The capsid protein of a plant single-stranded RNA virus is modified by O-linked N-acetylglucosamine
M Rosario Fernández-Fernández1, Emilio Camafeita, Pedro Bonay
1Centro Nacional de Biotecnologia, Consejo Superior de Investigaciones Cientificas, Campus de la Universidad Autónoma de Madrid, 28049 Cantoblanco, Madrid, Spain.
Abstract:
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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