O-GlcNAc modification of the coat protein of the potyvirus Plum pox virus enhances viral infection

José de Jesús Pérez, Namrata D. Udeshi, Jeffrey Shabanowitz, Sergio Ciordia, Silvia Juárez, Cheryl L. Scott, Neil E. Olszewski, Donald F. Hunt, Juan Antonio García

Research output: Contribution to journalArticlepeer-review

25 Scopus citations


O-GlcNAcylation is a dynamic protein modification which has been studied mainly in metazoans. We reported previously that an Arabidopsis thaliana O-GlcNAc transferase modifies at least two threonine residues of the Plum pox virus (PPV) capsid protein (CP). Now, six additional residues were shown to be involved in O-GlcNAc modification of PPV CP. CP O-GlcNAcylation was abolished in the PPV CP7-T/A mutant, in which seven threonines were mutated. PPV CP7-T/A infected Nicotiana clevelandii, Nicotiana benthamiana, and Prunus persica without noticeable defects. However, defects in infection of A. thaliana were readily apparent. In mixed infections of wild-type arabidopsis, the CP7-T/A mutant was outcompeted by wild-type virus. These results indicate that CP O-GlcNAcylation has a major role in the infection process. O-GlcNAc modification may have a role in virion assembly and/or stability as the CP of PPV CP7-T/A was more sensitive to protease digestion than that of the wild-type virus.

Original languageEnglish (US)
Pages (from-to)122-131
Number of pages10
Issue number2
StatePublished - Aug 1 2013


  • Capsid protein
  • Mass spectrometry
  • O-GlcNAcylation
  • Plum pox virus
  • Potyvirus

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