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Physical Characterization of the “Immunosignaturing Effect”
Identifying new, effective biomarkers for diseases is proving to be a challenging problem. We have proposed that antibodies may offer a solution to this problem. The physical features and abundance of antibodies make them ideal biomarkers. Additionally, antibodies are often elicited early in the ont...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Biochemistry and Molecular Biology
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3367934/ https://www.ncbi.nlm.nih.gov/pubmed/22261726 http://dx.doi.org/10.1074/mcp.M111.011593 |
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author | Stafford, Phillip Halperin, Rebecca Legutki, Joseph Bart Magee, Dewey Mitchell Galgiani, John Johnston, Stephen Albert |
author_facet | Stafford, Phillip Halperin, Rebecca Legutki, Joseph Bart Magee, Dewey Mitchell Galgiani, John Johnston, Stephen Albert |
author_sort | Stafford, Phillip |
collection | PubMed |
description | Identifying new, effective biomarkers for diseases is proving to be a challenging problem. We have proposed that antibodies may offer a solution to this problem. The physical features and abundance of antibodies make them ideal biomarkers. Additionally, antibodies are often elicited early in the ontogeny of different chronic and infectious diseases. We previously reported that antibodies from patients with infectious disease and separately those with Alzheimer's disease display a characteristic and reproducible “immunosignature” on a microarray of 10,000 random sequence peptides. Here we investigate the physical and chemical parameters underlying how immunosignaturing works. We first show that a variety of monoclonal and polyclonal antibodies raised against different classes of antigens produce distinct profiles on this microarray and the relative affinities are determined. A proposal for how antibodies bind the random sequences is tested. Sera from vaccinated mice and people suffering from a fugal infection are individually assayed to determine the complexity of signals that can be distinguished. Based on these results, we propose that this simple, general and inexpensive system could be optimized to generate a new class of antibody biomarkers for a wide variety of diseases. |
format | Online Article Text |
id | pubmed-3367934 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | The American Society for Biochemistry and Molecular Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-33679342012-06-07 Physical Characterization of the “Immunosignaturing Effect” Stafford, Phillip Halperin, Rebecca Legutki, Joseph Bart Magee, Dewey Mitchell Galgiani, John Johnston, Stephen Albert Mol Cell Proteomics Research Identifying new, effective biomarkers for diseases is proving to be a challenging problem. We have proposed that antibodies may offer a solution to this problem. The physical features and abundance of antibodies make them ideal biomarkers. Additionally, antibodies are often elicited early in the ontogeny of different chronic and infectious diseases. We previously reported that antibodies from patients with infectious disease and separately those with Alzheimer's disease display a characteristic and reproducible “immunosignature” on a microarray of 10,000 random sequence peptides. Here we investigate the physical and chemical parameters underlying how immunosignaturing works. We first show that a variety of monoclonal and polyclonal antibodies raised against different classes of antigens produce distinct profiles on this microarray and the relative affinities are determined. A proposal for how antibodies bind the random sequences is tested. Sera from vaccinated mice and people suffering from a fugal infection are individually assayed to determine the complexity of signals that can be distinguished. Based on these results, we propose that this simple, general and inexpensive system could be optimized to generate a new class of antibody biomarkers for a wide variety of diseases. The American Society for Biochemistry and Molecular Biology 2012-04 2012-01-18 /pmc/articles/PMC3367934/ /pubmed/22261726 http://dx.doi.org/10.1074/mcp.M111.011593 Text en © 2012 by The American Society for Biochemistry and Molecular Biology, Inc. Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/) applies to Author Choice Articles |
spellingShingle | Research Stafford, Phillip Halperin, Rebecca Legutki, Joseph Bart Magee, Dewey Mitchell Galgiani, John Johnston, Stephen Albert Physical Characterization of the “Immunosignaturing Effect” |
title | Physical Characterization of the “Immunosignaturing Effect” |
title_full | Physical Characterization of the “Immunosignaturing Effect” |
title_fullStr | Physical Characterization of the “Immunosignaturing Effect” |
title_full_unstemmed | Physical Characterization of the “Immunosignaturing Effect” |
title_short | Physical Characterization of the “Immunosignaturing Effect” |
title_sort | physical characterization of the “immunosignaturing effect” |
topic | Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3367934/ https://www.ncbi.nlm.nih.gov/pubmed/22261726 http://dx.doi.org/10.1074/mcp.M111.011593 |
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