[Monoclonal antibodies, 30 years of success].
The hybridoma fusion technology, proposed in 1975, gave for the first time an access to murine monoclonal antibodies. The high potential of these new molecules, as laboratory tools, was exploited during the two following decades. Nowadays, antibodies, still omnipresent in both diagnostic and research domains, have progressively invaded the therapeutic field. New technologies, such as phage display and transgenic mice, have been implemented, allowing for the isolation of fully human antibodies. The natural complexity of the antibody molecules and the development of engineering methodologies helped making them ideal candidates for new applications and immunotherapeutic challenges. The present review is a temporary update of the different antibody-derived molecules as well as a walk-through among the techniques recently applied to antibody engineering. In addition it also address an important issue, such as the development of expression systems suitable large-scale production of recombinant antibodies.
Laffly
Emmanuelle
E
LCCP, IBS, Institut de Biologie Structurale Jean-Pierre Ebel, 41, rue Jules Horowitz, F-38027 Grenoble, CEA, France.
Sodoyer
Régis
R
D000818:Animals; D000911:Antibodies, Monoclonal / Q000627:therapeutic use*; D046528:Chimerism; D006801:Humans; D051379:Mice; D008822:Mice, Transgenic; D009838:Oligodeoxyribonucleotides / Q000138:chemical synthesis / Q000737:chemistry; D015202:Protein Engineering / Q000379:methods / Q000639:trends; D012333:RNA, Messenger / Q000235:genetics; D011994:Recombinant Proteins / Q000627:therapeutic use; D012270:Ribosomes / Q000235:genetics / Q000276:immunology
D000911:Antibodies, Monoclonal; D009838:Oligodeoxyribonucleotides; D012333:RNA, Messenger; D011994:Recombinant Proteins