Deletion mapping analyses indicate that epitopes for monoclonal antibodies to the NS phosphoprotein of VSV are linear and clustered.
Thirteen distinct monoclonal antibodies to the 30-kDa NS phosphoprotein of vesicular stomatitis virus were isolated and assayed by Western blot analysis and immune precipitation reactions. Epitopes recognized by the antibodies were mapped by immune precipitation of NS deletion proteins synthesized in vitro from cloned NS gene constructs. None of the epitopes recognized by the 13 antibodies could be mapped to the phosphorylated amino-terminal half of the NS protein. Twelve of the antibodies recognized epitopes located within the carboxy-terminal 142 amino acids of the protein. The great majority of epitopes appeared to consist of a linear array of amino acids.
D000911:Antibodies, Monoclonal / Q000276:immunology*; D000914:Antibodies, Viral / Q000276:immunology*; D002213:Capsid / Q000235:genetics / Q000276:immunology*; D000939:Epitopes / Q000235:genetics; D010750:Phosphoproteins / Q000235:genetics / Q000276:immunology; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000276:immunology; D014721:Vesicular stomatitis Indiana virus / Q000235:genetics / Q000276:immunology*; D014758:Viral Core Proteins / Q000235:genetics / Q000276:immunology*; D017361:Viral Nonstructural Proteins
D000911:Antibodies, Monoclonal; D000914:Antibodies, Viral; D000939:Epitopes; D010750:Phosphoproteins; D011994:Recombinant Proteins; D014758:Viral Core Proteins; D017361:Viral Nonstructural Proteins