Mass Spectrometry-Based Characterization of the Virion Proteome, Phosphoproteome, and Associated Kinase Activity of Human Cytomegalovirus.
Human cytomegalovirus
mass spectrometry-based proteomics
phosphorylation
proteins
virion composition
virion-associated kinase
Journal
Microorganisms
ISSN: 2076-2607
Titre abrégé: Microorganisms
Pays: Switzerland
ID NLM: 101625893
Informations de publication
Date de publication:
30 May 2020
30 May 2020
Historique:
received:
05
05
2020
revised:
28
05
2020
accepted:
28
05
2020
entrez:
4
6
2020
pubmed:
4
6
2020
medline:
4
6
2020
Statut:
epublish
Résumé
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.
Identifiants
pubmed: 32486127
pii: microorganisms8060820
doi: 10.3390/microorganisms8060820
pmc: PMC7357008
pii:
doi:
Types de publication
Journal Article
Review
Langues
eng
Subventions
Organisme : Deutsche Forschungsgemeinschaft
ID : PL236/7-1
Organisme : Deutsche Forschungsgemeinschaft
ID : ZI1810/1-1
Organisme : Deutsche Forschungsgemeinschaft
ID : MA1289/8-1
Organisme : Else Kröner Fresenius Stiftung
ID : 2013_A203
Organisme : Interdisciplinary Center of Clinical Research of the Hospital/Universitätsklinikum Erlangen
ID : IZKF project A88
Organisme : Agence Nationale de la Recherche
ID : ANR-10-INBS-08-01
Déclaration de conflit d'intérêts
The authors declare no conflict of interest.
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