PXD006159

PXD006159 is an original dataset announced via ProteomeXchange.

Title	Phosphorylation coexists with O-GlcNAcylation in a plant virus protein and shapes viral infection
Description	Phosphorylation and O-GlcNAcylation are two widespread post-translational modifications (PTM) often affecting the same eukaryotic target protein. Plum pox virus (PPV) is a member of the genus Potyvirus that infects a wide range of plant species. O-GlcNAcylation of the capsid protein (CP) of PPV has been extensively studied, and some evidence about CP phosphorylation has been additionally reported. Here, we made use of proteomics analyses to demonstrate that PPV CP is phosphorylated in vivo at its N-terminal region. In contrast with the classical “Yin-Yang” mechanism that applies to some mammalian proteins, PPV CP phosphorylation affects residues different from the O-GlcNAcylated ones (serines Ser-25, Ser-81, Ser-101 and Ser-118). Our findings show that PPV CP can be concurrently phosphorylated and O-GlcNAcylated at nearby residues. However, an analysis using a differential proteomics strategy based on iTRAQ (Isobaric Tags for Relative and Absolute Quantitation) showed a significant enhancement of phosphorylation at Ser-25 in virions recovered from O-GlcNAcylation-deficient plants, which uncovers the existence of some cross-talk between O-GlcNAcylation and phosphorylation in PPV-CP. Whereas precluding phosphorylation at the four identified phosphotarget sites only had a limited impact in viral infection, mimicking phosphorylation prevents PPV infection in Prunus persica and weakens infection in Nicotiana benthamiana and other herbaceous hosts, favouring the emergence of potentially compensatory second mutations. We postulate that the joint action of phosphorylation and O-GlcNAcylation in the N-terminal region of CP allows a fine-tuning of the protein stability, providing the fair amount of CP required in each step of viral infection.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_05:35:06.828.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Sergio Ciordia
SpeciesList	scientific name: Nicotiana benthamiana; NCBI TaxID: 4100;
ModificationList	mono-N-acetylaminoglucosylated residue; phosphorylated residue; monohydroxylated residue; iodoacetamide derivatized residue
Instrument	TripleTOF 5600

Revision	Datetime	Status	ChangeLog Entry
0	2017-03-23 03:17:15	ID requested
1	2022-03-03 07:13:10	announced
⏵ 2	2024-10-22 05:35:07	announced	2024-10-22: Updated project metadata.

10.1111/mpp.12626;

Mart, í, nez-Turi, ñ, o S, P, é, rez JJ, Herv, á, s M, Navajas R, Ciordia S, Udeshi ND, Shabanowitz J, Hunt DF, Garc, í, a JA, Phosphorylation coexists with O-GlcNAcylation in a plant virus protein and influences viral infection. Mol Plant Pathol, 19(6):1427-1443(2018) [pubmed]

curator keyword: Biological

submitter keyword: yin-yang, plant virus, O-GlcNAcylation, Plum pox virus, phosphorylation, Potyvirus,Coat protein, crosstalk

Juan Antonio García
contact affiliation	Spanish National Center for Biotechnology (CNB-CSIC)
contact email	jagarcia@cnb.csic.es
lab head
Sergio Ciordia
contact affiliation	Spanish National Center for Biotechnology
contact email	sciordia@cnb.csic.es
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD006159
     1. Label: PRIDE project
     2. Name: Phosphorylation coexists with O-GlcNAcylation in a plant virus protein and shapes viral infection