Last update 01 Nov 2024

Lexigen Pharmaceuticals Corp.

Subsidiary Company|

Massachusetts, United States

Subsidiary Company|

Massachusetts, United States

Last update 01 Nov 2024

Overview

Pipeline

Deal

Translational Medicine

Overview

Basic Info

Introduction

Lexigen Pharmaceuticals is a company that specializes in conducting research in both the physical and biological fields. It was established by Stephen D. Gillies and is based in Billerica, Massachusetts.

Tags

Congenital Disorders

Neoplasms

Eye Diseases

Antibody fusion proteins

Disease domain score

A glimpse into the focused therapeutic areas

Technology Platform

Most used technologies in drug development

Targets

Most frequently developed targets

Disease Domain	Count

Neoplasms	1

Top 5 Drug Type	Count

Antibody fusion proteins	1

Top 5 Target	Count

GD2 x IL-2R	1

Drugs associated with Lexigen Pharmaceuticals Corp.

Lorukafusp alfa

Target

GD2 x IL-2R

Mechanism

GD2 inhibitors [+1]

Active Org.

APEIRON Biologics AG [+1]

Originator Org.

Lexigen Pharmaceuticals Corp.

Active Indication

Melanoma [+2]

Inactive Indication

Melanoma, Cutaneous Malignant [+3]

Drug Highest PhasePhase 2

First Approval Ctry. / Loc.-

First Approval Date-

Capravirine

Target

Mechanism

RT inhibitors

Active Org.-

Originator Org.

Shionogi & Co., Ltd.

Active Indication-

Inactive Indication

HIV Infections

Drug Highest PhaseSuspended

First Approval Ctry. / Loc.-

First Approval Date-

Cancer vaccine (Lexigen)

Target-

Mechanism

Immunostimulants

Active Org.-

Originator Org.

Lexigen Pharmaceuticals Corp. [+1]

Active Indication-

Inactive Indication

Colorectal Cancer [+1]

Drug Highest PhaseDiscontinued

First Approval Ctry. / Loc.-

First Approval Date-

Clinical Trials associated with Lexigen Pharmaceuticals Corp.

NCT00002214 / CompletedPhase 1

Phase I Trial of S-1153 in Patients With HIV Infection

To assess the toxicity profile and determine the maximum tolerated dose (MTD), if possible, of S-1153 administered orally 3 times daily for 14 days. To investigate the clinical pharmacokinetic parameters for S-1153. To assess anti-HIV activity associated with S-1153 administration through evaluation of CD4 and viral load measurements.

Start Date-

Sponsor / Collaborator

Lexigen Pharmaceuticals Corp.

100 Clinical Results associated with Lexigen Pharmaceuticals Corp.

0 Patents (Medical) associated with Lexigen Pharmaceuticals Corp.

Literatures (Medical) associated with Lexigen Pharmaceuticals Corp.

01 Jun 2002·BloodQ1 · MEDICINE

Antidisialoganglioside/granulocyte macrophage–colony-stimulating factor fusion protein facilitates neutrophil antibody-dependent cellular cytotoxicity and depends on FcγRII (CD32) and Mac-1 (CD11b/CD18) for enhanced effector cell adhesion and azurophil granule exocytosis

Q1 · MEDICINE

Article

Author: Super, Michael ; Gillies, Stephen D. ; Reynolds, C. Patrick ; Metelitsa, Leonid S. ; Seeger, Robert C. ; Shimada, Hiroyuki

Polymorphonuclear leukocytes (PMNs) mediate antibody-dependent cellular cytotoxicity (ADCC), which is increased by the addition of granulocyte-macrophage colony-stimulating factor (GM-CSF). We sought to determine whether PMN ADCC also would be increased by the addition of an antibody/GM-CSF fusion protein and whether this would be associated with the up-regulation and activation of Mac-1 (CD11b/CD18) and with azurophil granule exocytosis. ADCC against LA-N-1 human neuroblastoma cells was evaluated with 4-hour calcein acetoxymethyl ester (calcein-AM) microcytotoxicity assay, electron microscopy, and multi-parameter flow cytometry. With the calcein-AM assay, LA-N-1 cell survival was 10%, 55%, and 75% when PMN ADCC was mediated by the antidisialoganglioside (anti-GD2) immunocytokine hu14.18/GM-CSF, by monoclonal antibody (mAb) hu14.18 mixed with GM-CSF, and by hu14.18 alone. Function-blocking mAbs demonstrated that FcγRII and FcγRIII were required for ADCC with hu14.18 alone or mixed with GM-CSF, but that only FcγRII was required for ADCC with hu14.18/GM-CSF. ADCC mediated by hu14.18 and hu14.18/GM-CSF was Mac-1 dependent. Electron microscopy demonstrated the greatest PMN adhesion, spreading, and lysis of targets with hu14.18/GM-CSF. Monoclonal antibodies blocking Mac-1 function allowed the tethering of PMN to targets with hu14.18/GM-CSF but prevented adhesion, spreading, and cytolysis. Flow cytometry showed that hu14.18 with or without GM-CSF and hu14.18/GM-CSF all mediated Mac-1–dependent PMN–target cell conjugate formation but that GM-CSF was required for the highest expression and activation of Mac-1, as evidenced by the mAb24-defined β2-integrin activation epitope. Hu14.18/GM-CSF induced the highest sustained azurophil granule exocytosis, almost exclusively in PMNs with activated Mac-1. Thus, hu14.18/GM-CSF facilitates PMN ADCC against neuroblastoma cells associated with FcγRII and Mac-1–dependent enhanced adhesion and degranulation.

01 Jan 2002·Clinical cancer research : an official journal of the American Association for Cancer Research

Improved circulating half-life and efficacy of an antibody-interleukin 2 immunocytokine based on reduced intracellular proteolysis.

Article

Author: Wong, Wai-Keung ; Burger, Christa ; Lo, Kin-Ming ; Dahl, Thomas ; Lan, Yan ; Gillies, Stephen D

PURPOSEPrevious studies showed that reducing the interaction of antibody-interleukin 2 immunocytokines with Fc receptors improved their circulating half-life in mice and increased their antitumor activity. We sought to modify sequences that would increase half-life but retain the ability to activate Fc receptor-mediated effector functions.EXPERIMENTAL DESIGNModified immunocytokines were assessed in vitro for effector function and protease sensitivity and in vivo for pharmacokinetic and antitumor activities in an syngeneic tumor regression model.RESULTSSingle amino acid changes in the junction sequence between the antibody and interleukin-2 components had dramatic effects on circulating half-life and antitumor activity. This effect was independent of Fc receptor binding to either Fcgamma receptors or the Fc protection receptor, but was associated with changes in susceptibility to intracellular proteases.CONCLUSIONSWe have identified modifications that dramatically improve the circulating half-life of immunocytokines based on increased resistance to intracellular degradation and thus have demonstrated how these molecules can be recycled in and out of an intracellular compartment. Use of these improved immunocytokines with highly favorable pharmacokinetic properties and retained effector functions should lead to more effective treatment of epithelial cancers.

31 Dec 2001·Human Antibodies

Engineered antibodies take center stage

Review

Author: George, Andrew J.T. ; Huston, James S.

The start of the post-genomic era provides a useful juncture for reflection on the state of antibody engineering, which will be a critical technology for relating function and pathology to genomic sequence in biology and medicine. The phenomenal progress in deciphering the human genome has given significant impetus to the application of engineered antibodies in proteomics. Thus, advances in phage display antibody libraries can now help to define novel gene function and the measurement of abnormal protein expression in pathological states. Furthermore, intrabody and antibody engineering provide vehicles for the development of molecular medicines of the future. In addition to these new directions, antibody engineering has begun to show concrete success in its long-term efforts to develop targeted immunotherapies for cancer and other diseases. The cornerstones of clinical development are the detailed academic clinical trials that continue to push the boundaries of engineered antibodies into the real world. The field displays a healthy impatience for practical results, as research accelerates with concerted efforts to transfer preclinical insights into clinical trials. Growing private and governmental expenditures will lead to the rapid expansion of life-saving immunotherapeutic agents. The present review developed from our effort to report on the 11th Annual International Conference on Antibody Engineering (3-6 December 2000). This annual meeting is a forum for discussions on the latest advances in antibody engineering groups from around the world, and now includes the broader agenda of engineering in molecular immunology. In bringing scientists together to exchange ideas at this open forum, new collaborations and the threads of new discoveries are woven. For example, Professors Gerhard Wagner (Harvard Medical School), Dennis Burton (Scripps Research Institute), and Peter Hudson (CSIRO, Melbourne, Australia) gave exciting insights on structural immunobiology that had implications across many disciplines. The growth in antibody engineering was highlighted by the attendance of some 600 participants at the meeting, doubling that of the 1999 meeting. Dramatic clinical acceptance of monoclonal antibodies during the past two years has fostered this growth, with sales in 2000 of 1.8 billion dollars and projections for 2001 of 3 billion dollars. However, economic measures cannot begin to convey the medical revolution that is being effected by these first humanized and chimerized monoclonal antibodies. At this juncture, the 10 monoclonal antibody therapeutics in clinical use are of murine origin, of which 3 are entirely murine (OKT3, Mylotarg, 90Y-labeled Bexxar), 4 have been chimerized (human constant domains replacing murine) (ReoPro, Rituxan and its 131I-labeled analogue (Zevalin), Simulect, Remicade) and 3 were chimerized and humanized (human residues being substituted for at least some mouse-specific framework residues in VH and VL) (Zenapax, Herceptin, Synagis). Fully humanized anti-CD52 (CAMPATH-1H) has also been approved by the FDA for the treatment of B-cell chronic lymphocytic leukemia and should become available in late 2001. Humanization was initially developed by Dr. Greg Winter at the MRC Laboratory of Molecular Biology (Cambridge, UK), who presented the meeting's keynote address, "Antibodies as a Paradigm for Molecular Evolution". His pioneering work in antibody phage display libraries has been reformulated into a daring approach to develop truly novel proteins with genetically paired structural elements. He described studies in combinatorial protein engineering with enormous implications for both industrial and therapeutic applications of macromolecules.

100 Deals associated with Lexigen Pharmaceuticals Corp.

100 Translational Medicine associated with Lexigen Pharmaceuticals Corp.

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Pipeline

Pipeline Snapshot as of 24 Nov 2024

The statistics for drugs in the Pipeline is the current organization and its subsidiaries are counted as organizations,Early Phase 1 is incorporated into Phase 1, Phase 1/2 is incorporated into phase 2, and phase 2/3 is incorporated into phase 3

Phase 2 Clinical

Other

Current Projects

Drug(Targets)	Indications	Global Highest Phase

Lorukafusp alfa ( GD2 x IL-2R )	Neuroblastoma More	Phase 2
Cancer vaccine (Lexigen)	Colorectal Cancer More	Discontinued
Capravirine ( RT )	HIV Infections More	Discontinued
FP-21399 ( HIV envelope protein gp120 )	HIV Infections More	Pending

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