The Scripps Research Institute

Syngenta Participations Ag

Other

Novartis Ag

University of Pennsylvania

Carlos F Barbas, Iii

Richard A Lerner

Dennis R Burton

Christoph Rader

Roger Renzo Beerli

Brian R Murphy

Robert M Chanock

Xueni Guan

Justin Stege

Joel M Gottesfeld

James E Crowe, Jr

Bipin Dalmia

Brian M Lamb

Andrew Mercer

Thomas Gaj

Peter E Wright

Juergen Wagner

Lloyd J Old

Gerd J Ritter

Sydney Welt

Angray Singh Kang

Guofu Zhong

Benjamin List

Birgit Dreier

Michael Joseph Kadan

Ulrich Schopfer

Donald L Siegel

Doron Shabat

Subhash C Sinha

Jonathan Rosenblum

Hitoshi Ban

Julia Gavrilyuk

Russell M Gordley

Disclosed herein are chimeric polypeptides, including compositions thereof, expression vectors, and methods of use thereof, for the generation of transgenic cells, tissues, plants, and animals. The compositions, vectors, and methods of the present invention are also useful in gene therapy techniques.

Chimeric polypeptides having targeted binding specificity

The present invention provides antibodies containing one or more modular recognition domains (MRDs) for targeting the antibodies to specific sites. The use of the antibodies containing one or more modular recognition domains to treat disease, and methods of making antibodies containing one or more modular recognition domains are also provided in the invention.

Antibody targeting through a modular recognition domain

Disclosed herein are chimeric polypeptides, including compositions thereof, expression vectors, and methods of use thereof, for the generation of transgenic cells, tissues, plants, and animals. The compositions, vectors, and methods of the present invention are also useful in gene therapy techniques. The invention provides a chimeric polypeptide. The polypeptide includes: a) a recombinase, nuclease or transcription factor, or fragment thereof; and b) a transcription activator-like effector (TALE) protein.

The present invention relates to novel methods for detecting a member of a known binding pair in a sample, including a cell, where one member of the pair (termed the 'receptor') is expressed by a bacteriophage, which phage is then used to detect the presence of the other member of the pair (termed the 'ligand' or &#x201c;target&#x201d;). Rather than detecting the binding of the phage using antibody-based technology, the present invention relates to detecting marker molecule associated with the phage. In one aspect, the invention relates to identifying an antigen-bearing moiety (e.g., a red blood cell antigen) of interest present on a cell, e.g., a red blood cell, using antibody-displaying bacteriophage, as well as detecting anti-red blood cell auto- or alloantibodies and/or complement in a sample, using antiglobulin reagent-displaying bacteriophage and detecting a marker molecule associated with the phage. In one aspect, the phenotype of the phage is not linked with the genotype of the phage.

Phage particle diagnostic reagents

Provided herein is a method for chemically programmed vaccination. Methods include inducing a covalent-binding polyclonal antibody response in a subject and programming the polyclonal response with a targeting compound.

Chemically Programmed Vaccination

A new and versatile class of cyclic diazodicarboxamides that reacts efficiently and selectively with phenols and the phenolic side chain of tyrosine through an Ene-like reaction is reported. This mild aqueous tyrosine ligation reaction works over a broad pH range and expands the repertoire of aqueous chemistries available for small molecule, peptide, and protein modification. The tyrosine ligation reactions are shown to be compatible with the labeling of native enzymes and antibodies in buffered aqueous solution. This reaction provides a novel synthetic approach to bispecific antibodies. This reaction will find broad utility in peptide and protein chemistry and in the chemistry of phenol-containing compounds. 

Tyrosine bioconjugation through aqueous Ene-like reactions

The present invention is directed to chimeric recombinases comprising a serine recombinase operatively linked to a zinc finger nucleotide binding domain such that the chimeric recombinase protein catalyzes site-specific recombination at a DNA site specifically bound by the zinc finger nucleotide binding domain. The serine recombinase can be one of several naturally occurring serine recombinases. The invention also includes nucleic acids encoding the chimeric recombinases, vectors including the nucleic acids, host cells transformed or transfected with the vectors, methods of using the chimeric recombinases to carry out recombination, methods of using substrate-linked protein evolution to generate additional chimeric recombinases, methods of using the chimeric recombinases for gene therapy, and pharmaceutical compositions.

Chimeric zinc finger recombinases optimized for catalysis by directed evolution

Antibodies containing one or more modular recognition domains (MRDs) that can be used to target the antibodies to specific sites are described. The use of antibodies containing one or more modular recognition domains to treat disease, and methods of making antibodies containing one or more modular recognition domains are also described.

VEGF antibodies comprising modular recognition domains

EFGR antibodies comprising modular recognition domains

ERBB2 antibodies comprising modular recognition domains

Chemically programmed vaccination

Multispecific antibody targeting and multivalency through modular recognition domains

The present invention provides antibody targeting compounds in which the specificity of the antibody has been reprogrammed by covalently or noncovalently linking a targeting agent to the combining site of an antibody. By this approach, the covalently modified antibody takes on the binding specificity of the targeting agent. The compound may have biological activity provided by the targeting agent or by a separate biological agent. Various uses of the invention compounds are provided.

Antibody targeting compounds

Filamentous phage comprising a matrix of cpVIII proteins encapsulating a genome encoding first and second polypeptides of an antogenously assembling receptor, such as an antibody, and a receptor comprised of the first and second polypeptides surface-integrated into the matrix via a filamentous phage coat protein membrane anchor domain fused to at least one of the polypeptides.

Heterodimeric receptor libraries using phagemids

Growing community of inventors

Solana Beach, CA, United States of America

Carlos F Barbas, Iii