title: Role of N-linked glycosylation of the Hendra virus fusion protein.
abstract: The Hendra virus fusion (F) protein contains five potential sites for N-linked glycosylation in the ectodomain. Examination of F protein mutants with single asparagine-to-alanine mutations indicated that two sites in the F(2) subunit (N67 and N99) and two sites in the F(1) subunit (N414 and N464) normally undergo N-linked glycosylation. While N-linked modification at N414 is critical for protein folding and transport, F proteins lacking carbohydrates at N67, N99, or N464 remained fusogenically active. As N464 lies within heptad repeat B, these results contrast with those seen for several paramyxovirus F proteins.
authors.affiliation: Department of Molecular and Cellular Biochemistry University of Kentucky, 800 Rose Street, UKMC MN606 Lexington, KY 40536-0298, USA.
authors.forename: James Richard
authors.initials: JR
authors.lastname: Carter
authors.forename: Cara Theresia
authors.initials: CT
authors.lastname: Pager
authors.forename: Stephen Derrick
authors.initials: SD
authors.lastname: Fowler
authors.forename: Rebecca Ellis
authors.initials: RE
authors.lastname: Dutch
mesh_terms: D000818:Animals; D002522:Chlorocebus aethiops; D006224:Cricetinae; D006031:Glycosylation; D045404:Hendra Virus / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D008561:Membrane Fusion; D009154:Mutation; D017510:Protein Folding; D014709:Vero Cells; D014760:Viral Fusion Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
chemical_list: D014760:Viral Fusion Proteins