Purification of the 110-kilodalton glycoprotein receptor for mouse hepatitis virus (MHV)-A59 from mouse liver and identification of a nonfunctional, homologous protein in MHV-resistant SJL/J mice.

摘要: Abstract The receptor for mouse hepatitis virus strain A59 (MHV-A59) is a 110- to 120-kilodalton (kDa) glycoprotein which expressed in MHV-susceptible strains on the membranes of hepatocytes, intestinal epithelial cells, and macrophages. SJL/J mice, are highly resistant MHV-A59, were previously shown lack detectable levels by using either solid-phase assays or binding monoclonal anti-receptor antibody (MAb) blocks infection cells. This MAb was used affinity purification from livers Swiss Webster mice. The MHV an antigenically related protein 48 58 kDa copurified then separated preparative sodium dodecyl sulfate-polyacrylamide gel electrophoresis. first 15 amino acids sequenced, synthetic peptide this acid sequence prepared. Rabbit antiserum made against bound 48- 58-kDa BALB/c mice brush border In immunoblots hepatocyte MHV-resistant terminus identified proteins that 5 10 smaller than Thus, express shares some homology with but lacks virus-binding activity not recognized blocking MAb. These results suggest resistance MHV-A59 may be due absence mutation domain nonfunctional homolog