Using murine monoclonal antibodies (MAbs) to rubella virus haemagglutinin, five epitopes were identified in competitive ELISA binding assays: A, B, D and E by haemagglutination-inhibiting (HI) MAbs with no neutralizing (Nt) activity, and C by a MAb with neither activity. However, when HI and Nt activities were determined in the presence of anti-mouse immunoglobulins, epitopes A, B and D were defined by both HI and Nt MAbs, whereas epitopes C and E were identified by HI MAbs without Nt activity. A synergistic Nt activity, in the absence of anti-mouse immunoglobulins, was displayed by mixtures of antibodies of different epitope groups. Analysis of mixtures of MAb pairs each belonging to a different epitope class, showed that synergistic Nt activity was elicited primarily by the group A epitope, secondarily by groups B and D and only minimally by groups C and E.
AsheW. K.,
NotkinsA. L.1966; Neutralization of an infectious herpes simplex virus-antibody complex by antiglobulin. Proceedings of the National Academy of Sciences, U.S.A 56:447–451
BurnetteW. M.1981; “Western blotting”. Electrophoretic transfer of proteins from sodium dodecyl sulfatepolyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated Protein A. Analytical Biochemistry 112:195–203
CleggJ. C. S.,
ChanasA. C.,
GouldE. A.1983; Conformational changes in Sindbis virus E1 glycoprotein induced by monoclonal antibody binding. Journal of General Virology 64:1121–1126
GernaG.1975; Rubella virus identification in primary and continuous monkey kidney cell cultures by the immunoperoxidase technique. Archives of Virology 49:291–295
GreenK. Y.,
DorsettP. H.1986; Rubella virus antigens: localization of epitopes involved in hemagglutination and neutralization by using monoclonal antibodies. Journal of Virology 57:893–898
KingsfordL.1984; Enhanced neutralization of La Crosse virus by the binding of specific pairs of monoclonal antibodies to the G1 glycoprotein. Virology 136:265–273
LubeckM. D.,
GerhardW.1981; Topographical mapping of antigenic sites on the influenza A/PR/8/34 virus hemagglutinin using monoclonal antibodies. Virology 113:62–64
Oker-BlomC.,
KalkkinenN.,
KääriäinenL.,
PetterssonR. F.1983; Rubella virus contains one capsid protein and three envelope glycoproteins, E1, E2a, and E2b. Journal of Virology 46:964–973
PalmerD. F.,
HermannK. L.,
LincolnR. E.,
HearnM. V.,
FullerJ. M.1970A Procedural Guide to the Performance of the Standardized Rubella Hemagglutination-inhibition Test Immunity Series No. 2 Atlanta: Center for Disease Control;
UminoY.,
SatoT. A.,
KatowS.,
MatsunoT.,
SugiuraA.1985; Monoclonal antibodies directed to E1 glycoprotein of rubella virus. Archives of Virology 83:33–42
WaxhamM. N.,
WolinskyJ. S.1985; Detailed immunologic analysis of the structural polypeptides of rubella virus using monoclonal antibodies. Virology 143:153–165
WilsonM. B.,
NakaneP. K.1978; Developments in the periodate method of conjugating horseradish peroxidase to antibodies. In Immunofluorescence and Related Staining Techniques pp. 215–225KnappW.,
HolubarK.,
WickG.
Edited by Amsterdam: Elsevier;
WolinskyJ. S.,
WaxhamM. N.,
HessJ. L.,
TownsendJ. J.,
BaringerJ. R.1982; Immunochemical features of a case of progressive rubella panencephalitis. Clinical and Experimental Immunology 48:359–366