Proteomics

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Phosphorylation coexists with O-GlcNAcylation in a plant virus protein and shapes viral infection

ABSTRACT: 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.

INSTRUMENT(S): TripleTOF 5600

ORGANISM(S): Nicotiana Benthamiana

TISSUE(S): Leaf

SUBMITTER: Sergio Ciordia  

LAB HEAD: Juan Antonio García

PROVIDER: PXD006159 | Pride | 2022-03-03

REPOSITORIES: Pride

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Phosphorylation coexists with O-GlcNAcylation in a plant virus protein and influences viral infection.

Martínez-Turiño Sandra S   Pérez José De Jesús JJ   Hervás Marta M   Navajas Rosana R   Ciordia Sergio S   Udeshi Namrata D ND   Shabanowitz Jeffrey J   Hunt Donald F DF   García Juan Antonio JA  

Molecular plant pathology 20180130 6

Phosphorylation and O-GlcNAcylation are two widespread post-translational modifications (PTMs), often affecting the same eukaryotic target protein. Plum pox virus (PPV) is a member of the genus Potyvirus which infects a wide range of plant species. O-GlcNAcylation of the capsid protein (CP) of PPV has been studied extensively, and some evidence of CP phosphorylation has also been reported. Here, we use proteomics analyses to demonstrate that PPV CP is phosphorylated in vivo at the N-terminus and  ...[more]

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