Molecular and biological characterization of fusion regulatory proteins (FRPs): Anti-FRP mAbs induced HIV-mediated cell fusion via an integrin system

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Abstract

Anti-FRP mAbs induced polykaryocyte formation of U2ME-7 cells (CD4+U937 cells transfected with the HIV gp160 gene). Anti-FRP-1 mAb immunoprecipitated gp80-85, gp120 and homodimers of these peptides, and anti-FRP-2 mAb reacted with gp135 identically to the α3 subunit of integrin. Both anti-FRP-1 and anti-FRP-2 mAb-induced cell fusion was blocked by anti-β1 integrin antibody, fibronectin or inhibiting anti-FRP-1 antibody. Therefore, anti-FRP mAbs were thought to induce the fusion via an integrin system(s). FRP-mediated fusion was temperature, cytoskeleton, energy and Ca2+ dependent. These experiments showed a possible regulatory function of cell fusion by an integrin system(s).

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Ohta, H., Tsurudome, M., Matsumura, H., Koga, Y., Morikawa, S., Kawano, M., … Ito, Y. (1994). Molecular and biological characterization of fusion regulatory proteins (FRPs): Anti-FRP mAbs induced HIV-mediated cell fusion via an integrin system. EMBO Journal, 13(9), 2044–2055. https://doi.org/10.1002/j.1460-2075.1994.tb06479.x

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