Trypsin-sensitive neutralization site on VP1 of Theiler's murine encephalomyelitis viruses.
We generated Theiler's murine encephalomyelitis virus mutants resistant to several neutralizing monoclonal antibodies (MAbs) having their epitopes near a trypsin cleavage site of VP1. Neutralization and Western blot (immunoblot) studies suggest that two of the MAbs have identical epitopes that partly overlap the epitope of a third MAb. Sequencing of RNA of the mutants localized the epitopes to a site near the carboxyl end of VP1. The limited diversity of nucleotide changes seen in the mutants and the immunodominance of the site suggest that the carboxyl end of VP1 may have an important function.
Ohara
Y
Y
Department of Neurology, University of Chicago, Illinois 60637.
Senkowski
A
A
Fu
J L
JL
Klaman
L
L
Goodall
J
J
Toth
M
M
Roos
R P
RP
D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology; D001483:Base Sequence; D004770:Enterovirus / Q000276:immunology*; D000939:Epitopes / Q000276:immunology; D007118:Immunoassay; D004680:Maus Elberfeld virus / Q000235:genetics / Q000276:immunology*; D051379:Mice; D008969:Molecular Sequence Data; D009154:Mutation; D009500:Neutralization Tests; D012367:RNA, Viral / Q000235:genetics; D014357:Trypsin / Q000494:pharmacology; D014764:Viral Proteins / Q000235:genetics / Q000276:immunology*; D015678:Viral Structural Proteins
D000911:Antibodies, Monoclonal; D000939:Epitopes; D012367:RNA, Viral; D014764:Viral Proteins; D015678:Viral Structural Proteins; D014357:Trypsin