title: The use of two-dimensional SDS-PAGE to analyze the glycan heterogeneity of the respiratory syncytial virus fusion protein.
abstract: The respiratory syncytial virus (RSV) fusion (F) protein is synthesized as an inactive precursor (F0), which subsequently undergoes post-translational cleavage to give the disulphide bond-linked F1 and F2 subunits. The methodology detailing the use of two-dimensional electrophoresis, endoglycosidases, and alpha-mannosidase inhibitors, as applied to investigating F protein glycan maturation, is given. Examples are used to show how this methodology was used to provide evidence for glycan heterogeneity within the mature F protein.
authors.affiliation: MRC Virology Unit, Glasgow, UK.
authors.forename: Terence P
authors.initials: TP
authors.lastname: McDonald
authors.forename: Richard J
authors.initials: RJ
authors.lastname: Sugrue
mesh_terms: D000818:Animals; D002522:Chlorocebus aethiops; D015180:Electrophoresis, Gel, Two-Dimensional; D006031:Glycosylation; D011134:Polysaccharides / Q000032:analysis*; D011499:Protein Processing, Post-Translational / Q000502:physiology; D021122:Protein Subunits / Q000032:analysis* / Q000378:metabolism; D012136:Respiratory Syncytial Viruses / Q000737:chemistry* / Q000378:metabolism; D014709:Vero Cells; D014760:Viral Fusion Proteins / Q000032:analysis*
chemical_list: D011134:Polysaccharides; D021122:Protein Subunits; D014760:Viral Fusion Proteins