TY  - JOUR
AU  - Gómez-Velasco, Homero
AU  - García-Ramírez, Benjamín
AU  - Siliqi, Dritan
AU  - Graewert, Melissa A.
AU  - Quintero-Martinez, Adrián
AU  - Ortega, Enrique
AU  - Rodríguez-Romero, Adela
TI  - Allergen-induced structural rearrangements in IgE: insights from SAXS and molecular dynamics
JO  - International journal of biological macromolecules
VL  - 328
SN  - 0141-8130
CY  - New York, NY [u.a.]
PB  - Elsevier
M1  - PUBDB-2025-04015
SP  - 147658 -
PY  - 2025
AB  - The initiation of allergic responses critically depends on the recognition of an allergenic epitope by the paratope of IgE antibodies. While previous structural studies have focused on recombinant fragments or engineered forms of IgE, the structure of full-length IgE in its native state remains poorly understood. In this study, we investigate the conformational changes of a native murine IgE (2F5), both in its free form and upon binding to the Hevea brasiliensis allergen profilin (Hev b 8). Small-angle X-ray scattering (SAXS) data reveal that unbound IgE adopts an extended conformation with open Fab arms. However, when it binds to profilin, it transitions to a more compact arrangement characterized by closer proximity of the arms. Molecular dynamics (MD) simulations of the Fab region further identified conformational rearrangements upon allergen binding, including a twisting motion and partial disruption of interactions between the naturally paired heavy and light chains. These findings indicate that there may be allosteric communication between Fab and Fc regions, even in the absence of a hinge region, which is not present in IgE. Overall, this study provides valuable insights into the dynamic structural properties of native IgE and enhances our understanding of the molecular mechanisms underlying allergen recognition.
LB  - PUB:(DE-HGF)16
DO  - DOI:10.1016/j.ijbiomac.2025.147658
UR  - https://bib-pubdb1.desy.de/record/638197
ER  -