title: Characterization of post-translationally modified recombinant protein using liquid chromatography/mass spectrometry.
abstract: Post-translational modification plays an important role in the biological functions of many proteins. Characterization of such modifications is crucial in the development of recombinant protein-based vaccines. Liquid Chromatography coupled with Mass Spectrometry (LC/MS) provides a powerful tool with high resolution and accuracy to characterize proteins and their post-translational modifications. The technique was applied to characterization of a Lyme vaccine protein rOspA (recombinant Outer surface protein A). The results demonstrate that LC/MS could be used to resolve and characterize various forms of post-translational lipidation of the protein. It was this detailed structural information that made it possible to validate a method for quantitative determination of the lipidation forms of rOspA.
authors.affiliation: Aventis Pasteur, Swiftwater, PA 18370, USA.
authors.forename: X D
authors.initials: XD
authors.lastname: Wu
authors.forename: R A
authors.initials: RA
authors.lastname: Kircher
authors.forename: P H
authors.initials: PH
authors.lastname: McVerry
authors.forename: D A
authors.initials: DA
authors.lastname: Malinzak
mesh_terms: D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry* / Q000276:immunology; D002853:Chromatography, Liquid; D008055:Lipids / Q000737:chemistry; D008970:Molecular Weight; D010455:Peptides / Q000737:chemistry; D011499:Protein Processing, Post-Translational; D021241:Spectrometry, Mass, Electrospray Ionization; D014614:Vaccines, Synthetic / Q000737:chemistry / Q000276:immunology
chemical_list: D001425:Bacterial Outer Membrane Proteins; D008055:Lipids; D010455:Peptides; D014614:Vaccines, Synthetic