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      Still SDAPing Along: 20 Years of the Structural Database of Allergenic Proteins

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          Abstract

          The introduction of plant extracts to mitigate the symptoms of “hay fever”, about a century ago, led to discoveries beginning sixty years ago on determining the sequences and eventually structures of allergenic proteins. As more proteins were cloned, there was a need to rapidly identify and categorize those with significant similarity to known allergens. The Structural Database of Allergenic Proteins (SDAP) was created at the beginning of the 21st century as the first cross-referenced website to allow rapid overview of the structures and sequences of allergenic proteins. SDAP provides a way to identify sequence and functional similarities between these proteins, despite the complex nomenclature system based on the Latin names of their different sources. A rapid FASTA search simplifies grouping allergens from the same structural or functional family. SDAP also provides an overview of the rapidly expanding literature on the sequence, structure and epitopes of allergenic proteins and a way to estimate the potential allergenicity of novel proteins based on rules provided by the IUIS. Twenty years and a pandemic later, the list of allergenic proteins and their attributes continues to grow. SDAP is expanding and improving to allow rapid access to all this information.

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          Most cited references39

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          SDAP: database and computational tools for allergenic proteins.

          SDAP (Structural Database of Allergenic Proteins) is a web server that provides rapid, cross-referenced access to the sequences, structures and IgE epitopes of allergenic proteins. The SDAP core is a series of CGI scripts that process the user queries, interrogate the database, perform various computations related to protein allergenic determinants and prepare the output HTML pages. The database component of SDAP contains information about the allergen name, source, sequence, structure, IgE epitopes and literature references and easy links to the major protein (PDB, SWISS-PROT/TrEMBL, PIR-ALN, NCBI Taxonomy Browser) and literature (PubMed, MEDLINE) on-line servers. The computational component in SDAP uses an original algorithm based on conserved properties of amino acid side chains to identify regions of known allergens similar to user-supplied peptides or selected from the SDAP database of IgE epitopes. This and other bioinformatics tools can be used to rapidly determine potential cross-reactivities between allergens and to screen novel proteins for the presence of IgE epitopes they may share with known allergens. SDAP is available via the World Wide Web at http://fermi.utmb.edu/SDAP/.
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            New quantitative descriptors of amino acids based on multidimensional scaling of a large number of physical?chemical properties

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              The importance of the 2S albumins for allergenicity and cross-reactivity of peanuts, tree nuts, and sesame seeds

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                Author and article information

                Contributors
                Journal
                Front Allergy
                Front Allergy
                Front. Allergy
                Frontiers in Allergy
                Frontiers Media S.A.
                2673-6101
                2673-6101
                22 March 2022
                2022
                : 3
                : 863172
                Affiliations
                [1] 1Department of Biochemistry and Molecular Biology, Institute for Human Infections and Immunity, University of Texas Medical Branch at Galveston , Galveston, TX, United States
                [2] 2Sealy Center for Structural Biology and Molecular Biophysics, University of Texas Medical Branch at Galveston , Galveston, TX, United States
                [3] 3Margaret Maccallum Gage and Tracy Davis Gage Professorship in Biochemistry and Allergies, University of Texas Medical Branch at Galveston , Galveston, TX, United States
                Author notes

                Edited by: Soheila June Maleki, Agricultural Research Service (USDA), United States

                Reviewed by: Philip Johnson, University of Nebraska-Lincoln, United States

                *Correspondence: Catherine H. Schein chschein@ 123456utmb.edu

                This article was submitted to Allergens, a section of the journal Frontiers in Allergy

                Article
                10.3389/falgy.2022.863172
                8974667
                35386653
                01e842fe-320c-4ce5-a11d-663b65a2153d
                Copyright © 2022 Schein, Negi and Braun.

                This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

                History
                : 26 January 2022
                : 28 February 2022
                Page count
                Figures: 1, Tables: 0, Equations: 0, References: 39, Pages: 5, Words: 3254
                Funding
                Funded by: National Institute of Allergy and Infectious Diseases, doi 10.13039/100000060;
                Categories
                Allergy
                Perspective

                allergenic protein nomenclature,sequence and structure,physicochemical property scale,ige epitopes,history of allergen studies,peanut and nut allergens,property distance scale,component resolved extracts

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