Xbrane´s patented protein production technology has demonstrated in multiple academic studies to provide significantly higher productivity, leading to significantly lower production cost, compared to standard technologies in E.coli.

Biological drugs, and thus biosimilars as well, have proteins as active ingredients. Proteins are complex molecules which cannot be effectively manufactured synthetically but only in living cells through introducing a DNA-sequence into the host cell, which includes the formula for producing the given target protein.

Production takes place in fermentation tanks where the cells produce the target protein with the addition of substances including oxygen and glucose. Proteins can be produced in various kinds of living cells, the most common of which are bacteria cells of the E.coli type, mammal cells, yeast cells and various types of plant and animal cells. Different cells are suitable for different target proteins.

For example, thus far it has not been possible to produce full-length antibodies in E.coli, however, for many other proteins E.coli has the advantage that the bacteria strains are more cost-effective and have a relatively high regulatory acceptance by the authorities.

The benefit of Xbranes technology can be illustrated as a light dimmer to regulate the intensity of expression, or production, of the targeted protein. This stands in contrast to standard systems in E.coli where there is only an on and an off mode, where the on mode means a very accelerated expression or production of the target protein.

Being able to regulate the intensity is beneficial as too accelerated expression can lead to toxic effects for the host cell leading to mis-folding of the protein and a lower overall production of the right target protein. Xbranes technology is called LEMO, which stands for “LEss is MOre”.

Xbrane’s technology is based on production of proteins in E.coli cells. The unique aspect of Xbrane’s technology is that it can lead to significantly lower production costs for specific proteins. This can be achieved because the technology enables the production intensity of the given target protein to be regulated in the host cells.

It has been shown that a toxic effect can arise in the host cells at too high a production intensity and the key is therefore to find the optimum production intensity for the given protein, which maximises the productivity for the entire system. This is precisely what Xbrane’s technology enables, and it has been demonstrated in academic studies to lead to up to twelve times higher productivity compared with a standard system based on E.coli.

Productivity refers to the number of grams of protein that are produced per litre in the fermentation tank. As the production cost for a given scale of fermentation tank is independent of the productivity in the system, a higher productivity has a direct effect on the production cost per gram of protein.

Xbrane´s technology is called LEMO, coming from LEss is MOre, and is patent protected as per patent ”Expression system for proteins” (EP2268818 and WO2009106635 A1) which is approved in Europe and US up until 2029. There are multiple academic studies that has been published in several scientific journals, amongst them Nature, demonstrating the superiority of Xbrane´s technology.

Xbrane´s technology has demonstrated to have an up to 12 times productivity advantage vs. standard system in E.coli.

Source: Schlegel S, Rujas E, Ytterberg AJ, Zubarev RA, Luirink J, de Gier JW. Optimizing heterologous protein production in the periplasm of E. coli by regulating gene expression levels. Microb Cell Fact. 2013 Mar 12;12:24. Wagner S, Klepsch MM, Schlegel S, Appel A, Draheim R, Tarry M, Högbom M, van Wijk KJ, Slotboom DJ, Persson JO, de Gier JW. Tuning Escherichia coli for membrane protein overexpression. Proc Natl Acad Sci U S A. 2008 Sep 23;105(38):14371-6. Löw C1, Jegerschöld C, Kovermann M, Moberg P, Nordlund P. Optimisation of over-expression in E. coli and biophysical characterisation of human membrane protein synaptogyrin 1. PLoS One. 2012;7(6).