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Background: Royal jelly (RJ) is a proteinaceous secretion produced from the hypopharyngeal and mandibular glands of nurse bees.It plays vital roles in honeybee biology and in the improvement of human health.However, some proteins remain hidden in R J, and mapping N-glycosylation modification sites on RJ proteins demands further investigation.We used two different liquid chromatography tandem mass spectrometry techniques, complementary N-glycopeptide enrichment strategies, and bioinformatic approaches to gain a better understanding of novel and glycosylated proteins in RJ.Results: A total of 25 N-glycosylated proteins, carrying 53 N-glycosylation sites, were identified in RJ proteins, of which 42 N-linked glycosylation sites were mapped as novel on RJ proteins.Most of the glycosylated proteins were related to metabolic activities and health improvement.The newly identified 13 proteins were also mainly associated with metabolic processes and health improvement activities.Conclusion: Our in-depth, large-scale mapping of novel glycosylation sites represents a crucial step toward systematically revealing the functionality of N-glycosylated RJ proteins, which is potentially useful for producing a protein with desirable pharmacokinefic and biological activity using a genetic engineering approach.The newly-identified proteins significantly extend the proteome coverage of RJ.These findings contribute vital, new knowledge to our understanding of the innate biochemical nature of RJ at both the proteome and the glycoproteome levels.