Multiscale Structural Remodeling of Oleosins by Thermal Processing: Mechanisms and Implications for Allergenicity Modulation in Oilseed Crops.

Oleosins, the predominant structural proteins that stabilize plant oil bodies, are increasingly recognized as major allergens in oilseed crops. This review examines how thermal processing hierarchically remodels oleosin structure from primary sequence to quaternary assembly, integrating structural biology, thermodynamics, and immunology to establish a causal chain linking thermal energy input to immunological outcomes. Central to this framework is the identification of a "thermal vulnerability code" embedded within oleosins, comprising two universally conserved core elements-the proline-knot hydrogen network and hydrophobic clusters within the central hydrophobic domain-and a facultative third element, conserved disulfide bonds present in a subset of oleosins. Disruption of these elements shapes the trajectory of structural remodeling, leading either to allergenicity attenuation through the destruction of conformational epitopes or to allergenicity potentiation through the exposure of cryptic linear epitopes. This framework provides a molecular roadmap for precision thermal processing, offering actionable strategies for developing safer oilseed‑based foods and establishing a new paradigm for plant allergen mitigation.