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J Gen Virol 75 (1994), 1451-1456; DOI 10.1099/0022-1317-75-6-1451
© 1994 Society for General Microbiology
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Antibody-dependent cellular cytotoxicity and neutralization of human immunodeficiency virus type 1 by high affinity cross-linking of gp41 to human macrophage Fc IgG receptor using bispecific antibody

Aloïse Mabondzo1, François Boussin1, Hervé Raoul1, Richard Le Naour1, Gabriel Gras1, Bruno Vaslin1, Jacques Bartholeyns3, Jean-Loup Romet-Lemonne2 and Dominique Dormont1

1 Laboratoire de Neuropathologie expérimentale et Neurovirologie, CRSSA, DSV/DPTE, Commissariat à l'Energie Atomique, BP 6, 92265 Fontenay-aux-Roses Cedex
2 Immuno-Designed-Molecules, 128 Boulevard Richard Lenoir, 75011 Paris
and3 CNTS, BP100, 91943 Les Ulis, France

Human monocytes/macrophages, which express Fc receptors for IgG are involved in human immuno-deficiency virus type 1 (HIV-1) infection and pathogenesis. These receptors are known to mediate numerous immunological functions including cell-mediated killing and possibly targeting of HIV to the lysophagosome monocyte-derived macrophage (MDM) entry route for virus neutralization. To study both activities in HIV-1 infection, MDM Fc{gamma}RI was specifically selected using bispecific antibody (Bs-Ab) containing whole human monoclonal antibody against gp41 and the Fab' fragment of murine anti-Fc{gamma}RI 22·2 antibody. Bs-Ab was found to mediate potent antibody-dependent cellular cytotoxicity and virus neutralization.

Received 9 August 1993; accepted 13 December 1993.


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