title: Site directed mutagenesis of the murine coronavirus spike protein. Effects on fusion.
abstract: Mutations were introduced in the transmembrane region of the spike protein of the murine coronavirus A59. The maturation of these mutant S proteins was not affected, they were all expressed at the cell surface, and became acylated, however some mutant S proteins did not induce cell-to-cell fusion. An I-->K change in the middle of the predicted transmembrane (TM) anchor and mutation of the first three cysteine residues of the TM domain resulted in a fusion-negative phenotype. We propose a model by which these data can be explained.
authors.affiliation: Institute of Virology, Faculty of Medicine, University of Leiden, The Netherlands.
authors.forename: E C
authors.initials: EC
authors.lastname: Bos
authors.forename: L
authors.initials: L
authors.lastname: Heijnen
authors.forename: W J
authors.initials: WJ
authors.lastname: Spaan
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002459:Cell Fusion; D008562:Membrane Glycoproteins / Q000096:biosynthesis / Q000737:chemistry / Q000502:physiology*; D051379:Mice; D008954:Models, Biological; D008969:Molecular Sequence Data; D006517:Murine hepatitis virus / Q000235:genetics / Q000378:metabolism*; D016297:Mutagenesis, Site-Directed; D017354:Point Mutation; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000378:metabolism; D064370:Spike Glycoprotein, Coronavirus; D014759:Viral Envelope Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000502:physiology*
chemical_list: D008562:Membrane Glycoproteins; D011994:Recombinant Proteins; D064370:Spike Glycoprotein, Coronavirus; D014759:Viral Envelope Proteins