Vrije Universiteit Brussel

Conopco, Inc.

Bac IP B.v.

Vrije Universiteit

Raymond Hamers

Cecile Casterman

Cornelis T Verrips

Cecile Hamers-Casterman

Leon G J Frenken

Serge Muyldermans

Serge V M Muyldermans

Serge Vm Muyldermans

Cécile Casterman

A process is provided for the production of an antibody or a fragment or functionalized fragment thereof using a transformed lower eukaryotic host containing an example DNA sequence encoding the antibody or (functionalized) fragment thereof, wherein the antibody or (functionalized) fragment thereof is derived from a heavy chain immunoglobulin of Camelidae and is devoid of light chains, and wherein the lower eukaryotic host is a mould, preferably belonging to the generaor, or a yeast, preferably belonging to the yeast genera, or. The heavy chain fragment can contain at least the whole variable domain. A complementary determining region (CDR) different from the CDR belonging to the natural antibody ex Camelidae can be grafted on the framework of the variable domain of the heavy chain immunoglobulin. The catalytic antibodies can be raised in Camelidae against transition state molecules. The functionalized antibody or fragment thereof can comprise a fusion protein of both a heavy chain immunoglobulin from Camelidae or a fragment thereof and another polypeptide, e.g., an enzyme, preferably an oxido-reductase. Also provided are new products obtainable by a process as described, and compositions containing a product produced by a process as described, which composition may contain a new product as provided.

Prosuction of antibodies or (functionalized) fragments thereof derived from heavy chain immunoglobulins of camelidae

There are provided methods for screening a library of Vpolypeptides for Vpolypeptides that bind to an antigen including subjecting a library of Vpolypeptides to antigen-affinity selection with the antigen.

Method for screening a library of VHH polypeptides

The invention relates to an immunoglobulin having determined antigen specificity, and having a variable fragment which is derived from a so-called heavy-chain immunoglobulin having two heavy polypeptide chains capable of recognizing and binding one or several antigens and which is further naturally devoid of light chains, wherein the immunoglobulin having determined antigen specificity is devoid of CH1 constant region between the variable region and the hinge region and has within its constant region at least part of a constant region of a human antibody.

Immunoglobulins devoid of light chains

The invention relates to an immunoglobulin having determined antigen specificity, and having a variable fragment which is obtainable from a camelid heavy-chain immunoglobulin having two heavy polypeptide chains capable of recognizing and binding an antigen and which is further devoid of polypeptide light chains, wherein the immunoglobulin having determined antigen specificity is devoid of a CH1 constant region between the variable region and the hinge region and has within its constant region at least part of a constant region of a human antibody.

The present invention relates to fragments, especially variable fragments of immunoglobulins which are by nature devoid of light chains, these fragments being nevertheless capable of exhibiting a recognition and binding activity toward specific antigens. The present invention further relates to the use of such immunoglobulin fragments formed of at least one heavy chain variable fragment or derived therefrom, for therapeutic or veterinary purposes and especially for passive immunotherapy or serotherapy.

Recombinant bivalent monospecific immunoglobulin having at least two variable fragments of heavy chains of an immunoglobulin devoid of light chains

A process is provided for the production of an antibody or a fragment or functionalized fragment thereof using a transformed lower eukaryotic host containing an expressible DNA sequence encoding the antibody or (functionalized) fragment thereof, wherein the antibody or (functionalized) fragment thereof is derived from a heavy chain immunoglobulin ofand is devoid of light chains, and wherein the lower eukaryotic host is a mould, preferably belonging to the generaoror a yeast, preferably belonging to the yeast genera. The heavy chain fragment can contain at least the whole variable domain. A complementary determining region (CDR) different from the CDR belonging to the natural antibody excan be grafted on the framework of the variable domain of the heavy chain immunoglobulin. The catalytic antibodies can be raised inagainst transition state molecules. The functionalized antibody or fragment thereof can comprise a fusion protein of both heavy chain immunoglobulin fromor a fragment thereof and another polypeptide, e.g., an enzyme, preferably an oxido-reductase. Also provided are new products obtainable by a process as described, and compositions containing a product produced by a process as described, which composition may contain a new product as provided.

Production of antibodies or (functionalized) fragments thereof derived from heavy chain immunoglobulins of camelidae

There is provided an isolated immunoglobulin comprising two heavy polypeptide chains sufficient for the formation of a complete antigen binding site or several antigen binding sites, wherein the immunoglobulin is further devoid of light polypeptide chains.

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Sint-Genesius-Rode, Belgium

Raymond Hamers