Role of N-linked glycosylation in the activity of the Friend murine leukemia virus SU protein receptor-binding domain.
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 infectious virions. A truncated version of the mutant protein which included only the N-terminal domain was poorly transported but still able to interact with the receptor. Interference assays indicated that the interaction between the mutated protein and the virus receptor was weaker. We conclude that the elimination of N-linked oligosaccharide chains in the envelope N-terminal domain do not prevent receptor interaction but results in subtle conformational changes that may alter recognition and binding.
Battini
J L
JL
Laboratoire Rétrovirus et Transfert Génétique, URA CNRS 1157 Département SIDA et Rétrovirus, Institut Pasteur, Paris, France.
Kayman
S C
SC
Pinter
A
A
Heard
J M
JM
Danos
O
O
D016475:3T3 Cells; D000818:Animals; D005622:Friend murine leukemia virus / Q000378:metabolism*; D006031:Glycosylation; D051379:Mice; D016297:Mutagenesis, Site-Directed; D009154:Mutation; D011487:Protein Conformation; D011991:Receptors, Virus / Q000378:metabolism*; D014759:Viral Envelope Proteins / Q000235:genetics / Q000378:metabolism*; D014762:Viral Interference
D011991:Receptors, Virus; D014759:Viral Envelope Proteins