Couté Y, Kraut A, Zimmermann C, Büscher N, Hesse AM, Bruley C, De Andrea M, Wangen C, Hahn F, Marschall M, Plachter B (2020)
Publication Type: Journal article, Review article
Publication year: 2020
Book Volume: 8
Article Number: 820
Journal Issue: 6
DOI: 10.3390/microorganisms8060820
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.
APA:
Couté, Y., Kraut, A., Zimmermann, C., Büscher, N., Hesse, A.M., Bruley, C.,... Plachter, B. (2020). Mass spectrometry-based characterization of the virion proteome, phosphoproteome, and associated kinase activity of human cytomegalovirus. Microorganisms, 8(6). https://doi.org/10.3390/microorganisms8060820
MLA:
Couté, Yohann, et al. "Mass spectrometry-based characterization of the virion proteome, phosphoproteome, and associated kinase activity of human cytomegalovirus." Microorganisms 8.6 (2020).
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