Successful Discovery Alliance Between Heptares and MorphoSys Combines Two Leading Technologies
Tokyo, Japan – 30 July 2015: Sosei Group Corporation (“Sosei”; TSE Mothers Index: 4565) is pleased to announce that its wholly-owned subsidiary Heptares Therapeutics (“Heptares”) has exercised an option to initiate a therapeutic antibody program arising from the alliance it entered with MorphoSys AG (FSE: MOR; Prime Standard Segment, TecDAX; OTC: MPSYY) in February 2013. The program will leverage MorphoSys’s Ylanthia® antibody library to generate novel antibody leads and addresses a GPCR target selected by Heptares, and for which Heptares has engineered a StaR® antigen.
The development and commercialization of this program by Heptares is covered by the existing collaboration agreement between the two companies. MorphoSys will receive a licensing fee and R&D funding from Heptares and is eligible to receive milestone payments and royalties on the sales of any therapeutic antibodies resulting from the program. Further financial details were not disclosed.
Malcolm Weir, CEO of Heptares, added: “The expertise at Heptares in GPCRs and MorphoSys’ antibody discovery capabilities form a powerful combination to unlock GPCR-targeted antibody discovery. We are delighted with the progress that has been made in the alliance, and to be adding this first antibody development program to our pipeline. This achievement highlights the power and versatility of our StaR® technology in both small molecule and biologics discovery for expanding our own pipeline and in partnerships.”
Marlies Sproll, Chief Scientific Officer of MorphoSys AG commented: “Antibodies developed with our Ylanthia® platform are increasingly gaining a foothold in the GPCR target space. MorphoSys has already successfully applied its comprehensive capabilities to generate functional antibodies against GPCRs in several projects. We are now looking forward to seeing the progress of this first therapeutic antibody program driven by Heptares as part of our very productive discovery collaboration with them.”
In February 2013, Heptares and MorphoSys, announced an agreement to discover novel antibody therapeutics targeting G protein-coupled receptors (GPCRs). Under the terms of the agreement, Heptares generates stabilized receptors (StaR®) for a set of GPCR disease targets proposed by MorphoSys. MorphoSys then utilizes its proprietary Ylanthia® library for the generation and further development of specific and functionally active anti-GPCR antibodies. The agreement also includes the option, now exercised by Heptares, to develop and commercialize a therapeutic antibody created by MorphoSys against a GPCR target selected by Heptares.
GPCRs are membrane proteins involved in a broad range of biological processes and diseases, including inflammatory disease, neuroscience indications, metabolic diseases and cancer. They comprise the single largest class of targets for pharmaceuticals currently on the market. Technical challenges, however, have meant that GPCRs have been largely intractable to therapeutic antibody development and to date only one GPCR-targeting antibody has been approved (for adult T-cell lymphoma), which reflects the central technical challenge of accessing reliable high-quality GPCR antigen.
The Heptares StaR® technology provides a breakthrough solution to this challenge, enabling the purification of properly folded and functional protein removed from the cell membrane. StaR proteins also preserve epitopes from the desired pharmacological state (active or inactive) of the GPCR, thereby enabling generation of panels of functional antibodies targeting the disease-relevant form of the receptor.
MorphoSys’s Ylanthia® antibody library comprises more than 100 billion distinct, fully human antibodies, which makes it the industry's largest known antibody Fab library. Ylanthia’s genetic composition translates into unprecedented structural diversity of the antibodies and offers optimized developability features. The library's diversity is expected to result in antibodies against previously inaccessible target molecules and to provide unique epitope coverage.