Article
Role of N-linked glycosylation in the activity of the Friend murine leukemia virus SU protein receptor-binding domain.
Virology - 1 Jul 1994
Battini J L, Kayman S C, Pinter A, Heard J M, Danos O
Abstract excerpt
The 243 N-terminal residues of Friend Murine Leukemia Virus envelope glycoprotein (SU) fold into a structurally and functionally autonomous domain which contains the determinants for binding to the ecotropic virus receptor. The two N-linked glycosylation sites present in this N-terminal portion of the viral SU were removed by site-directed mutagenesis without disturbing its biosynthesis and incorporation into...
Topics
- 3T3 Cells
- Animals
- Friend murine leukemia virus
- Glycosylation
- Mice
- Mutagenesis, Site-Directed
- Mutation
- Protein Conformation
- Receptors, Virus
- Viral Envelope Proteins
- Viral Interference
