Mapping of two O-GlcNAc modification sites in the capsid protein of the potyvirus Plum pox virus

José de Jesús Pérez, Silvia Juárez, Dinghu Chen, Cheryl L. Scott, Lynn M. Hartweck, Neil E. Olszewski, Juan Antonio García

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21 Scopus citations


A large number of O-linked N-acetylglucosamine (O-GlcNAc) residues have been mapped in vertebrate proteins, however targets of O-GlcNAcylation in plants still have not been characterized. We show here that O-GlcNAcylation of the N-terminal region of the capsid protein of Plum pox virus resembles that of animal proteins in introducing O-GlcNAc monomers. Thr-19 and Thr-24 were specifically O-GlcNAcylated. These residues are surrounded by amino acids typical of animal O-GlcNAc acceptor sites, suggesting that the specificity of O-GlcNAc transferases is conserved among plants and animals. In laboratory conditions, mutations preventing O-GlcNAcylation of Thr-19 and Thr-24 did not have noticeable effects on PPV competence to infect Prunus persicae or Nicotiana clevelandii. However, the fact that Thr-19 and Thr-24 are highly conserved among different PPV strains suggests that their O-GlcNAc modification could be relevant for efficient competitiveness in natural conditions.

Original languageEnglish (US)
Pages (from-to)5822-5828
Number of pages7
JournalFEBS Letters
Issue number25
StatePublished - Oct 30 2006

Bibliographical note

Funding Information:
We thank Elvira Domínguez for technical assistance. This work was supported by Grants BIO2004-02687 from Spanish MEC and SP22-CT-2004 from European Union to J.A.G and the National Science Foundation (MCB-0112826 and -0516690) to N.E.O and by the US Department of Energy (DE-FG02-02ER15353) to N.E.O and L.M.H.


  • Capsid protein
  • O-glycosylation
  • Plum pox virus
  • Potyvirus


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