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ARS Home » Southeast Area » New Orleans, Louisiana » Southern Regional Research Center » Food Processing and Sensory Quality Research » Research » Publications at this Location » Publication #428779
Research Project: Enhancing Marketability and Ensuring Safety for Peanut and Tree Nut Consumers

Location: Food Processing and Sensory Quality Research

Title: Structural analysis of 8-anilino-1-naphthalene sulfonate (ANS) binding to the PR-10 allergen Ara h 8

Author
item O’MALLEY, ANDREA - Michigan State University
item OFFERMANN, LESA - University Of South Carolina
item KHATRI, KRITI - Michigan State University
item LINN, CHRISTINA - Michigan State University
item POTE, SWANANDI - University Of South Carolina
item McBride, Jane
item PERDUE, MAKENZIE - Michigan State University
item Hurlburt, Barry
item Maleki, Soheila
item MIAS, GEORGE - Michigan State University
item CHRUSZCZ, MAKSYMILIAN - Michigan State University

Submitted to: Biochemical and Biophysical Research Communications
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 11/17/2025
Publication Date: 11/18/2025
Citation: O’Malley, A., Offermann, L.R., Khatri, K., Linn, C., Pote, S., Mcbride, J.K., Perdue, M.L., Hurlburt, B.K., Maleki, S.J., Mias, G.I., Chruszcz, M. 2025. Structural analysis of 8-anilino-1-naphthalene sulfonate (ANS) binding to the PR-10 allergen Ara h 8. Biochemical and Biophysical Research Communications. https://doi.org/10.1016/j.bbrc.2025.153013.
DOI: https://doi.org/10.1016/j.bbrc.2025.153013

Interpretive Summary: In our earlier work, we studied the peanut allergen called Ara h 8.0101, looking at its crystal structure when it wasn’t attached to anything (apo form) and when it was bound to certain model substances. These studies showed how well Ara h 8 can bind different types of substances and its similarities to another major allergen called Bet v 1. In this study, we took it a step further by examining two different forms of Ara h 8—Ara h 8.0101 and Ara h 8.0201—when they were bound to a specific molecule called 8-anilino-1-naphthalene sulfonate (ANS). We also looked at Ara h 8.0201 in its apo form. To understand how ANS affects how Ara h 8.0101 and Ara h 8.0201 bind other substances, we did some experiments using fluorescence. We compared our findings to the allergen Bet v 1.0101. Since ANS is often used in tests to see how well substances bind, we also looked at various studies to summarize the binding sites for ANS from a protein database.

Technical Abstract: We previously determined crystal structures of peanut allergen Ara h 8.0101 in the apo form and in complex with model ligands. These structures illustrated the varied ligand binding capabilities of PR-10s and Ara h 8’s structural similarity to major birch allergen Bet v 1. Here, we expanded on those structural studies with structures of Ara h 8.0101 and Ara h 8.0201 in complex with 8-anilino-1-naphthalene sulfonate (ANS), as well as the apo form of Ara h 8.0201. We also examined the impact of ANS on the ligand binding cavities of Ara h 8.0101 and Ara h 8.0201 with fluorescence assays, comparing the results to prototypic PR-10 Bet v 1.0101. Moreover, as ANS is often used in fluorescence-based ligand binding assays, we analyzed structures from the PDB and provided a summary on experimentally determined ANS binding sites.