Glycosylation-dependent inactivation of the ecotropic murine leukemia virus receptor.

Abstract

The ecotropic murine leukemia virus (E-MuLV) receptor expressed on Mus dunni tail fibroblast (MDTF) cells is a receptor for all E-MuLVs with the notable of Moloney murine leukemia virus (Mo-MuLV). Substitution of isoleucine for valine at position 214 in the third extracellular region (the putative E-MuLV binding site) of the MDTF receptor molecule allows this molecule to function as a Mo-MuLV receptor (M.V. Eiden, K. Farrell, J. Warsowe, L. A. Mahan, and C. A. Wilson, J. Virol. 67:4056-4061, 1993). We have now determined that treating MDTF cells with tunicamycin, an inhibitor of N-linked glycosylation, also renders them susceptible to Mo-MuLV infection. Two potential N-linked glycosylation sites are present in the third extracellular regions of both the NIH 3T3 and MDTF ecotropic receptors. The glycosylation site at position 229 of the MDTF receptor cDNA was eliminated by substituting a threonine codon for the asparagine codon. Mo-MuLV-resistant human HOS cells, expressing this form of the receptor, are susceptible to Mo-MuLV infection. Thus, our studies suggest that without a glycan moiety at position 229, the valine residue at 214 is no longer restrictive for Mo-MuLV infection. BHK-21 and CHO K1 hamster cells also express glycosylation-inactivated forms of the ecotropic receptor. Sequence analysis of these receptors together with our analysis of MDTF receptor function suggests that a single asparagine-linked glycosylation site is responsible for glycosylation inactivation of these receptors.

• Authors: M V Eiden, K Farrell, C A Wilson
• Journal: Journal of virology (J Virol) Vol. 68 Issue 2 Pg. 626-31 (Feb 1994) ISSN: 0022-538X [Print] United States
• PMID: 8289366 (Publication Type: Comparative Study, Journal Article)

Chemical References

• Carrier Proteins
• Membrane Glycoproteins
• Membrane Proteins
• Polysaccharides
• Receptors, Virus
• ecotropic murine leukemia virus receptor
• Tunicamycin

Topics

• Amino Acid Sequence
• Animals
• Carrier Proteins (classification, drug effects, genetics, metabolism)
• Cells, Cultured
• Cricetinae
• Glycosylation (drug effects)
• Humans
• Leukemia Virus, Murine (pathogenicity)
• Membrane Glycoproteins
• Membrane Proteins (classification, drug effects, genetics, metabolism)
• Mice
• Models, Molecular
• Molecular Sequence Data
• Muridae
• Polysaccharides (metabolism)
• Protein Processing, Post-Translational (drug effects)
• Receptors, Virus
• Retroviridae Infections
• Sequence Homology, Amino Acid
• Species Specificity
• Tunicamycin (pharmacology)
• Virulence