Mass Spectrometry-Based Characterization of the Virion Proteome, Phosphoproteome, and Associated Kinase Activity of Human Cytomegalovirus
The assembly of human cytomegalovirus (HCMV) virions is an orchestrated process that requires, as an essential prerequisite, the complex crosstalk between viral structural proteins. Currently, however, the mechanisms governing the successive steps in the constitution of virion protein complexes rema...
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| Format: | Article |
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MDPI AG
2020-05-01
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| Series: | Microorganisms |
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| Online Access: | https://www.mdpi.com/2076-2607/8/6/820 |
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| author | Yohann Couté Alexandra Kraut Christine Zimmermann Nicole Büscher Anne-Marie Hesse Christophe Bruley Marco De Andrea Christina Wangen Friedrich Hahn Manfred Marschall Bodo Plachter |
| author_facet | Yohann Couté Alexandra Kraut Christine Zimmermann Nicole Büscher Anne-Marie Hesse Christophe Bruley Marco De Andrea Christina Wangen Friedrich Hahn Manfred Marschall Bodo Plachter |
| author_sort | Yohann Couté |
| collection | DOAJ |
| description | The assembly of human cytomegalovirus (HCMV) virions is an orchestrated process that requires, as an essential prerequisite, the complex crosstalk between viral structural proteins. Currently, however, the mechanisms governing the successive steps in the constitution of virion protein complexes remain elusive. Protein phosphorylation is a key regulator determining the sequential changes in the conformation, binding, dynamics, and stability of proteins in the course of multiprotein assembly. In this review, we present a comprehensive map of the HCMV virion proteome, including a refined view on the virion phosphoproteome, based on previous publications supplemented by new results. Thus, a novel dataset of viral and cellular proteins contained in HCMV virions is generated, providing a basis for future analyses of individual phosphorylation steps and sites involved in the orchestrated assembly of HCMV virion-specific multiprotein complexes. Finally, we present the current knowledge on the activity of pUL97, the HCMV-encoded and virion-associated kinase, in phosphorylating viral and host proteins. |
| first_indexed | 2024-03-10T19:29:17Z |
| format | Article |
| id | doaj.art-033374bdb6c744bdbbd9566fd3bbcb9b |
| institution | Directory Open Access Journal |
| issn | 2076-2607 |
| language | English |
| last_indexed | 2024-03-10T19:29:17Z |
| publishDate | 2020-05-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Microorganisms |
| spelling | doaj.art-033374bdb6c744bdbbd9566fd3bbcb9b2023-11-20T02:15:06ZengMDPI AGMicroorganisms2076-26072020-05-018682010.3390/microorganisms8060820Mass Spectrometry-Based Characterization of the Virion Proteome, Phosphoproteome, and Associated Kinase Activity of Human CytomegalovirusYohann Couté0Alexandra Kraut1Christine Zimmermann2Nicole Büscher3Anne-Marie Hesse4Christophe Bruley5Marco De Andrea6Christina Wangen7Friedrich Hahn8Manfred Marschall9Bodo Plachter10University Grenoble Alpes, CEA, Inserm, BIG-BGE, 38000 Grenoble, FranceUniversity Grenoble Alpes, CEA, Inserm, BIG-BGE, 38000 Grenoble, FranceInstitute for Virology and Forschungszentrum für Immuntherapie, University Medical Center of the Johannes Gutenberg-University Mainz, Obere Zahlbacher Str. 67, D-55131 Mainz, GermanyInstitute for Virology and Forschungszentrum für Immuntherapie, University Medical Center of the Johannes Gutenberg-University Mainz, Obere Zahlbacher Str. 67, D-55131 Mainz, GermanyUniversity Grenoble Alpes, CEA, Inserm, BIG-BGE, 38000 Grenoble, FranceUniversity Grenoble Alpes, CEA, Inserm, BIG-BGE, 38000 Grenoble, FranceDepartment of Public Health and Pediatric Sciences, Turin Medical School, University of Turin, 10126 Turin, and CAAD – Center for Translational Research on Autoimmune and Allergic Disease, Novara Medical School, 28100 Novara, ItalyInstitute for Clinical and Molecular Virology, Friedrich-Alexander University of Erlangen-Nürnberg (FAU), 91054 Erlangen, GermanyInstitute for Clinical and Molecular Virology, Friedrich-Alexander University of Erlangen-Nürnberg (FAU), 91054 Erlangen, GermanyInstitute for Clinical and Molecular Virology, Friedrich-Alexander University of Erlangen-Nürnberg (FAU), 91054 Erlangen, GermanyInstitute for Virology and Forschungszentrum für Immuntherapie, University Medical Center of the Johannes Gutenberg-University Mainz, Obere Zahlbacher Str. 67, D-55131 Mainz, GermanyThe assembly of human cytomegalovirus (HCMV) virions is an orchestrated process that requires, as an essential prerequisite, the complex crosstalk between viral structural proteins. Currently, however, the mechanisms governing the successive steps in the constitution of virion protein complexes remain elusive. Protein phosphorylation is a key regulator determining the sequential changes in the conformation, binding, dynamics, and stability of proteins in the course of multiprotein assembly. In this review, we present a comprehensive map of the HCMV virion proteome, including a refined view on the virion phosphoproteome, based on previous publications supplemented by new results. Thus, a novel dataset of viral and cellular proteins contained in HCMV virions is generated, providing a basis for future analyses of individual phosphorylation steps and sites involved in the orchestrated assembly of HCMV virion-specific multiprotein complexes. Finally, we present the current knowledge on the activity of pUL97, the HCMV-encoded and virion-associated kinase, in phosphorylating viral and host proteins.https://www.mdpi.com/2076-2607/8/6/820human cytomegalovirusvirion compositionproteinsphosphorylationvirion-associated kinasemass spectrometry-based proteomics |
| spellingShingle | Yohann Couté Alexandra Kraut Christine Zimmermann Nicole Büscher Anne-Marie Hesse Christophe Bruley Marco De Andrea Christina Wangen Friedrich Hahn Manfred Marschall Bodo Plachter Mass Spectrometry-Based Characterization of the Virion Proteome, Phosphoproteome, and Associated Kinase Activity of Human Cytomegalovirus Microorganisms human cytomegalovirus virion composition proteins phosphorylation virion-associated kinase mass spectrometry-based proteomics |
| title | Mass Spectrometry-Based Characterization of the Virion Proteome, Phosphoproteome, and Associated Kinase Activity of Human Cytomegalovirus |
| title_full | Mass Spectrometry-Based Characterization of the Virion Proteome, Phosphoproteome, and Associated Kinase Activity of Human Cytomegalovirus |
| title_fullStr | Mass Spectrometry-Based Characterization of the Virion Proteome, Phosphoproteome, and Associated Kinase Activity of Human Cytomegalovirus |
| title_full_unstemmed | Mass Spectrometry-Based Characterization of the Virion Proteome, Phosphoproteome, and Associated Kinase Activity of Human Cytomegalovirus |
| title_short | Mass Spectrometry-Based Characterization of the Virion Proteome, Phosphoproteome, and Associated Kinase Activity of Human Cytomegalovirus |
| title_sort | mass spectrometry based characterization of the virion proteome phosphoproteome and associated kinase activity of human cytomegalovirus |
| topic | human cytomegalovirus virion composition proteins phosphorylation virion-associated kinase mass spectrometry-based proteomics |
| url | https://www.mdpi.com/2076-2607/8/6/820 |
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