Journal article
Development of recombinant Aleuria aurantia lectins with altered binding specificities to fucosylated glycans
Biochemical and biophysical research communications, v 414(1), pp 84-89
14 Oct 2011
PMID: 21945439
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
► Linkage specific changes in fucosylation have been associated with cancer. ► The Aleuria aurantia lectin (AAL) can bind fucose but has limited linkage specificity. ► Through site-directed mutagenesis we developed AALs with altered binding affinities. ► These AAL molecules could be used to determine fucose changes in cancer.
Changes in glycosylation have long been associated with disease. While there are many methods to detect changes in glycosylation, plant derived lectins are often used to determine changes on specific proteins or molecules of interest. One change in glycosylation that has been observed by us and by others is a disease or antigen associated increase in fucosylation on N-linked glycans. To measure this change, the fucose binding Aleuria aurantia lectin (AAL) is often utilized in plate and solution based assays. AAL is a mushroom derived lectin that contains five fucose binding sites that preferentially bind fucose linked (α-1,3, α-1,2, α-,4, and α-1,6) to N-acetyllactosamine related structures. Recently, several reports by us and by others have indicated that specific fucose linkages found on certain serum biomarker glycoprotein’s are more associated with disease than others. Taking a site-directed mutagenesis approach, we have created a set of recombinant AAL proteins that display altered binding affinities to different analytes containing various fucose linkages.
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Details
- Title
- Development of recombinant Aleuria aurantia lectins with altered binding specificities to fucosylated glycans
- Creators
- Patrick R Romano - Drexel University College of Medicine, Department of Microbiology and Immunology and Drexel Institute for Biotechnology and Virology, 3805 Old Easton Avenue, Doylestown, PA 18901, USAAndrew Mackay - Institute for Hepatitis and Virus Research, 3805 Old Easton Avenue, Doylestown, PA 18901, USAMinh Vong - Institute for Hepatitis and Virus Research, 3805 Old Easton Avenue, Doylestown, PA 18901, USAJohann deSa - Drexel University, School of Biomedical Engineering, Science & Health Systems, Philadelphia, PA 19104, USAAnne Lamontagne - Drexel University College of Medicine, Department of Microbiology and Immunology and Drexel Institute for Biotechnology and Virology, 3805 Old Easton Avenue, Doylestown, PA 18901, USAMary Ann Comunale - Drexel University College of Medicine, Department of Microbiology and Immunology and Drexel Institute for Biotechnology and Virology, 3805 Old Easton Avenue, Doylestown, PA 18901, USAJulie Hafner - Immunotope, Inc., 3805 Old Easton Road, Doylestown, PA 18901, USATimothy Block - Drexel University College of Medicine, Department of Microbiology and Immunology and Drexel Institute for Biotechnology and Virology, 3805 Old Easton Avenue, Doylestown, PA 18901, USARyszard Lec - Drexel University, School of Biomedical Engineering, Science & Health Systems, Philadelphia, PA 19104, USAAnand Mehta - Drexel University College of Medicine, Department of Microbiology and Immunology and Drexel Institute for Biotechnology and Virology, 3805 Old Easton Avenue, Doylestown, PA 18901, USA
- Publication Details
- Biochemical and biophysical research communications, v 414(1), pp 84-89
- Publisher
- Elsevier
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Microbiology and Immunology; School of Biomedical Engineering, Science, and Health Systems
- Web of Science ID
- WOS:000296215200016
- Scopus ID
- 2-s2.0-80054076675
- Other Identifier
- 991014878036204721
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- Web of Science research areas
- Biochemistry & Molecular Biology
- Biophysics