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17D Yellow Fever Virus Infection of P388D₁ Cells Mediated by Monoclonal Antibodies: Properties of the Macrophage Fc Receptor

Department of Medicine, The Rochester General Hospital and the University of Rochester School of Medicine and Dentistry, Rochester, New York 14621, U.S.A.

Thirteen IgG monoclonal antibodies to the envelope protein of 17D yellow fever virus (17D YF) were produced. All of the antibodies, whether type-specific to 17D YF or flavivirus cross-reactive, mediated antibody-dependent enhancement (ADE) of virus growth in P388D₁ cells. There was no consistent relationship between ADE titres and the degree or pattern of neutralizing and/or haemagglutination inhibition activity. Monoclonal antibodies of different isotypes were used to investigate further the properties of P388D₁ Fc receptors. The effects of trypsin treatment of P388D₁ on ADE were similar to those previously described in experiments measuring direct binding of IgG proteins or rosetting of sheep red blood cells (SRBC) by macrophages, demonstrating sensitivity to digestion by trypsin of the Fc receptor for monomeric IgG_2a but not for IgG_2b. Aggregated myeloma proteins of IgG_2a and IgG_2b isotypes competed equally well with either IgG_2a or IgG_2b monoclonal antibodies to 17D YF in inhibition of ADE. However, selective inhibition by the homologous isotype was observed when rosetting by P388D₁ of SRBC coated with IgG_2a or IgG_2b monoclonal antibodies was examined. These results may help to explain apparent discrepancies previously reported between experiments utilizing direct binding of IgG proteins and those using rosetting of antibody-coated SRBC to examine Fc receptor properties and indicate that immune complexes of virus and antibody resemble aggregated immunoglobulins with respect to macrophage Fc receptor function and differ from antibody-coated SRBCs.

Keywords: yellow fever virus, monoclonal Abs, enhancement, Fc receptors

Received 5 November 1982; accepted 30 December 1982.

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