TY - JOUR
T1 - Identification of epitopes on the E glycoprotein of Saint Louis encephalitis virus using monoclonal antibodies
AU - Roehrig, J. T.
AU - Mathews, J. H.
AU - Trent, D. W.
N1 - Copyright:
Copyright 2018 Elsevier B.V., All rights reserved.
PY - 1983/7/15
Y1 - 1983/7/15
N2 - Twenty-one hybridomas producing monoclonal antibodies specific for the E glycoprotein of St. Louis encephalitis (SLE) virus, strain MSI-7, have been isolated. Serologic reactivities were initially determined by cross-reactivity indirect immunofluorescence assays using 22 strains of SLE virus and 8 other related flaviviruses. Four groups demonstrating type-, subcomplex-, supercomplex-, and group-specific reactivity patterns were identified. Analysis of hemagglutination-inhibition (HI) and virus neutralization (N) subdivided the cross-reactivity groups into eight epitopes (E-1a,b,c,d, E-2, E-3, and E-4a,b). The antibodies could detect strain differences between SLE viruses isolated from various geographic areas. Analysis of the spatial arrangements of these epitopes using competitive binding assays with representative antibodies possessing similar binding avidities, indicated that the protein was a continuum of six overlapping domains.
AB - Twenty-one hybridomas producing monoclonal antibodies specific for the E glycoprotein of St. Louis encephalitis (SLE) virus, strain MSI-7, have been isolated. Serologic reactivities were initially determined by cross-reactivity indirect immunofluorescence assays using 22 strains of SLE virus and 8 other related flaviviruses. Four groups demonstrating type-, subcomplex-, supercomplex-, and group-specific reactivity patterns were identified. Analysis of hemagglutination-inhibition (HI) and virus neutralization (N) subdivided the cross-reactivity groups into eight epitopes (E-1a,b,c,d, E-2, E-3, and E-4a,b). The antibodies could detect strain differences between SLE viruses isolated from various geographic areas. Analysis of the spatial arrangements of these epitopes using competitive binding assays with representative antibodies possessing similar binding avidities, indicated that the protein was a continuum of six overlapping domains.
UR - http://www.scopus.com/inward/record.url?scp=0020565814&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0020565814&partnerID=8YFLogxK
U2 - 10.1016/0042-6822(83)90323-9
DO - 10.1016/0042-6822(83)90323-9
M3 - Article
C2 - 6192585
AN - SCOPUS:0020565814
SN - 0042-6822
VL - 128
SP - 118
EP - 126
JO - Virology
JF - Virology
IS - 1
ER -