectrometry
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