title: The phosphoproteome of the adenovirus type 2 virion.
abstract: We have used a proteomics approach to identify sites of phosphorylation in the structural proteins of the Adenovirus type 2 particle. This protein modification might play an important role during infection. Peptides from highly purified virus were enriched for phosphorylations and analyzed by liquid chromatography-high-resolving mass spectrometry. Phosphorylations were identified in 11 structural peptides and 29 non-redundant phosphorylation sites were unambiguously assigned to specific amino acid. An unexpected result was the finding of phosphotyrosine in two of the viral polypeptides. The most highly phosphorylated protein was pIIIa with 12 identified phosphorylation sites. An identified preference for proline or leucine residue flanking the phosphorylation sites downstream suggests that cellular kinases are involved in many of the phosphorylations. Structural modeling showed that one site in the hexon is located on the outer side of the virus and could be of importance for the virus when attaching and entering cells.
authors.affiliation: Department of Immunology, Genetics and Pathology, Science for Life Laboratory, Rudbeck Laboratory, Uppsala University, SE-751 85 Uppsala, Sweden. sara.lind@igp.uu.se
authors.forename: Sara
authors.initials: S
authors.lastname: Bergström Lind
authors.forename: Konstantin A
authors.initials: KA
authors.lastname: Artemenko
authors.forename: Lioudmila
authors.initials: L
authors.lastname: Elfineh
authors.forename: Yanhong
authors.initials: Y
authors.lastname: Zhao
authors.forename: Jonas
authors.initials: J
authors.lastname: Bergquist
authors.forename: Ulf
authors.initials: U
authors.lastname: Pettersson
mesh_terms: D000256:Adenoviridae / Q000235:genetics / Q000378:metabolism*; D000595:Amino Acid Sequence; D002853:Chromatography, Liquid; D006367:HeLa Cells; D006801:Humans; D007930:Leucine / Q000737:chemistry / Q000378:metabolism; D013058:Mass Spectrometry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry / Q000378:metabolism; D010750:Phosphoproteins / Q000737:chemistry / Q000378:metabolism*; D010766:Phosphorylation; D019000:Phosphotyrosine / Q000737:chemistry / Q000378:metabolism; D011392:Proline / Q000737:chemistry / Q000378:metabolism; D020543:Proteome / Q000737:chemistry / Q000378:metabolism*; D040901:Proteomics; D014764:Viral Proteins / Q000737:chemistry / Q000378:metabolism*; D014771:Virion / Q000235:genetics / Q000378:metabolism*
chemical_list: D010455:Peptides; D010750:Phosphoproteins; D020543:Proteome; D014764:Viral Proteins; D019000:Phosphotyrosine; D011392:Proline; D007930:Leucine