Pattathil S.,University of Georgia |
Avci U.,University of Georgia |
Baldwin D.,University of Georgia |
Swennes A.G.,University of Georgia |
And 20 more authors.
Plant Physiology | Year: 2010
A collection of 130 new plant cell wall glycan-directed monoclonal antibodies (mAbs) was generated with the aim of facilitating in-depth analysis of cell wall glycans. An enzyme-linked immunosorbent assay-based screen against a diverse panel of 54 plant polysaccharides was used to characterize the binding patterns of these new mAbs, together with 50 other previously generated mAbs, against plant cell wall glycans. Hierarchical clustering analysis was used to group these mAbs based on the polysaccharide recognition patterns observed. The mAb groupings in the resulting cladogram were further verified by immunolocalization studies in Arabidopsis (Arabidopsis thaliana) stems. The mAbs could be resolved into 19 clades of antibodies that recognize distinct epitopes present on all major classes of plant cell wall glycans, including arabinogalactans (both protein- and polysaccharide-linked), pectins (homogalacturonan, rhamnogalacturonan I), xyloglucans, xylans, mannans, and glucans. In most cases, multiple subclades of antibodies were observed to bind to each glycan class, suggesting that the mAbs in these subgroups recognize distinct epitopes present on the cell wall glycans. The epitopes recognized by many of the mAbs in the toolkit, particularly those recognizing arabinose- and/or galactose-containing structures, are present on more than one glycan class, consistent with the known structural diversity and complexity of plant cell wall glycans. Thus, these cell wall glycan-directed mAbs should be viewed and utilized as epitope-specific, rather than polymer-specific, probes. The current world-wide toolkit of approximately 180 glycan-directed antibodies from various laboratories provides a large and diverse set of probes for studies of plant cell wall structure, function, dynamics, and biosynthesis. © 2010 American Society of Plant Biologists. Source
Abeome Corporation | Date: 2012-04-16
Certain transgenic animals which are prone to the rapid cell division of their antibody-secreting cells have superior properties for the generation of monoclonal antibodies. Not only can their antibody producing cells can be made into hybridomas with superior growth to hybridomas from non-prone animals, but the antibody producing cells themselves can be cultured directly without cell fusion or further manipulation. Disclosed herein are methods of making monoclonal antibodies comprising exposing the transgenic animals disclosed herein to an antigen and extracting antigen-specific antibody secreting cells from the transgenic animal.
Agency: Department of Health and Human Services | Branch: | Program: SBIR | Phase: Phase I | Award Amount: 242.07K | Year: 2014
DESCRIPTION (provided by applicant): We have developed and completed a proof-of-principle on a new transgenic mouse model for comprehensive characterization of the antibody repertoire made in response to ovalbumin injection using surface antibody capture and next-generation DNA sequencing technologies. A more commercially valuable proof is now sought using a novel screening method with an emerging drug target for hypercholesterolemia, known as PCSK9. PUBLIC HEALTH RELEVANCE PUBLIC HEALTH RELEVANCE: Therapeutic and diagnostic applications of monoclonal antibodies (mAbs) offer a way to target treatments to specific proteins. However, monoclonal antibodies have traditionally been made using hybridoma technologies which only access a small fraction ofthe immune system. Abeome has developed a novel method of antibody discovery using next-generation DNA sequencing of the variable gene repertoire of antigen-specific antibody producing cells. Thus, the immediate goal for this Phase I project is to us
Abeome Corporation | Date: 2007-12-04
Shoreibah M.G.,Abeome Corporation |
Jackson C.L.,Abeome Corporation |
Price P.W.,Abeome Corporation |
Meagher R.,University of Georgia |
And 3 more authors.
Stem Cells and Development | Year: 2011
Hesca-2, a monoclonal antibody (mAb) IgM raised to the human embryonic stem cell (hESC) line BG-01v, binds with high affinity (nM) to the disaccharide epitope (Galβ1-3GlcNAc) on a glycan microarray. This epitope was expressed on pluripotent progenitor hESCs in culture, but not in various differentiated cells derived from hESC based on immunofluorescence microscopy. Hesca-2 stains a limited subset of cells in adult human tissues (eg, esophagus and breast). This mAb also crossreacts in immunofluorescence microscopy studies with several human ovarian cancer cell lines and is cytotoxic to them based on the release of cytosolic enzyme lactate dehydrogenase into the media. Hesca-2 immunohistochemically stained tissue from a number of human tumors, including ovary, breast, colon, and esophageal cancer. These data suggest that Hesca-2 recognizes a surface marker found both in stem cells and certain cancer cells. © 2011, Mary Ann Liebert, Inc. Source