Dana A Gebhart

20110293566, Dec 1, 2011

May 27, 2011

13/117467

Dean M. SCHOLL - Burlingame CA, US
Dana M. Gebhart - San Francisco CA, US
Steven R. Williams - San Francisco CA, US
Gregory R. Govoni - San Carlos CA, US
David W. Martin, JR. - Mill Valley CA, US

AvidBiotics Corp. - South San Francisco CA

A61K 38/16
C07K 14/33
C12P 21/02
A61K 35/00
C12N 15/74
C12N 1/21
C07H 21/04
A61P 31/04

424 932, 536 237, 530350, 530324, 514 24, 4353201, 4352523, 43525231, 435 691

This disclosure relates to the discovery and isolation of the entire cluster of genes encoding R-type high molecular weight bacteriocins that specifically kill bacteria, dangerous human pathogens. Also disclosed are methods of producing the R-type bacteriocins in innocuous producer cells that, unlike , do not die in the presence of oxygen. Disclosed also is the specific gene of the isolated gene cluster that determines the killing spectrum of the R-type bacteriocin and the demonstration that the killing spectra of diffocins can be altered by engineering orf1374 of the diffocin genetic locus. This invention offers a potent bactericidal agent and a means to make it in order to kill selectively bacteria in the environment of the gastrointestinal tract where they can cause great harm and even death of the infected patient or farm animal.

20130203652, Aug 8, 2013

Mar 14, 2013

13/829725

Dana M. Gebhart - San Francisco CA, US
Dean M. Scholl - Burlingame CA, US

AvidBiotics Corp. - South San Francisco CA

C12N 15/11
C07K 14/33

514 24, 536 237, 4353201, 530350, 435 691

This disclosure relates to the discovery and isolation of the entire cluster of genes encoding R-type high molecular weight bacteriocins that specifically kill bacteria, dangerous pathogens. Also disclosed are methods of producing the R-type bacteriocins in innocuous aerobic producer cells. Disclosed also are small, non-ORF1374 receptor binding domains (RBDs), which are incorporated into diffocins to form engineered or variant diffocins having altered killing spectra. Variant diffocins provided herein may include a heterologous RBD and its cognate base plate attachment region (BPAR), or a fused BPAR. This invention offers a potent bactericidal agent with increased thermal and pH stability, and methods for producing it, in order to kill selectively bacteria in the environment of the gastrointestinal tract where they can cause great harm and even death of the infected patient or farm animal.

20080286236, Nov 20, 2008

May 14, 2007

11/748437

Dana M. Gebhart - San Francisco CA, US
Dean M. Scholl - South San Francisco CA, US

AvidBiotics Corporation - South San Francisco CA

A61K 35/74
A01N 63/02
A61P 31/04
G01N 33/569
C12Q 1/04
A01P 1/00

424 932, 424780, 424 936, 435 34, 435 732

The disclosure relates to the targeting of mediated by the binding activity of tail fibers from naturally occurring R-type pyocins from . The targeting may be mediated by a macromolecular complex such as the pyocin itself, a high molecular weight (hmw) bacteriocin modified to have the tail fiber's binding activity, or a bacteriophage modified to have the tail fiber's binding activity. Compositions comprising such complexes are described. Also disclosed are methods for the use of a complex, such as to inhibit the growth of a species like , by compromising the integrity of its cytoplasmic membrane are also described. Additional methods include use of the binding activity to identify

20160304578, Oct 20, 2016

Jun 24, 2016

15/192400

- South San Francisco CA, US
Daniel P. STEIGER - San Francisco CA, US
Steven R. WILLIAMS - San Francisco CA, US
David W. MARTIN, JR. - Mill Valley CA, US
Dana GEBHART - San Francisco CA, US
Tarah BARON - Daly City CA, US

AvidBiotics Corp. - South San Francisco CA

C07K 14/705
C07K 16/32
C07K 16/28

This application relates generally to the production of polypeptides having specific antigen-binding properties of Fv domains, for example, insertable variable fragments of antibodies, and modified α1-α2 domains of NKG2D ligands. This application further relates to modified α1-α2 domains of NKG2D ligands attached to polypeptides, in some embodiments antibodies or fragments of antibodies. This application further relates to antigen-binding peptides derived from light and heavy chain antibody variable domains, which contain two linker regions and a split variable domain.