Mass spectrometry-based characterization of the virion proteome and phosphoproteome of human cytomegalovirus

ABSTRACT: The assembly of human cytomegalovirus (HCMV) virions is an orchestrated process that requires, as an essential prerequisite, the complex crosstalk between viral structural proteins. So far, however, the mechanisms governing the successive steps in the constitution of virion protein complexes remained elusive. Protein phosphorylation is a key regulator determining the sequential changes in conformation, binding, dynamics and stability of proteins in the course of multiprotein assembly. Here, we present new results to complete knowledge on HCMV virion proteome and phosphoproteome. Thus, a novel dataset of viral and cellular proteins contained in HCMV virions has been generated, providing a basis for future analyses of individual phosphorylation steps and sites involved in the orchestrated assembly of HCMV virion-specific multiprotein complexes.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human) Human Cytomegalovirus (strain Ad169) (hhv-5) (human Herpesvirus 5)

SUBMITTER: Yohann Couté  

LAB HEAD: Virginie Brun

PROVIDER: PXD012921 | Pride | 2020-06-05

REPOSITORIES: Pride