Tropomyosin is the most potent
allergen of shrimp that can cause severe
food allergy. However, to date, an effective approach to eliminate this allergenicity is still lacking. Glycation is a promising approach that can reduce the allergenicity of shrimp
tropomyosin by destroying the
epitopes; however,
advanced glycation end products (AGEs) are also generated during glycation, which can function as neoallergens to strengthen the allergenicity; therefore, it is hard to tell how the glycation of an
allergen with different saccharides affects the allergenicity via
epitope loss and neoallergen generation. This study was aimed at the elucidation of how the glycation of
tropomyosin (TM) with saccharides of different molecular sizes (
glucose,
maltose, and
maltotriose) affected the allergenicity through
epitope loss and the generation of neoallergns that belonged to
advanced glycation end products (AGEs). Saccharides of higher molecular sizes (
maltotriose) could lead to higher glycated TM than saccharides of smaller molecular sizes (
glucose and
maltose). Compared with TM, the TM glycated by
glucose (TM-G) and
maltotriose (TM-MTS) had lower allergenicity and contributed to weaker mouse
allergy symptoms; on the other hand, the TM glycated by
maltose (TM-M) had no significant impact on the allergenicity due to the generation of AGE-related neoallergens, which might offset the glycation-induced
epitope loss. The glycation of TM by
maltotriose led to lower generation of AGE neoallergens (e.g. CML) than that in the cases of
glucose and
maltose; therefore,
maltotriose could be applied to desensitize TM-induced
food allergy through glycation, and this could be a potential
immunotherapy for shrimp
allergy patients.