Looking for breakthrough ideas for innovation challenges? Try Patsnap Eureka!

Method of producing a plurality of isolated antibodies to a plurality of cognate antigens

Inactive Publication Date: 2006-03-09
MONTECITO BIO SCI
View PDF2 Cites 137 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

However, this is a very time-consuming process requiring as much as 6-10 weeks to complete, depending on the complexity of the antigen mixture.
However, the disadvantage of such antibodies is that they are typically naive (i.e., non-immunocompetent) and therefore have a significantly lower binding affinity and are not as efficient or useful for binding experiments.

Method used

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
View more

Image

Smart Image Click on the blue labels to locate them in the text.
Viewing Examples
Smart Image
  • Method of producing a plurality of isolated antibodies to a plurality of cognate antigens
  • Method of producing a plurality of isolated antibodies to a plurality of cognate antigens

Examples

Experimental program
Comparison scheme
Effect test

Embodiment Construction

[0011] A high-throughput, one-step selection method for producing a plurality of antigen-specific antibodies has now been developed. The method of the invention is advantageous over the art in that a plurality or collection of antibodies can be produced in one step and said antibodies are antigen-specific, species-specific, and have a high affinity to their cognate antigens. The method of the invention involves binding a plurality of antibody-producing B-cells from a mammal to a plurality of cognate antigens; isolating each bound antibody-producing B-cell and cognate antigen; amplifying nucleic acid sequences encoding each antibody, or fragment thereof, from the B-cells; introducing each nucleic acid sequence encoding each antibody, or fragment thereof, into an expression system for expressing an antibody to produce a plurality of isolated antibodies to a plurality of cognate antigens. While recombinant technology is desirable, conventional hybridoma technology can also be employed....

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to View More

PUM

No PUM Login to View More

Abstract

The present invention relates to a method for producing high affinity antibodies that are antigen-specific. The method involves binding a plurality of antibody-producing B-cells from a mammal to a plurality of cognate antigens; sorting the bound antibody-producing B-cell and cognate antigen; amplifying nucleic acid sequences encoding each antibody, or fragment thereof, from the B-cells; and expressing the each antibody in a protein expression system. Antibodies produced in this manner are useful in diagnostic and therapeutic applications.

Description

INTRODUCTION [0001] This application claims the benefit of U.S. Provisional Application No. 60 / 608,526 filed Sep. 9, 2005, which is herein incorporated by reference in its entirety.BACKGROUND OF THE INVENTION [0002] Recent developments in antibody engineering and recombinant DNA technology have made it possible to generate recombinant antibodies with high specificity and affinity for theoretically any antigen by employing phage display technology and constructing very large repertoires of antibodies that are displayed on the surface of filamentous phage (Winter et. al., (1994) Ann. Rev. Immunol. 12:433-455). International patent application WO 92 / 18619 describes methods for producing a library of DNA molecules capable of expressing a fusion polypeptide on the surface of a filamentous phage particle (phagemids) and producing heterodimeric receptors such as antibodies, and T-cell receptors. [0003] These large repertoires of naive, immunocompetent, or synthetic antibody fragments are f...

Claims

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to View More

Application Information

Patent Timeline
no application Login to View More
IPC IPC(8): A61K39/395C12P21/06C12N5/06C07K16/44
CPCC07K16/00
Inventor GORLACH, JORN
Owner MONTECITO BIO SCI
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Patsnap Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Patsnap Eureka Blog
Learn More
PatSnap group products