Elizabeth A Ward

US Patent:

6399368, Jun 4, 2002

Filed:

Dec 9, 1994

Appl. No.:

08/353940

Inventors:

Elizabeth S. Ward - Dallas TX

Assignee:

Board of Regents, The University of Texas System - Austin TX

International Classification:

C12N 1513

US Classification:

4353201, 435 6, 435 711, 435170, 4352528, 4352523, 536 241, 536 253

Abstract:

Variable domain murine T-cell receptor genes have been isolated and used to construct cloning and expression vectors. V , V and single chain V -V fragments have been expressed as secreted domains in using the vectors. The domains are secreted into the culture supernatant in milligram quantities. The single domains and the single chain T-cell receptors are folded into -pleated sheet structures similar to those of immunoglobulin variable domains. The secreted fragments may be useful for immunization to generate anti-clonotypic antibodies, in vaccination or for high resolution structural studies. The genes encoding these domains may also serve as templates for in vitro mutagenesis and improvement of affinities of the TCR fragments for their interaction with cognate peptide-MHC complexes.

US Patent:

6623957, Sep 23, 2003

Filed:

Jun 4, 2002

Appl. No.:

10/162127

Inventors:

Elizabeth S. Ward - Dallas TX

Assignee:

Board of Regents University of Texas System - Austin TX

International Classification:

C12P 2104

US Classification:

4353201, 435 6, 435 701, 435 703, 435 711, 435 914, 536 241

Abstract:

Variable domain murine T-cell receptor genes have been isolated and used to construct cloning and expression vectors. V , V , and single chain V -V fragments have been expressed as secreted domains in using the vectors. The domains are secreted into the culture supernatant in milligram quantities. The single domains and the single chain T-cell receptors are folded into -pleated sheet structures similar to those of immunoglobulin variable domains. The secreted fragments may be useful for immunization to generate anti-clonotypic antibodies, in vaccination or for high resolution structural studies. The genes encoding these domains may also serve as templates for in vitro mutagenesis and improvement of affinities of the TCR fragments for their interaction with cognate peptide-MHC complexes.

US Patent:

6821505, Nov 23, 2004

Filed:

Aug 20, 2001

Appl. No.:

09/933497

Inventors:

Elizabeth Sally Ward - Dallas TX

Assignee:

Board of Regents, The University of Texas System - Austin TX

International Classification:

A61K 39395

US Classification:

424 91, 424 92, 4241331, 435 721, 5303873

Abstract:

Disclosed are recombinant vectors encoding immunoglobulin-like domains and portions thereof, such as antibody Fc-hinge fragments, subfragments and mutant domains with extended biological half lives. Methods of producing large quantities of such domains, heterodimers, and fusion proteins following expression by host cells are also reported. Described are antibody Fc and Fc-hinge domains, which have the same in vivo stability as intact antibodies; and domains engineered to have increased in vivo half lives. These DNA constructs and protein domains will be useful as templates for in vitro mutagenesis and high resolution structural studies; for immunization and vaccination; and for the production of recombinant antibodies or chimeric proteins with increased stability and longevity for therapeutic and diagnostic uses.

US Patent:

8475792, Jul 2, 2013

Filed:

Oct 24, 2012

Appl. No.:

13/659144

Inventors:

Elizabeth Sally Ward Ober - Dallas TX, US

Assignee:

MedImmune, LLC - Gaithersburg MD
Board of Regents, The Texas University System - Austin TX

International Classification:

A61K 39/395
C07K 16/00
C12P 21/08
C12N 1/00

US Classification:

4241301, 435810, 5303871, 5303877, 5303879

Abstract:

The present invention provides molecules, including IgGs, non-IgG immunoglobulins, proteins and non-protein agents, that have increased in vivo half-lives due to the presence of an IgG constant domain, or a portion thereof that binds the FcRn, having one or more amino acid modifications that increase the affinity of the constant domain or fragment for FcRn. Such proteins and molecules with increased half-lives have the advantage that smaller amounts and or less frequent dosing is required in the therapeutic, prophylactic or diagnostic use of such molecules.

US Patent:

20080299618, Dec 4, 2008

Filed:

May 27, 2008

Appl. No.:

12/127237

Inventors:

Gregory P. WINTER - Cambridge, GB
Elizabeth S. Ward - Dallas TX, US
Detlef Gussow - London, GB

Assignee:

MEDICAL RESEARCH COUNCIL - LONDON

International Classification:

C12P 21/04
C07K 16/00
C07K 16/28
C07H 21/00
C07K 17/00
C12P 19/34

US Classification:

435 697, 5303871, 5303911, 5303913, 5303873, 435 912, 536 2433

Abstract:

The present invention relates to single domain ligands derived from molecules in the immunoglobulin (Ig) superfamily, receptors comprising at least one such ligand, methods for cloning, amplifying and expressing DNA sequences encoding such ligands, preferably using the polymerase chain reaction, methods for the use of said DNA sequences in the productions of Ig-type molecules and said ligands or receptors, and the use of said ligand or receptors in therapy, diagnosis or catalysis.

US Patent:

20130272964, Oct 17, 2013

Filed:

May 20, 2013

Appl. No.:

13/898042

Inventors:

ELIZABETH SALLY WARD OBER - DALLAS TX, US

International Classification:

C07K 16/28

US Classification:

424 91, 5303873, 5303911, 4241331, 536 2353, 43525233, 43525231, 43525421, 43525423, 435419, 435328

Abstract:

The present invention provides molecules, including IgGs, non-IgG immunoglobulins, proteins and non-protein agents, that have increased in vivo half-lives due to the presence of an IgG constant domain, or a portion thereof that binds the FcRn, having one or more amino acid modifications that increase the affinity of the constant domain or fragment for FcRn. Such proteins and molecules with increased half-lives have the advantage that smaller amounts and or less frequent dosing is required in the therapeutic, prophylactic or diagnostic use of such molecules.

US Patent:

62773755, Aug 21, 2001

Filed:

Mar 3, 1997

Appl. No.:

8/811463

Inventors:

Elizabeth Sally Ward - Dallas TX

Assignee:

Board of Regents, The University of Texas System - Austin TX

International Classification:

A61K 39395
C07K 1600

US Classification:

4241331

Abstract:

Disclosed are recombinant vectors encoding immunoglobulin-like domains and portions thereof, such as antibody Fc-hinge fragments, subfragments and mutant domains with extended biological half lives. Methods of producing large quantities of such domains, heterodimers, and fusion proteins following expression by host cells are also reported. Described are antibody Fc and Fc-hinge domains, which have the same in vivo stability as intact antibodies; and domains engineered to have increased in vivo half lives. These DNA constructs and protein domains will be useful as templates for in vitro mutagenesis and high resolution structural studies; for immunization and vaccination; and for the production of recombinant antibodies or chimeric proteins with increased stability and longevity for therapeutic and diagnostic uses.

US Patent:

20140377181, Dec 25, 2014

Filed:

Jun 20, 2014

Appl. No.:

14/310507

Inventors:

- Gaithersburg MD, US
- Austin TX, US
Elizabeth Sally Ward Ober - Dallas TX, US

Assignee:

BOARD OF REGENTS, THE UNIVERSITY OF TEXAS SYSTEM - Austin TX
MEDIMMUNE, LLC - Gaithersburg MD

International Classification:

C07K 16/28
A61K 49/00
C07K 2/00

US Classification:

424 91, 5303896, 5303873, 4241331, 536 2353, 4241731, 435328

Abstract:

The present invention provides molecules, including IgGs, non-IgG immunoglobulins, proteins and non-protein agents, that have increased in vivo half-lives due to the presence of an IgG constant domain, or a portion thereof that binds the FcRn, having one or more amino acid modifications that increase the affinity of the constant domain or fragment for FcRn. Such proteins and molecules with increased half-lives have the advantage that smaller amounts and or less frequent dosing is required in the therapeutic, prophylactic or diagnostic use of such molecules.