title: Mapping of two O-GlcNAc modification sites in the capsid protein of the potyvirus Plum pox virus.
abstract: 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.
authors.affiliation: Department of Plant Molecular Genetics, Centro Nacional de Biotecnología (CSIC), Campus Universidad Autónoma de Madrid, 28049 Madrid, Spain.
authors.forename: José
authors.initials: J
authors.lastname: de Jesús Pérez
authors.forename: Silvia
authors.initials: S
authors.lastname: Juárez
authors.forename: Dinghu
authors.initials: D
authors.lastname: Chen
authors.forename: Cheryl L
authors.initials: CL
authors.lastname: Scott
authors.forename: Lynn M
authors.initials: LM
authors.lastname: Hartweck
authors.forename: Neil E
authors.initials: NE
authors.lastname: Olszewski
authors.forename: Juan Antonio
authors.initials: JA
authors.lastname: García
mesh_terms: D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D001483:Base Sequence; D001665:Binding Sites; D036022:Capsid Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D004279:DNA, Viral / Q000235:genetics; D006031:Glycosylation; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D010935:Plant Diseases / Q000821:virology; D017801:Plum Pox Virus / Q000737:chemistry* / Q000235:genetics / Q000472:pathogenicity; D011499:Protein Processing, Post-Translational; D027861:Prunus / Q000821:virology; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D013912:Threonine / Q000737:chemistry; D014026:Nicotiana / Q000821:virology
chemical_list: D036022:Capsid Proteins; D004279:DNA, Viral; D011993:Recombinant Fusion Proteins; D013912:Threonine