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Molecular and biological characterization of fusion regulatory proteins (FRPs): anti‐FRP mAbs induced HIV‐mediated cell fusion via an integrin system.
Author(s) -
Ohta H.,
Tsurudome M.,
Matsumura H.,
Koga Y.,
Morikawa S.,
Kawano M.,
Kusugawa S.,
Komada H.,
Nishio M.,
Ito Y.
Publication year - 1994
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1994.tb06479.x
Subject(s) - microbiology and biotechnology , library science , biology , medicine , computer science
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 alpha 3 subunit of integrin. Both anti‐FRP‐1 and anti‐FRP‐2 mAb‐induced cell fusion was blocked by anti‐beta 1 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).