title: Evidence for a phosphorylation site in cytomegalovirus glycoprotein gB.
abstract: As part of our vaccine program, we have purified a recombinant form of human cytomegalovirus glycoprotein B that is able to induce high titers of virus-neutralizing antibodies. The isolated protein was found to be phosphorylated at a serine residue in position -7 from the C terminus of the protein. The corresponding synthetic peptide, HLKDSDEEENV, was an efficient in vitro substrate of casein kinase II.
authors.affiliation: Chiron Corporation, Emeryville, California 94608, USA.
authors.forename: N
authors.initials: N
authors.lastname: Norais
authors.forename: J A
authors.initials: JA
authors.lastname: Hall
authors.forename: L
authors.initials: L
authors.lastname: Gross
authors.forename: D
authors.initials: D
authors.lastname: Tang
authors.forename: S
authors.initials: S
authors.lastname: Kaur
authors.forename: S H
authors.initials: SH
authors.lastname: Chamberlain
authors.forename: R L
authors.initials: RL
authors.lastname: Burke
authors.forename: F
authors.initials: F
authors.lastname: Marcus
mesh_terms: D000595:Amino Acid Sequence; D003587:Cytomegalovirus / Q000378:metabolism*; D006801:Humans; D010766:Phosphorylation; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D014759:Viral Envelope Proteins / Q000235:genetics / Q000378:metabolism*
chemical_list: D011994:Recombinant Proteins; D014759:Viral Envelope Proteins