Site directed mutagenesis of the murine coronavirus spike protein. Effects on fusion

Adv Exp Med Biol. 1995:380:283-6. doi: 10.1007/978-1-4615-1899-0_45.

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.

Publication types

  • Comparative Study
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cell Fusion*
  • Membrane Glycoproteins / biosynthesis
  • Membrane Glycoproteins / chemistry
  • Membrane Glycoproteins / physiology*
  • Mice
  • Models, Biological
  • Molecular Sequence Data
  • Murine hepatitis virus / genetics
  • Murine hepatitis virus / metabolism*
  • Mutagenesis, Site-Directed
  • Point Mutation
  • Protein Conformation
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Spike Glycoprotein, Coronavirus
  • Viral Envelope Proteins / biosynthesis
  • Viral Envelope Proteins / chemistry
  • Viral Envelope Proteins / physiology*

Substances

  • Membrane Glycoproteins
  • Recombinant Proteins
  • Spike Glycoprotein, Coronavirus
  • Viral Envelope Proteins