Monoclonal antibodies distinguish between wild and vaccine strains of yellow fever virus by neutralization, hemagglutination inhibition, and immune precipitation of the virus envelope protein

J J Schlesinger, M W Brandriss, T P Monath
Virology 1983, 125 (1): 8-17
Nineteen monoclonal antibodies were produced to the 17D strain of yellow fever virus (17D YF). Virus-specific structural and nonstructural proteins were identified for 17D YF and for the parent wild Asibi YF by radioimmunoprecipitation and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Fourteen of the monoclonal antibodies were directed against the envelope glycoprotein, E, and five against the nonstructural protein gp 48. The E protein of 17D YF was resolved as a double complex whereas the E protein of Asibi YF appeared as a single band of slightly lower molecular weight. The only IgM anti-E antibody obtained precipitated and neutralized 17D YF specifically with no activity against Asibi YF. This antibody also distinguished clearly by neutralization (N) between the 17D-204 derived vaccine strain to which the animal had been immunized and 17D YF strains of different origin. All 13 IgG anti-E monoclonal antibodies had hemagglutination-inhibition (HI) activity to 17D YF and all but one neutralized Asibi YF; however, only 3 of the 13 neutralized 17D YF. Four anti-E antibodies cross-reacted with other flaviviruses by HI or HI and N. Three of the five anti-gp 48 antibodies had complement-fixation (CF) titers against 17D YF and Asibi YF but none had N or HI activity.

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