BioWa and Lonza are joining forces to develop a new technology platform to produce more potent antibodies with enhanced cell-killing powers.
The agreement will see the combination of BioWa's Potelligent technology with Lonza's GS (glutamine synthetase) Gene Expression System and CHOK1SV cell line.
The aim is to produce a high-yield mammalian expression system which will produce more potent antibodies with an enhanced antibody-dependent cellular cytotoxicity (ADCC).
"We believe that combining both parties' technologies addresses a clear market need to improve production yields and can significantly aid the development of more effective targeted treatments for cancer and other life-threatening and debilitating diseases," BioWa president and chief executive Dr Masamichi Koike said.
"This collaboration with Lonza . . . will enable us to jointly offer a superior production platform to parties interested in the development of efficacy-enhanced antibody therapeutics," Koike said.
Under the terms of the agreement, the companies intend to make the new Potelligent CHOK1SV cell line available for licensing and it will be offered as part of Lonza's development services in combination with Lonza's GS Gene Expression System.
The two companies will jointly market the new technology platform.
Potelligent technology involves the reduction of the amount of fucose in the carbohydrate structure of an antibody using a proprietary fucosyltransferase-knockout CHO cell line as a production cell.
Potelligent antibodies are designed to increase the ADCC activity of an antibody - where an antibody first binds to an antigen on tumour cells and then to Fc receptors on monocytes, macrophages, and natural killer cells, for example. These cells then engulf the tumour cell and destroy it.
The activity makes the antibody more potent.
Genentech, Biogen Idec, Medarex, MedImmune and Takeda are all licensed to use the Potelligent technology.
GS is the enzyme responsible for the biosynthesis of glutamine from glutamate and ammonium in an enzymatic reaction that provides the only pathway for glutamine formation in a mammalian cell.
Thus, in the absence of glutamine in the growth medium, the GS enzyme is essential for the survival of the mammalian cells in culture.
Some mammalian cell lines, such as mouse myeloma lines, do not express sufficient GS to survive without added glutamine, so with these cell lines a transfected GS gene can function as a selectable marker by permitting growth in a glutamine-free medium.
Other cell lines however, such as Chinese Hamster Ovary (CHO) cell lines, do contain sufficient active GS to survive without exogenous glutamine and in these cases the specific GS inhibitor, methionine sulphoximine (MSX), can be used to inhibit endogenous GS activity such that only transfectants with additional GS activity can survive.
Using this method, cell lines have been created that are capable of producing 5.5g/L of recombinant antibody with specific production rates of typically 20 to 50pg/cell/day.
Financial details were not disclosed.