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J. Biol. Chem., Vol. 277, Issue 1, 135-140, January 4, 2002

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The Capsid Protein of a Plant Single-stranded RNA Virus Is Modified by O-Linked N-Acetylglucosamine^*

M. Rosario Fernández-Fernández, Emilio Camafeita, Pedro Bonay^§, Enrique Méndez, Juan Pablo Albar, and Juan A. García^¶

From the  Centro Nacional de Biotecnología, Consejo Superior de Investigaciones Científicas, and ^§ Centro de Biología Molecular "Severo Ochoa," Campus de la Universidad Autónoma de Madrid, 28049 Cantoblanco, Madrid, Spain

Plum pox virus (PPV) is a member of the Potyvirus genus of plant viruses. Labeling with UDP-[³H]galactose and galactosyltransferase indicated that the capsid protein (CP) of PPV is a glycoprotein with N-acetylglucosamine terminal residues. Mass spectrometry analysis of different PPV isolates and mutants revealed O-linked N-acetylglucosamination, a modification barely studied in plant proteins, of serine and/or threonine residues near the amino end of PPV CP. CP of PPV virions is also modified by serine and threonine phosphorylation, as shown by Western blot analysis with anti-phosphoserine and anti-phosphothreonine antibodies. Thus, "yin-yang" glycosylation and phosphorylation may play an important role in the regulation of the different functions in which the potyviral CP is involved.

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