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To: Icebrg who wrote (792)3/19/2004 5:11:44 AM
From: Icebrg  Respond to of 2240
 
ROCHE SELECTS TWO GENMAB ANTIBODIES AS CLINICAL CANDIDATES

Summary: Roche has selected two Genmab antibodies as clinical candidates for two different disease areas.

Copenhagen, Denmark; March 19, 2004 –Genmab A/S (CSE: GEN) announced today Roche has selected two Genmab antibodies as candidates for clinical development. The antibodies, developed under a collaboration between Roche and Genmab which began in May 2001, are each designed to target a different disease area.

“The selection of these antibodies as clinical candidates underlines Genmab’s skill in producing antibody product candidates as well as Roche’s ability to identify valid disease targets,” said Lisa N. Drakeman, Ph.D., Chief Executive Officer of Genmab. “Our partnership with Roche continues to be fruitful.”

Under the agreement, Genmab utilizes its broad antibody expertise and development capabilities to create human antibodies to a broad range of disease targets identified by Roche. Roche has a proven successful track record in developing biologicals as innovative new products. Genmab receives milestone and royalty payments based on successful products. In certain circumstances, Genmab may obtain rights to develop products based on disease targets identified by Roche. If all goals are reached, the value of the collaboration to Genmab could be $100 million, plus royalties.



To: Icebrg who wrote (792)3/19/2004 6:01:11 PM
From: Icebrg  Read Replies (1) | Respond to of 2240
 
J Immunol. 2004 Mar 1;172(5):2845-52. Related Articles, Links

[More on MDX-1307]

Mannose receptor targeting of tumor antigen pmel17 to human dendritic cells directs anti-melanoma T cell responses via multiple HLA molecules.

Ramakrishna V, Treml JF, Vitale L, Connolly JE, O'Neill T, Smith PA, Jones CL, He LZ, Goldstein J, Wallace PK, Keler T, Endres MJ.

Medarex, Inc., Bloomsbury, NJ 08804, USA.

Targeting recycling endocytic receptors with specific Abs provides a means for introducing a variety of tumor-associated Ags into human dendritic cells (DCs), culminating in their efficient presentation to T cells. We have generated a human mAb (B11) against the mannose receptor that is rapidly internalized by DCs through receptor-mediated endocytosis. By genetically linking the melanoma Ag, pmel17, to Ab B11, we obtained the fully human fusion protein, B11-pmel17. Treatment of DCs with B11-pmel17 resulted in the presentation of pmel17 in the context of HLA class I and class II molecules. Thus, potent pmel17-specific T cells were cytotoxic toward gp100(+) HLA-matched melanoma targets, but not HLA-mismatched melanoma or gp100(-) nonmelanoma tumor lines. Importantly, competitive inhibition of lysis of an otherwise susceptible melanoma cell line by cold targets pulsed with known gp100 CD8 T cell epitopes as well as a dose-dependent proliferative response to Th epitopes demonstrates that DCs can process targeted Ag for activation of cytotoxic as well as helper arms of the immune response. Thus, the specific targeting of soluble exogenous tumor Ag to the DC mannose receptor directly contributes to the generation of multiple HLA-restricted Ag-specific T cell responses.

ncbi.nlm.nih.gov