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Role of N-linked glycosylation in the activity of the Friend murine leukemia virus SU protein receptor-binding domain.

Battini, JL; Kayman, SC; Pinter, A; Heard, JM; Danos, O; (1994) Role of N-linked glycosylation in the activity of the Friend murine leukemia virus SU protein receptor-binding domain. Virology , 202 (1) pp. 496-499. 10.1006/viro.1994.1369.

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Abstract

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.

Type: Article
Title: Role of N-linked glycosylation in the activity of the Friend murine leukemia virus SU protein receptor-binding domain.
Location: United States
DOI: 10.1006/viro.1994.1369
Keywords: 3T3 Cells, Animals, Friend murine leukemia virus, Glycosylation, Mice, Mutagenesis, Site-Directed, Mutation, Protein Conformation, Receptors, Virus, Viral Envelope Proteins, Viral Interference
UCL classification: UCL > Provost and Vice Provost Offices
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Medical Sciences > Cancer Institute
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Medical Sciences > Cancer Institute > Research Department of Haematology
URI: http://discovery.ucl.ac.uk/id/eprint/90919
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