Glycozym Aps

Velico Medical, Inc.

Cancer Research Technology Limited

Other

University of Copenhagen

Københavns Universitet

Go Therapeutics, Inc.

Novo Nordisk A/s

Danmarks Tekniske Universitet

The Brigham and Women's Hospital, Inc.

Neose Technologies, Inc.

The Biomembrane Institute

Zymequest, Inc.

Biogenerix Ag

Ratiopharm Gmbh

Henrik Clausen

Eric Bennett

Ulla Mandel

Tilo Schwientek

Eric Paul Bennett

Qiyong Peter Liu

Shawn DeFrees

Hans H Wandall

Mads Agervig Tarp

Joyce Taylor-Papadimitriou

Zhang Yang

Anne Louise Sørensen

Joy Burchell

David A Zopf

Thomas P Stossel

Keith Rosiello

John H Hartwig

Karin M Hoffmeister

Cheryl Hill

Rudi Steffensen

Margarida Amado

Johannes Wirenfeldt Vad Pedersen

Humberto De La Vega

Carsten Behrens

Zhi-Guang Wang

Adnan Fevzi Halim

Sergey Vakhrushev

Shamim Herbert Rahman

Weihua Tian

Claus Kristensen

Malene Bech Vester-Christensen

Caryn Bowe

Sen-itiroh Hakomori

Michael Felo

Peter Ulvskov

Ruye Xing

Walter Scott Willett

Susann Taudte

Fumi-ichiro Yamamoto

Thayer White

Bingyuan Wu

Johannes W Pedersen

Hans Heugh Wandall

Ulta Mandel

Helle Hassan

Celso Albuquerque Reis

Jochen G&auml;tgens

Detlef Eisenkr&auml;tzer

Frau Helle Hassan

Damian Paul Drew

Emma Adhiambo Arigi

John-Erik Stig Hansen

Steven B Levery

Brent Larsen Petersen

Walter S Willett

Marc Schwartz

The present invention relates to lysosomal enzymes modified by use of cell based methods, a compositions comprising a modified lysosomal enzyme, as well as methods for producing a modified lysosomal enzyme and therapeutic use of such modified lysosomal enzyme. In particular, the present disclosure relates to a modified lysosomal enzyme which has low Man6P and low exposed Mannose and high sialic acid content of alpha2,3 type enabling long circulation time and improved uptake into difficult-to-reach organs like heart, kidney and brain.

Lysosomal enzymes modified by cell based glycoengineering

The present inventors have demonstrated that circulating auto-antibodies to cancer antigens hold promise as specific and sensitive biomarkers for the early detection of cancer. The present invention thus relates to methods of detecting cancer in a sample, comprising utilising a glycopeptide bait derived from human mucins with different cancer-associated O-glycans. Detected antibodies were demonstrated as glycopeptide specific, and it could be discriminated between e.g. colorectal cancer patients and healthy individuals. The inventors have also developed monoclonal antibodies based on the identified glycopeptides epitope baits, and demonstrated differential expression of the relevant target antigens. The invention thus, in a lock and key-based manner includes both glycopeptides and antibody tools for early detection of cancer, as well as methods of using the same for in situ visualisation and treatment of specific cancer types.

CORE3-MUC1 binding polypeptides and uses thereof

Modified recombinant lysosomal alpha-galactosidase A and aspartylglucoaminidase having low mannose-6-phosphate and high sialic acid

Tn-MUC4 binding polypeptides and uses thereof

The present invention provides a method for inducing a cancer specific immune response against MUC1 using an immunogenic glycopeptide. Other aspects of the invention are a pharmaceutical composition comprising the immunogenic glycopeptide and a cancer vaccine comprising the immunogenic glycopeptide. Another aspect is an antibody generated using the immunogenic glycopeptide and the use of said antibody in therapy and diagnosis.

Generation of a cancer-specific immune response toward MUC1 and cancer specific MUC1 antibodies

The present invention relates to a cell comprising a gene encoding a polypeptide of interest, wherein the polypeptide of interest is expressed comprising one or more posttranslational modification patterns. These modifications are useful for example in improvement of pharmacokinetic properties, i.e. by attaching PEG chains to proteins. The present invention also relates to methods for producing the antibodies and compositions comprising the antibodies, and their uses.

Production of N-glycoproteins for enzyme assisted glycomodification

The present invention relates to a mammalian cell comprising a gene encoding a polypeptide of interest, wherein the polypeptide of interest is expressed comprising one or more posttranslational modification patterns. These modifications are useful for example in glycoprotein production where the antibodies with the modifications have an enhanced antibody-dependent cell-mediated cytotoxicity (ADCC). The present invention also relates to methods for producing the glycoproteins and compositions comprising the glycoproteins, and their uses.

N-glycosylation

The present inventors have demonstrated that circulating auto-antibodies to cancer antigens hold promise as specific and sensitive biomarkers for the early detection of cancer. The present invention thus relates to methods of detecting cancer in a sample, comprising utilizing a glycopeptide bait derived from human mucins with different cancer-associated O-glycans. Detected antibodies were demonstrated as glycopeptide specific, and it could be discriminated between e.g. colorectal cancer patients and healthy individuals. The inventors have also developed monoclonal antibodies based on the identified glycopeptides epitope baits, and demonstrated differential expression of the relevant target antigens. The invention thus, in a lock and key-based manner includes both glycopeptides and antibody tools for early detection of cancer, as well as methods of using the same for in situ visualization and treatment of specific cancer types.

Method for early detection of cancer

This invention relates to novel &#x3b1;-galactosidases for the enzymatic removal of the immunodominant monosaccharides on blood products and tissues. Specifically this invention provides a novel family of &#x3b1;3 glycosidases, used for the enzymatic removal of type B antigens from blood group B and AB reactive blood products, and the Galili antigen from non-human animal tissues, thereby converting these to non-immunogenic cells and tissues suitable for transplantation.

Methods of preparing tissues for xenotransplantation using alpha-galactosidases

The invention relates to methods of preparing and purifying conjugates between Granulocyte Colony Stimulating Factor and PEG moieties. The conjugates are linked via an intact glycosyl linking group that is interposed between and covalently attached to the peptide and the modifying group. The conjugates are purified using various chromatography methods.

Glycopegylated granulocyte colony stimulating factor

This invention discloses the development of a novel platform for recombinant production of bioactive glycoproteins and cancer specific vaccines in plants. Plants and plant cell cultures have been humanized with respect to human mucin-type protein O-glycosylation. A panel of plant cell factories for production of recombinant glycoproteins with designed human O-glycosylation, including an improved cancer vaccine candidate, has been developed. The platform provides basis for i) production of an essentially unlimited array of O-glycosylated human glycoprotein therapeutics, such as human interferon &#x3b1;2B and podoplanin, and ii) for further engineering of additional cancer specific O-glycans on glycoproteins of therapeutical value. Currently, mammalian cells are required for human O-glycosylation, but plants offer a unique cell platform for engineering O-glycosylation since they do not perform human type O-glycosylation. Introduction of O-glycosylation into plant cells requires i) that wild-type plant cells do not modify the target peptide substrates and ii) that the appropriate enzymes and substrates are introduced into of plant cells such that O-glycosylation in the secretory pathway proceed and the glycosylated peptide substrates are preferentially exported to the exterior of the cell or accumulated in the cell. In this invention i) the integrity of transiently and stably expressed 'mucin' type target peptides in plants cells has been determined and ii) mucin-type O-glycosylation has been established in plants by transient and stable introduction of aC4-epimerase, the human polypeptide GalNAc-transferases T2 and T4 (GalNAc-T2 and T4) and various human target peptides or proteins. In the present invention GalNAc-T2 and -T4 have been used to produce a Tn cancer glycoform of MUC1.

Methods for glyco-engineering plant cells for controlled human O-glycosylation

Growing community of inventors

Holte, Denmark

Henrik Clausen