Comprehensive Identification of Novel Proteins and N-glycosylation Sites in Royal Jelly
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.
Royal jelly N-glycosylation hydrazide chemistry lectin affinity tandem mass spectrometry
Bin Han Yu Fang Mao Feng Jianke Li
Institute of Apicultural Research, Chinese Academy of Agricultural Science, Beijing 100093, China
国内会议
第十届海峡两岸蜜蜂与蜂产品学术研讨会暨首届全国蜂产业高峰论坛
扬州
英文
321-335
2013-11-03（万方平台首次上网日期，不代表论文的发表时间）