Enhanced immunomodulatory properties of ovalbumin through transglutaminase and tyrosinase/caffeic acid-catalyzed crosslinking plus galactomannan conjugation alleviates allergic asthma

Abstract

Ovalbumin (OVA) is the primary allergenic protein, associated with T helper 2 (Th2)-mediated allergy reactions. Here, we studied OVA’s conformational structure, digestibility, and allergenic potency upon galactomannan (Man) conjugation along with transglutaminase-catalyzed crosslinking (TG-Man/OVA) and tyrosinase/caffeic acid-catalyzed crosslinking (Tyr-Man/OVA). Enzymatic glycosylation altered OVA’s conformation and enhanced the gastrointestinal digestibility. Stimulation of bone marrow-derived dendritic cells (BMDCs) with enzymatically glycosylated OVA reduced the expression of CD40, CD80, CD86 and MHC class II molecules. Furthermore, glycosylated OVA increased IL-10 production while suppressing proinflammatory cytokine production in BMDCs. In an OVA-induced mouse asthma model, TG-Man/OVA and Tyr-Man/OVA upregulated IFN-γ and IL-10 expression and downregulated IL-4, IL-5, and IL-13 in lungs. Crosslinked OVA diminished infiltrated cells in bronchoalveolar lavage fluid and lung and attenuated eosinophilic airway inflammation. These findings offer valuable insights into the development of a novel product with improved hypoallergenic and immunomodulatory properties and hold promise in attenuating allergic diseases.

Keywords

• Ovalbumin
• Enzymatic glycosylation
• Galactomannan
• Conformational structure
• Digestion stability
• Asthma